{"gene":"KIF3B","run_date":"2026-06-10T02:59:49","timeline":{"discoveries":[{"year":1998,"finding":"KIF3B is localized to nodal monocilia and is essential for their assembly; loss of KIF3B abolishes nodal cilia while basal bodies remain present, eliminating leftward nodal fluid flow and randomizing left-right asymmetry in mice.","method":"Gene targeting (knockout mouse), immunocytochemistry for KIF3B in nodal cilia, video microscopy of cilia motility and fluid flow, lefty-2 expression analysis","journal":"Cell","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic loss-of-function with direct localization and functional readout, replicated across multiple phenotypic assays in one rigorous study","pmids":["9865700"],"is_preprint":false},{"year":2014,"finding":"The KIF3B homolog FLA8 in Chlamydomonas is phosphorylated at the conserved residue S663 by a calcium-dependent kinase; this phosphorylation disrupts the interaction between kinesin-II and the IFT-B complex, inactivates kinesin-II, blocks IFT entry into cilia, and is required for IFT-B unloading at the ciliary tip, acting as a molecular switch controlling IFT entry and turnaround.","method":"Phosphorylation site identification, site-directed mutagenesis, in vivo IFT assays, co-immunoprecipitation of kinesin-II with IFT-B, cellular fractionation","journal":"Developmental cell","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — multiple orthogonal methods including mutagenesis, co-IP, and in vivo IFT assays establishing mechanism in a single rigorous study","pmids":["25175706"],"is_preprint":false},{"year":2018,"finding":"Cellular signaling in response to changes in flagellar length regulates phosphorylation of FLA8/KIF3B: phosphorylated FLA8 levels are low in cells with short flagella and high in cells with long flagella. Depletion of phosphatases CrPP1 and CrPP6 increases pFLA8, decreasing IFT entry and flagellar length, demonstrating that KIF3B phosphorylation is the effector of a length-sensing mechanism controlling ciliary assembly.","method":"Phosphatase depletion (siRNA), quantification of pFLA8 levels vs. flagellar length, IFT entry measurements, Chlamydomonas genetics","journal":"Current biology : CB","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal approaches (genetic, biochemical, functional IFT measurements) in a single focused study building on prior mechanistic work","pmids":["30057303"],"is_preprint":false},{"year":2009,"finding":"CLC-5 (chloride/proton antiporter) physically interacts with KIF3B via the CLC-5 C-terminus and the KIF3B coiled-coil and globular domains; KIF3B transports CLC-5-containing vesicles along microtubules in kidney cells, and KIF3B knockdown decreases CLC-5 surface expression and endocytosis of albumin and transferrin while overexpression has reciprocal effects.","method":"Yeast two-hybrid, GST pull-down, co-immunoprecipitation (endogenous), confocal live-cell imaging, siRNA knockdown, whole-cell chloride current measurement, endocytosis assays","journal":"American journal of physiology. Renal physiology","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal co-IP, live imaging, siRNA functional assays, and in vivo tissue confirmation provide multiple orthogonal lines of evidence","pmids":["19940036"],"is_preprint":false},{"year":2010,"finding":"KIF3A/KIF3B kinesin drives anterograde transport of MT1-MMP-positive vesicles along microtubules in primary human macrophages; siRNA-mediated knockdown of KIF3A/KIF3B impairs MT1-MMP delivery to the cell surface, shedding of CD44 and syndecan-1, and degradation of extracellular matrix at podosomes.","method":"siRNA knockdown, live-cell imaging of vesicle movement along microtubules, surface expression assay, ECM degradation assay at podosomes","journal":"Blood","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — siRNA knockdown with multiple functional readouts in one lab, but KIF3A and KIF3B studied together without full separation of individual subunit contributions","pmids":["20505159"],"is_preprint":false},{"year":2011,"finding":"RING/TRIM protein RNF33/TRIM60 interacts with KIF3A and KIF3B through its RB and B30.2 domains binding the respective C-terminal non-motor (tail) domains of KIF3A and KIF3B; this interaction occurs independently of the KAP3 adaptor, leaving the motor head free for microtubule-based movement.","method":"Yeast two-hybrid, co-immunoprecipitation, deletion mapping","journal":"Molecular and cellular biochemistry","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — yeast two-hybrid and co-IP with domain mapping, single lab, no in vivo transport functional rescue","pmids":["21909995"],"is_preprint":false},{"year":2011,"finding":"Human kidney anion exchanger 1 (kAE1) interacts with KIF3B via a dileucine motif at the kAE1 C-terminus; KIF3B knockdown by siRNA reduces membrane localization of kAE1 and increases its intracellular accumulation, indicating KIF3B mediates kAE1 trafficking to the plasma membrane.","method":"Co-immunoprecipitation, siRNA knockdown, immunofluorescence colocalization in kidney tissue and cells","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — co-IP with domain identification and siRNA functional assay, single lab, multiple methods but limited mechanistic depth","pmids":["21871436"],"is_preprint":false},{"year":2019,"finding":"KIF3B transports vesicles simultaneously containing NMDAR subunit NR2A (GluN2A) and the APC complex in neurons; Kif3b+/- neurons show reduced dendritic levels of NR2A and NR2B (NR2B due to increased degradation), decreased NMDAR electrophysiological responses, and disrupted synaptic plasticity. A human SCZ-associated KIF3B mutation is functionally defective in a rescue experiment.","method":"Heterozygous knockout mouse, vesicle co-fractionation/co-IP of NR2A and APC with KIF3B, electrophysiology in hippocampal slices, behavioral assays, rescue experiment with human variant","journal":"The EMBO journal","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (biochemical co-transport, electrophysiology, behavioral phenotyping, human variant rescue) in one rigorous study","pmids":["31746486"],"is_preprint":false},{"year":2020,"finding":"Heterozygous human KIF3B missense variants (E250Q in the motor domain; L523P in the stalk) cause dominant ciliopathy with retinitis pigmentosa and polydactyly; mutant KIF3B proteins increase primary cilia length in vitro and impair rhodopsin trafficking in photoreceptors in zebrafish.","method":"Exome sequencing of patients, in vitro cilia length measurement, zebrafish mRNA injection and rhodopsin trafficking assay, genome-wide association study + whole-genome sequencing in Bengal cats","journal":"American journal of human genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo zebrafish model + cell-based cilia assays, single study; mechanism of length increase not fully resolved at molecular level","pmids":["32386558"],"is_preprint":false},{"year":2022,"finding":"KIF3B transports the PTEN-like phosphatase Talpid3 to terminate PI3K signaling in limb bud cells; loss of KIF3B motor activity in hypomorphic mice disrupts a distal-to-proximal FGF/PI3K gradient and a posterior-to-anterior Shh gradient, causing preaxial polydactyly. High vs. low PI3K signaling differentially sorts endocytosed Shh into exosome-like particles vs. cytonemal puncta, establishing a Shh spatial gradient.","method":"KIF3B hypomorphic mouse genetics, bead transplantation experiments, subcellular fractionation, immunofluorescence of Shh/PI3K/Talpid3 distribution","journal":"Developmental cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis with multiple cellular readouts in a single lab; Talpid3 transport is inferred from KIF3B loss-of-function rather than direct reconstitution","pmids":["36220081"],"is_preprint":false},{"year":2024,"finding":"Disease-causing KIF3B mutation E250Q (motor domain) is a rigor mutation that causes the motor to decorate microtubules and fails to rescue ciliogenesis; L523P (stalk/coiled-coil domain) does not disrupt KIF3A/KIF3B/KAP3 complex formation but impairs motility along microtubules; A334T reduces motor protein levels and impairs Golgi dispersal under high load but restores ciliogenesis to wild-type levels.","method":"Kif3a;Kif3b double-knockout 3T3 cell rescue assay, ciliogenesis quantification, fluorescent tagging/microtubule decoration assay, Golgi dispersal assay, complex formation assessment","journal":"Frontiers in molecular biosciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — cell-based rescue with multiple mutant alleles and orthogonal functional assays, single lab","pmids":["38665936"],"is_preprint":false},{"year":2020,"finding":"KIF3B knockdown in primary cortical neurons increases dendritic spine density (thin and mushroom spines), increases dendritic branching, and elevates PSD-95 distribution; KIF3B overexpression reduces spine density and branching, demonstrating that KIF3B functions as an inhibitory constraint on structural plasticity in post-mitotic neurons.","method":"RNAi knockdown and overexpression in primary cortical neurons, confocal imaging of dendritic morphology, immunostaining for PSD-95","journal":"Frontiers in cellular neuroscience","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — loss- and gain-of-function with quantitative morphological readouts, single lab, no mechanistic pathway placement beyond structural phenotype","pmids":["33192305"],"is_preprint":false},{"year":2021,"finding":"KIF3B silencing in breast cancer cells decreases the expression of Dvl2, phospho-GSK-3β, and nuclear β-catenin and downregulates Wnt/β-catenin target genes (CyclinD1, c-Myc, MMP-2, MMP-7, MMP-9), and inhibits epithelial-mesenchymal transition, placing KIF3B upstream of the Wnt/β-catenin pathway.","method":"siRNA knockdown in breast cancer cell lines, western blot for pathway components, in vivo xenograft","journal":"Frontiers in oncology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, western blot of pathway markers after knockdown without direct mechanistic link establishing how KIF3B activates Wnt/β-catenin","pmids":["33542902"],"is_preprint":false},{"year":2023,"finding":"YY1 transcriptionally activates KIF3B; KIF3B in turn interacts with Integrin-beta1 (ITGB1) to inactivate the Hippo signaling pathway (reducing YAP1 phosphorylation and nuclear exclusion), conferring radioresistance in esophageal squamous cell carcinoma cells.","method":"Multi-group sequencing, siRNA knockdown, co-immunoprecipitation of KIF3B with ITGB1, Hippo pathway component western blot, in vitro and in vivo radiosensitivity assays","journal":"Cell death & disease","confidence":"Low","confidence_rationale":"Tier 3 / Weak — co-IP and knockdown with pathway readout, single lab, limited mechanistic depth on how KIF3B-ITGB1 interaction activates Hippo","pmids":["38065955"],"is_preprint":false},{"year":2025,"finding":"High-resolution cryo-EM structures of the KIF3A/KIF3B/KAP3 heterotrimer bound to APC cargo reveal a previously uncharacterized 'Hitchdock domain' in the KIF3 tail; KIF3A helical regions mediate APC cargo binding while KIF3B provides structural support; the β-hairpin region and KAP3 interface are also defined. Mutagenesis and MD simulations confirm functional importance of the Hitchdock domain.","method":"Cryo-electron microscopy, mutagenesis, molecular dynamics simulations","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — high-resolution cryo-EM structure with mutagenesis, preprint not yet peer-reviewed","pmids":[],"is_preprint":true},{"year":2024,"finding":"A conserved beta-hairpin motif in the kinesin-2 tail (including KIF3B) mediates autoinhibition by sequestering motor domains away from microtubules via molecular mimicry. KAP3 binds via a multipartite interface with both KIF3A and KIF3B and provides a platform for cargo adaptors that occlude the beta-hairpin motif to activate motility, rather than activating motility directly.","method":"Cryo-EM structural analysis, single-molecule motility assays, cell biological assays, mutagenesis of beta-hairpin motif","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — structural plus single-molecule functional data, but preprint not yet peer-reviewed","pmids":[],"is_preprint":true},{"year":2026,"finding":"A KIF3B-enriched, KAP3-associated kinesin-2 assembly (distinct from canonical KIF3A/KIF3B/KAP3) preferentially associates with TRIM46, a protein required for axon initial segment organization, and the KIF3B tail domain facilitates this transport; structural differences in tail conformation accompany distinct assembly states and may underlie cargo selectivity.","method":"Biochemical fractionation, co-immunoprecipitation, cellular imaging, structural analysis of tail conformations","journal":"The Journal of cell biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal biochemical and structural data, single lab, peer-reviewed","pmids":["41910726"],"is_preprint":false},{"year":2025,"finding":"14-3-3ε binds to the C-terminal tail domain of KIF3B in vitro, identified as a potential adaptor for kinesin-2 cargo recognition; the binding site was mapped by acceptor photobleaching-FRET and split-APEX2 assays.","method":"In vitro binding assay, acceptor photobleaching-FRET, split-APEX2 proximity assay","journal":"bioRxiv","confidence":"Low","confidence_rationale":"Tier 3 / Weak — preprint, single lab, in vitro interaction only without functional transport validation","pmids":[],"is_preprint":true},{"year":1999,"finding":"KIF3A and KIF3B subunits of kinesin-II are concentrated in photoreceptor inner segments, the outer limiting membrane, and axonemes (connecting cilium) in Xenopus and human/monkey retina, consistent with a role in transport from cell body to outer segment.","method":"Immunoblotting, immunohistochemistry/immunofluorescence on retinal sections with subunit-specific antibodies","journal":"Experimental eye research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — localization by antibody staining without direct functional manipulation of KIF3B specifically","pmids":["10548469"],"is_preprint":false},{"year":2017,"finding":"KIF3B localizes to spindles and is enriched at the central spindle during mitosis in HeLa cells; KIF3B knockdown increases rates of multipolar division and multi-nucleation, indicating KIF3B is required for normal spindle formation and cytokinesis.","method":"siRNA knockdown, immunofluorescence during cell cycle stages, quantification of multipolar divisions and multi-nucleate cells","journal":"Experimental cell research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, morphological readout from knockdown, limited mechanistic resolution of how KIF3B contributes to spindle function","pmids":["28161539"],"is_preprint":false}],"current_model":"KIF3B functions as the motor subunit of the heterotrimeric kinesin-2 complex (KIF3A/KIF3B/KAP3), driving anterograde intraflagellar transport (IFT) essential for ciliogenesis and ciliary length control—regulated by calcium-dependent phosphorylation of S663 (FLA8/KIF3B) that disrupts IFT-B interaction and gates IFT entry; it also transports diverse cargoes including MT1-MMP vesicles, CLC-5/kAE1 to kidney membranes, NR2A/APC complexes to neuronal dendrites, and Talpid3 to terminate PI3K signaling in limb buds, with autoinhibition achieved through a conserved beta-hairpin motif in its tail that is relieved upon KAP3-mediated cargo adaptor engagement."},"narrative":{"mechanistic_narrative":"KIF3B is the motor subunit of the heterotrimeric kinesin-2 complex (KIF3A/KIF3B/KAP3) that drives microtubule-based anterograde transport underlying ciliogenesis and selective intracellular cargo delivery [PMID:9865700, PMID:25175706]. In cilia, KIF3B powers anterograde intraflagellar transport (IFT), and its loss abolishes nodal monocilia, eliminates leftward nodal flow, and randomizes left-right body asymmetry [PMID:9865700]. Entry of the motor into the cilium and turnaround at the tip are gated by calcium-dependent phosphorylation of the conserved residue S663, which disrupts the kinesin-II/IFT-B interaction and inactivates the motor; this phosphorylation is the effector of a flagellar length-sensing feedback loop, accumulating in long cilia to throttle further IFT entry [PMID:25175706, PMID:30057303]. Beyond cilia, KIF3B transports a diverse cargo repertoire along microtubules: MT1-MMP vesicles required for matrix degradation at macrophage podosomes [PMID:20505159], CLC-5 and the anion exchanger kAE1 to the kidney plasma membrane [PMID:19940036, PMID:21871436], and NR2A/APC-containing vesicles to neuronal dendrites, where KIF3B haploinsufficiency reduces NMDAR levels and synaptic plasticity and a schizophrenia-associated variant is transport-defective [PMID:31746486]. Motor activity is held in check by autoinhibition: a conserved beta-hairpin motif in the kinesin-2 tail sequesters the motor domains by molecular mimicry, and KAP3 provides a multipartite platform for cargo adaptors that occlude this motif to license motility. Heterozygous KIF3B missense variants cause a dominant ciliopathy with retinitis pigmentosa and polydactyly; mechanistically, the motor-domain E250Q behaves as a rigor mutation that decorates microtubules and fails to rescue ciliogenesis, while the stalk L523P preserves complex assembly but impairs motility [PMID:32386558, PMID:38665936]. KIF3B also delivers the Talpid3 phosphatase to terminate PI3K signaling and shape Shh gradients during limb patterning [PMID:36220081].","teleology":[{"year":1998,"claim":"Establishing that KIF3B is genetically required for cilium assembly and left-right axis specification answered whether this motor has an essential developmental function.","evidence":"Knockout mouse with cilia localization, motility/fluid-flow video microscopy, and lefty-2 expression analysis","pmids":["9865700"],"confidence":"High","gaps":["Did not resolve which cargoes or IFT machinery KIF3B carries into the cilium","Mechanism linking ciliary loss to asymmetry randomization inferred from flow defect"]},{"year":2014,"claim":"Identification of S663 phosphorylation as a switch that disrupts kinesin-II/IFT-B binding explained how IFT entry and tip turnaround are gated rather than constitutive.","evidence":"Phosphosite mapping, site-directed mutagenesis, in vivo IFT assays and co-IP in Chlamydomonas FLA8/KIF3B","pmids":["25175706"],"confidence":"High","gaps":["Kinase identity defined only as calcium-dependent","Conservation of this switch in mammalian KIF3B not directly tested"]},{"year":2018,"claim":"Linking pFLA8 levels to flagellar length defined KIF3B phosphorylation as the effector of a length-sensing feedback loop controlling ciliary assembly.","evidence":"Phosphatase (CrPP1/CrPP6) depletion with pFLA8 quantification and IFT entry measurements in Chlamydomonas","pmids":["30057303"],"confidence":"High","gaps":["How length information is converted into kinase/phosphatase activity not established","Phosphatase specificity in vivo not fully resolved"]},{"year":2009,"claim":"Demonstrating direct KIF3B–CLC-5 binding and transport extended KIF3B function beyond cilia to membrane-protein trafficking and endocytic regulation in kidney cells.","evidence":"Yeast two-hybrid, GST pull-down, reciprocal co-IP, live imaging, siRNA, endocytosis assays","pmids":["19940036"],"confidence":"High","gaps":["Requirement for full KIF3A/KAP3 complex not dissected","In vivo renal consequences not tested"]},{"year":2011,"claim":"Mapping kAE1 and RNF33/TRIM60 binding to the KIF3B tail clarified how non-ciliary cargo and regulatory proteins engage the motor's non-motor domain.","evidence":"Co-IP, yeast two-hybrid, and deletion mapping of dileucine motif (kAE1) and RB/B30.2 domains (RNF33)","pmids":["21871436","21909995"],"confidence":"Medium","gaps":["No in vivo transport rescue for either interaction","Functional role of RNF33 binding (KAP3-independent) on transport not measured"]},{"year":2010,"claim":"Showing KIF3A/KIF3B delivers MT1-MMP vesicles connected the motor to matrix degradation and surface receptor shedding in macrophages.","evidence":"siRNA knockdown, live vesicle imaging, surface expression and podosome ECM degradation assays","pmids":["20505159"],"confidence":"Medium","gaps":["KIF3A and KIF3B contributions not individually separated","Direct cargo adaptor not identified"]},{"year":2019,"claim":"Demonstrating co-transport of NR2A/APC vesicles and rescue failure of a disease variant tied KIF3B to synaptic NMDAR delivery and plasticity, with a human psychiatric link.","evidence":"Heterozygous knockout mouse, vesicle co-IP, hippocampal electrophysiology, behavior, human variant rescue","pmids":["31746486"],"confidence":"High","gaps":["Causal contribution of KIF3B variant to disease in patients not established beyond cellular rescue","Mechanism of NR2B degradation downstream of reduced transport not detailed"]},{"year":2020,"claim":"Characterizing the neuronal morphological phenotype showed KIF3B acts as a constraint on dendritic spine density and branching in post-mitotic neurons.","evidence":"RNAi knockdown and overexpression in cortical neurons with morphology and PSD-95 imaging","pmids":["33192305"],"confidence":"Medium","gaps":["Pathway connecting transport activity to spine number not defined","Relationship to NR2A transport function not integrated"]},{"year":2020,"claim":"Identifying heterozygous KIF3B missense variants causing retinitis pigmentosa and polydactyly established KIF3B as a dominant ciliopathy gene.","evidence":"Patient exome sequencing, in vitro cilia length assay, zebrafish rhodopsin trafficking, feline GWAS/WGS","pmids":["32386558"],"confidence":"Medium","gaps":["Molecular basis of cilia length increase not resolved at this stage","Dominant-negative vs haploinsufficient mechanism unclear"]},{"year":2022,"claim":"Connecting KIF3B to Talpid3 transport and PI3K termination explained how the motor shapes Shh and FGF gradients during limb patterning.","evidence":"Hypomorphic mouse genetics, bead transplantation, fractionation, immunofluorescence of Shh/PI3K/Talpid3","pmids":["36220081"],"confidence":"Medium","gaps":["Talpid3 transport inferred from loss-of-function, not reconstituted","Direct KIF3B–Talpid3 binding not shown"]},{"year":2024,"claim":"Allele-resolved rescue assays defined distinct molecular defects for disease mutations, separating rigor binding (E250Q), motility impairment (L523P), and load-dependent defects (A334T).","evidence":"Kif3a;Kif3b double-knockout 3T3 rescue, ciliogenesis, microtubule decoration, Golgi dispersal, complex formation assays","pmids":["38665936"],"confidence":"Medium","gaps":["Single lab, cell-based assays only","In vivo correspondence of each allele's defect not tested"]},{"year":2024,"claim":"Structural definition of a tail beta-hairpin autoinhibition motif and the KAP3 cargo-adaptor platform explained how kinesin-2 motility is switched on by cargo engagement.","evidence":"Cryo-EM, single-molecule motility, and beta-hairpin mutagenesis (preprint)","pmids":[],"confidence":"Medium","gaps":["Preprint, not yet peer-reviewed","Which physiological cargo adaptors occlude the motif in cells not enumerated"]},{"year":2026,"claim":"Discovery of a KIF3B-enriched, TRIM46-associated kinesin-2 assembly distinct from the canonical heterotrimer indicated assembly-state diversity may underlie cargo selectivity.","evidence":"Biochemical fractionation, co-IP, imaging, and tail conformation structural analysis","pmids":["41910726"],"confidence":"Medium","gaps":["Stoichiometry and composition of the alternative assembly not fully defined","Functional consequence for axon initial segment in vivo not established"]},{"year":null,"claim":"How distinct cargo adaptors (e.g. 14-3-3ε, KAP3-linked factors) and tail conformations are selected to direct KIF3B to specific cargoes in different cell types remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No unified model linking adaptor identity to cargo specificity","In vitro 14-3-3ε binding lacks functional transport validation"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003774","term_label":"cytoskeletal motor activity","supporting_discovery_ids":[0,1,10,15]},{"term_id":"GO:0140657","term_label":"ATP-dependent activity","supporting_discovery_ids":[1,15]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0,3,10]}],"localization":[{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[0,1,8]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[3,4,19]},{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[19]}],"pathway":[{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[3,4,6,7]},{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[3,4,7]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[0,9]},{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[0,1,2]}],"complexes":["kinesin-2 (KIF3A/KIF3B/KAP3) heterotrimer"],"partners":["KIF3A","KAP3","CLC-5","KAE1","RNF33/TRIM60","ITGB1","TRIM46","APC"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O15066","full_name":"Kinesin-like protein KIF3B","aliases":["HH0048","Microtubule plus end-directed kinesin motor 3B"],"length_aa":747,"mass_kda":85.1,"function":"Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation (PubMed:32386558). Involved in photoreceptor integrity and opsin trafficking in rod photoreceptors (PubMed:32386558). Transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit GRIN2A into neuronal dendrites (By similarity)","subcellular_location":"Cytoplasm, cytoskeleton; Cell projection, cilium; Cell projection, dendritic spine","url":"https://www.uniprot.org/uniprotkb/O15066/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/KIF3B","classification":"Not Classified","n_dependent_lines":3,"n_total_lines":1208,"dependency_fraction":0.0024834437086092716},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000101350","cell_line_id":"CID001424","localizations":[{"compartment":"cytoplasmic","grade":3},{"compartment":"centrosome","grade":2}],"interactors":[{"gene":"KIF3A","stoichiometry":10.0},{"gene":"KIFAP3","stoichiometry":10.0}],"url":"https://opencell.sf.czbiohub.org/target/CID001424","total_profiled":1310},"omim":[{"mim_id":"618955","title":"RETINITIS PIGMENTOSA 89; RP89","url":"https://www.omim.org/entry/618955"},{"mim_id":"612991","title":"ASXL TRANSCRIPTIONAL REGULATOR 2; ASXL2","url":"https://www.omim.org/entry/612991"},{"mim_id":"612990","title":"ASXL TRANSCRIPTIONAL REGULATOR 1; ASXL1","url":"https://www.omim.org/entry/612990"},{"mim_id":"607491","title":"PROTEIN O-FUCOSYLTRANSFERASE 1; POFUT1","url":"https://www.omim.org/entry/607491"},{"mim_id":"606062","title":"STRUCTURAL MAINTENANCE OF CHROMOSOMES 3; SMC3","url":"https://www.omim.org/entry/606062"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Primary cilium tip","reliability":"Approved"},{"location":"Flagellar centriole","reliability":"Approved"},{"location":"Cytosol","reliability":"Additional"},{"location":"Connecting piece","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/KIF3B"},"hgnc":{"alias_symbol":["KIAA0359","FLA8","KLP-11"],"prev_symbol":[]},"alphafold":{"accession":"O15066","domains":[{"cath_id":"3.40.850.10","chopping":"13-341","consensus_level":"medium","plddt":87.4419,"start":13,"end":341},{"cath_id":"-","chopping":"353-380_412-475","consensus_level":"medium","plddt":75.9233,"start":353,"end":475}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O15066","model_url":"https://alphafold.ebi.ac.uk/files/AF-O15066-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O15066-F1-predicted_aligned_error_v6.png","plddt_mean":76.5},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=KIF3B","jax_strain_url":"https://www.jax.org/strain/search?query=KIF3B"},"sequence":{"accession":"O15066","fasta_url":"https://rest.uniprot.org/uniprotkb/O15066.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O15066/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O15066"}},"corpus_meta":[{"pmid":"9865700","id":"PMC_9865700","title":"Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein.","date":"1998","source":"Cell","url":"https://pubmed.ncbi.nlm.nih.gov/9865700","citation_count":1243,"is_preprint":false},{"pmid":"20505159","id":"PMC_20505159","title":"KIF5B and KIF3A/KIF3B kinesins drive MT1-MMP surface exposure, CD44 shedding, and extracellular matrix degradation in primary macrophages.","date":"2010","source":"Blood","url":"https://pubmed.ncbi.nlm.nih.gov/20505159","citation_count":116,"is_preprint":false},{"pmid":"25175706","id":"PMC_25175706","title":"FLA8/KIF3B phosphorylation regulates kinesin-II interaction with IFT-B to control IFT entry and turnaround.","date":"2014","source":"Developmental cell","url":"https://pubmed.ncbi.nlm.nih.gov/25175706","citation_count":91,"is_preprint":false},{"pmid":"19940036","id":"PMC_19940036","title":"CLC-5 and KIF3B interact to facilitate CLC-5 plasma membrane expression, endocytosis, and microtubular transport: relevance to pathophysiology of Dent's disease.","date":"2009","source":"American journal of physiology. 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cilia, video microscopy of cilia motility and fluid flow, lefty-2 expression analysis\",\n      \"journal\": \"Cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic loss-of-function with direct localization and functional readout, replicated across multiple phenotypic assays in one rigorous study\",\n      \"pmids\": [\"9865700\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"The KIF3B homolog FLA8 in Chlamydomonas is phosphorylated at the conserved residue S663 by a calcium-dependent kinase; this phosphorylation disrupts the interaction between kinesin-II and the IFT-B complex, inactivates kinesin-II, blocks IFT entry into cilia, and is required for IFT-B unloading at the ciliary tip, acting as a molecular switch controlling IFT entry and turnaround.\",\n      \"method\": \"Phosphorylation site identification, site-directed mutagenesis, in vivo IFT assays, co-immunoprecipitation of kinesin-II with IFT-B, cellular fractionation\",\n      \"journal\": \"Developmental cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — multiple orthogonal methods including mutagenesis, co-IP, and in vivo IFT assays establishing mechanism in a single rigorous study\",\n      \"pmids\": [\"25175706\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Cellular signaling in response to changes in flagellar length regulates phosphorylation of FLA8/KIF3B: phosphorylated FLA8 levels are low in cells with short flagella and high in cells with long flagella. Depletion of phosphatases CrPP1 and CrPP6 increases pFLA8, decreasing IFT entry and flagellar length, demonstrating that KIF3B phosphorylation is the effector of a length-sensing mechanism controlling ciliary assembly.\",\n      \"method\": \"Phosphatase depletion (siRNA), quantification of pFLA8 levels vs. flagellar length, IFT entry measurements, Chlamydomonas genetics\",\n      \"journal\": \"Current biology : CB\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal approaches (genetic, biochemical, functional IFT measurements) in a single focused study building on prior mechanistic work\",\n      \"pmids\": [\"30057303\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"CLC-5 (chloride/proton antiporter) physically interacts with KIF3B via the CLC-5 C-terminus and the KIF3B coiled-coil and globular domains; KIF3B transports CLC-5-containing vesicles along microtubules in kidney cells, and KIF3B knockdown decreases CLC-5 surface expression and endocytosis of albumin and transferrin while overexpression has reciprocal effects.\",\n      \"method\": \"Yeast two-hybrid, GST pull-down, co-immunoprecipitation (endogenous), confocal live-cell imaging, siRNA knockdown, whole-cell chloride current measurement, endocytosis assays\",\n      \"journal\": \"American journal of physiology. Renal physiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal co-IP, live imaging, siRNA functional assays, and in vivo tissue confirmation provide multiple orthogonal lines of evidence\",\n      \"pmids\": [\"19940036\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"KIF3A/KIF3B kinesin drives anterograde transport of MT1-MMP-positive vesicles along microtubules in primary human macrophages; siRNA-mediated knockdown of KIF3A/KIF3B impairs MT1-MMP delivery to the cell surface, shedding of CD44 and syndecan-1, and degradation of extracellular matrix at podosomes.\",\n      \"method\": \"siRNA knockdown, live-cell imaging of vesicle movement along microtubules, surface expression assay, ECM degradation assay at podosomes\",\n      \"journal\": \"Blood\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — siRNA knockdown with multiple functional readouts in one lab, but KIF3A and KIF3B studied together without full separation of individual subunit contributions\",\n      \"pmids\": [\"20505159\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"RING/TRIM protein RNF33/TRIM60 interacts with KIF3A and KIF3B through its RB and B30.2 domains binding the respective C-terminal non-motor (tail) domains of KIF3A and KIF3B; this interaction occurs independently of the KAP3 adaptor, leaving the motor head free for microtubule-based movement.\",\n      \"method\": \"Yeast two-hybrid, co-immunoprecipitation, deletion mapping\",\n      \"journal\": \"Molecular and cellular biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — yeast two-hybrid and co-IP with domain mapping, single lab, no in vivo transport functional rescue\",\n      \"pmids\": [\"21909995\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"Human kidney anion exchanger 1 (kAE1) interacts with KIF3B via a dileucine motif at the kAE1 C-terminus; KIF3B knockdown by siRNA reduces membrane localization of kAE1 and increases its intracellular accumulation, indicating KIF3B mediates kAE1 trafficking to the plasma membrane.\",\n      \"method\": \"Co-immunoprecipitation, siRNA knockdown, immunofluorescence colocalization in kidney tissue and cells\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — co-IP with domain identification and siRNA functional assay, single lab, multiple methods but limited mechanistic depth\",\n      \"pmids\": [\"21871436\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"KIF3B transports vesicles simultaneously containing NMDAR subunit NR2A (GluN2A) and the APC complex in neurons; Kif3b+/- neurons show reduced dendritic levels of NR2A and NR2B (NR2B due to increased degradation), decreased NMDAR electrophysiological responses, and disrupted synaptic plasticity. A human SCZ-associated KIF3B mutation is functionally defective in a rescue experiment.\",\n      \"method\": \"Heterozygous knockout mouse, vesicle co-fractionation/co-IP of NR2A and APC with KIF3B, electrophysiology in hippocampal slices, behavioral assays, rescue experiment with human variant\",\n      \"journal\": \"The EMBO journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (biochemical co-transport, electrophysiology, behavioral phenotyping, human variant rescue) in one rigorous study\",\n      \"pmids\": [\"31746486\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Heterozygous human KIF3B missense variants (E250Q in the motor domain; L523P in the stalk) cause dominant ciliopathy with retinitis pigmentosa and polydactyly; mutant KIF3B proteins increase primary cilia length in vitro and impair rhodopsin trafficking in photoreceptors in zebrafish.\",\n      \"method\": \"Exome sequencing of patients, in vitro cilia length measurement, zebrafish mRNA injection and rhodopsin trafficking assay, genome-wide association study + whole-genome sequencing in Bengal cats\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo zebrafish model + cell-based cilia assays, single study; mechanism of length increase not fully resolved at molecular level\",\n      \"pmids\": [\"32386558\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"KIF3B transports the PTEN-like phosphatase Talpid3 to terminate PI3K signaling in limb bud cells; loss of KIF3B motor activity in hypomorphic mice disrupts a distal-to-proximal FGF/PI3K gradient and a posterior-to-anterior Shh gradient, causing preaxial polydactyly. High vs. low PI3K signaling differentially sorts endocytosed Shh into exosome-like particles vs. cytonemal puncta, establishing a Shh spatial gradient.\",\n      \"method\": \"KIF3B hypomorphic mouse genetics, bead transplantation experiments, subcellular fractionation, immunofluorescence of Shh/PI3K/Talpid3 distribution\",\n      \"journal\": \"Developmental cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis with multiple cellular readouts in a single lab; Talpid3 transport is inferred from KIF3B loss-of-function rather than direct reconstitution\",\n      \"pmids\": [\"36220081\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Disease-causing KIF3B mutation E250Q (motor domain) is a rigor mutation that causes the motor to decorate microtubules and fails to rescue ciliogenesis; L523P (stalk/coiled-coil domain) does not disrupt KIF3A/KIF3B/KAP3 complex formation but impairs motility along microtubules; A334T reduces motor protein levels and impairs Golgi dispersal under high load but restores ciliogenesis to wild-type levels.\",\n      \"method\": \"Kif3a;Kif3b double-knockout 3T3 cell rescue assay, ciliogenesis quantification, fluorescent tagging/microtubule decoration assay, Golgi dispersal assay, complex formation assessment\",\n      \"journal\": \"Frontiers in molecular biosciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — cell-based rescue with multiple mutant alleles and orthogonal functional assays, single lab\",\n      \"pmids\": [\"38665936\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"KIF3B knockdown in primary cortical neurons increases dendritic spine density (thin and mushroom spines), increases dendritic branching, and elevates PSD-95 distribution; KIF3B overexpression reduces spine density and branching, demonstrating that KIF3B functions as an inhibitory constraint on structural plasticity in post-mitotic neurons.\",\n      \"method\": \"RNAi knockdown and overexpression in primary cortical neurons, confocal imaging of dendritic morphology, immunostaining for PSD-95\",\n      \"journal\": \"Frontiers in cellular neuroscience\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — loss- and gain-of-function with quantitative morphological readouts, single lab, no mechanistic pathway placement beyond structural phenotype\",\n      \"pmids\": [\"33192305\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"KIF3B silencing in breast cancer cells decreases the expression of Dvl2, phospho-GSK-3β, and nuclear β-catenin and downregulates Wnt/β-catenin target genes (CyclinD1, c-Myc, MMP-2, MMP-7, MMP-9), and inhibits epithelial-mesenchymal transition, placing KIF3B upstream of the Wnt/β-catenin pathway.\",\n      \"method\": \"siRNA knockdown in breast cancer cell lines, western blot for pathway components, in vivo xenograft\",\n      \"journal\": \"Frontiers in oncology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, western blot of pathway markers after knockdown without direct mechanistic link establishing how KIF3B activates Wnt/β-catenin\",\n      \"pmids\": [\"33542902\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"YY1 transcriptionally activates KIF3B; KIF3B in turn interacts with Integrin-beta1 (ITGB1) to inactivate the Hippo signaling pathway (reducing YAP1 phosphorylation and nuclear exclusion), conferring radioresistance in esophageal squamous cell carcinoma cells.\",\n      \"method\": \"Multi-group sequencing, siRNA knockdown, co-immunoprecipitation of KIF3B with ITGB1, Hippo pathway component western blot, in vitro and in vivo radiosensitivity assays\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — co-IP and knockdown with pathway readout, single lab, limited mechanistic depth on how KIF3B-ITGB1 interaction activates Hippo\",\n      \"pmids\": [\"38065955\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"High-resolution cryo-EM structures of the KIF3A/KIF3B/KAP3 heterotrimer bound to APC cargo reveal a previously uncharacterized 'Hitchdock domain' in the KIF3 tail; KIF3A helical regions mediate APC cargo binding while KIF3B provides structural support; the β-hairpin region and KAP3 interface are also defined. Mutagenesis and MD simulations confirm functional importance of the Hitchdock domain.\",\n      \"method\": \"Cryo-electron microscopy, mutagenesis, molecular dynamics simulations\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — high-resolution cryo-EM structure with mutagenesis, preprint not yet peer-reviewed\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"A conserved beta-hairpin motif in the kinesin-2 tail (including KIF3B) mediates autoinhibition by sequestering motor domains away from microtubules via molecular mimicry. KAP3 binds via a multipartite interface with both KIF3A and KIF3B and provides a platform for cargo adaptors that occlude the beta-hairpin motif to activate motility, rather than activating motility directly.\",\n      \"method\": \"Cryo-EM structural analysis, single-molecule motility assays, cell biological assays, mutagenesis of beta-hairpin motif\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — structural plus single-molecule functional data, but preprint not yet peer-reviewed\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"A KIF3B-enriched, KAP3-associated kinesin-2 assembly (distinct from canonical KIF3A/KIF3B/KAP3) preferentially associates with TRIM46, a protein required for axon initial segment organization, and the KIF3B tail domain facilitates this transport; structural differences in tail conformation accompany distinct assembly states and may underlie cargo selectivity.\",\n      \"method\": \"Biochemical fractionation, co-immunoprecipitation, cellular imaging, structural analysis of tail conformations\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal biochemical and structural data, single lab, peer-reviewed\",\n      \"pmids\": [\"41910726\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"14-3-3ε binds to the C-terminal tail domain of KIF3B in vitro, identified as a potential adaptor for kinesin-2 cargo recognition; the binding site was mapped by acceptor photobleaching-FRET and split-APEX2 assays.\",\n      \"method\": \"In vitro binding assay, acceptor photobleaching-FRET, split-APEX2 proximity assay\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — preprint, single lab, in vitro interaction only without functional transport validation\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 1999,\n      \"finding\": \"KIF3A and KIF3B subunits of kinesin-II are concentrated in photoreceptor inner segments, the outer limiting membrane, and axonemes (connecting cilium) in Xenopus and human/monkey retina, consistent with a role in transport from cell body to outer segment.\",\n      \"method\": \"Immunoblotting, immunohistochemistry/immunofluorescence on retinal sections with subunit-specific antibodies\",\n      \"journal\": \"Experimental eye research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — localization by antibody staining without direct functional manipulation of KIF3B specifically\",\n      \"pmids\": [\"10548469\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"KIF3B localizes to spindles and is enriched at the central spindle during mitosis in HeLa cells; KIF3B knockdown increases rates of multipolar division and multi-nucleation, indicating KIF3B is required for normal spindle formation and cytokinesis.\",\n      \"method\": \"siRNA knockdown, immunofluorescence during cell cycle stages, quantification of multipolar divisions and multi-nucleate cells\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, morphological readout from knockdown, limited mechanistic resolution of how KIF3B contributes to spindle function\",\n      \"pmids\": [\"28161539\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"KIF3B functions as the motor subunit of the heterotrimeric kinesin-2 complex (KIF3A/KIF3B/KAP3), driving anterograde intraflagellar transport (IFT) essential for ciliogenesis and ciliary length control—regulated by calcium-dependent phosphorylation of S663 (FLA8/KIF3B) that disrupts IFT-B interaction and gates IFT entry; it also transports diverse cargoes including MT1-MMP vesicles, CLC-5/kAE1 to kidney membranes, NR2A/APC complexes to neuronal dendrites, and Talpid3 to terminate PI3K signaling in limb buds, with autoinhibition achieved through a conserved beta-hairpin motif in its tail that is relieved upon KAP3-mediated cargo adaptor engagement.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"KIF3B is the motor subunit of the heterotrimeric kinesin-2 complex (KIF3A/KIF3B/KAP3) that drives microtubule-based anterograde transport underlying ciliogenesis and selective intracellular cargo delivery [#0, #1]. In cilia, KIF3B powers anterograde intraflagellar transport (IFT), and its loss abolishes nodal monocilia, eliminates leftward nodal flow, and randomizes left-right body asymmetry [#0]. Entry of the motor into the cilium and turnaround at the tip are gated by calcium-dependent phosphorylation of the conserved residue S663, which disrupts the kinesin-II/IFT-B interaction and inactivates the motor; this phosphorylation is the effector of a flagellar length-sensing feedback loop, accumulating in long cilia to throttle further IFT entry [#1, #2]. Beyond cilia, KIF3B transports a diverse cargo repertoire along microtubules: MT1-MMP vesicles required for matrix degradation at macrophage podosomes [#4], CLC-5 and the anion exchanger kAE1 to the kidney plasma membrane [#3, #6], and NR2A/APC-containing vesicles to neuronal dendrites, where KIF3B haploinsufficiency reduces NMDAR levels and synaptic plasticity and a schizophrenia-associated variant is transport-defective [#7]. Motor activity is held in check by autoinhibition: a conserved beta-hairpin motif in the kinesin-2 tail sequesters the motor domains by molecular mimicry, and KAP3 provides a multipartite platform for cargo adaptors that occlude this motif to license motility [#15]. Heterozygous KIF3B missense variants cause a dominant ciliopathy with retinitis pigmentosa and polydactyly; mechanistically, the motor-domain E250Q behaves as a rigor mutation that decorates microtubules and fails to rescue ciliogenesis, while the stalk L523P preserves complex assembly but impairs motility [#8, #10]. KIF3B also delivers the Talpid3 phosphatase to terminate PI3K signaling and shape Shh gradients during limb patterning [#9].\",\n  \"teleology\": [\n    {\n      \"year\": 1998,\n      \"claim\": \"Establishing that KIF3B is genetically required for cilium assembly and left-right axis specification answered whether this motor has an essential developmental function.\",\n      \"evidence\": \"Knockout mouse with cilia localization, motility/fluid-flow video microscopy, and lefty-2 expression analysis\",\n      \"pmids\": [\"9865700\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not resolve which cargoes or IFT machinery KIF3B carries into the cilium\", \"Mechanism linking ciliary loss to asymmetry randomization inferred from flow defect\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Identification of S663 phosphorylation as a switch that disrupts kinesin-II/IFT-B binding explained how IFT entry and tip turnaround are gated rather than constitutive.\",\n      \"evidence\": \"Phosphosite mapping, site-directed mutagenesis, in vivo IFT assays and co-IP in Chlamydomonas FLA8/KIF3B\",\n      \"pmids\": [\"25175706\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Kinase identity defined only as calcium-dependent\", \"Conservation of this switch in mammalian KIF3B not directly tested\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Linking pFLA8 levels to flagellar length defined KIF3B phosphorylation as the effector of a length-sensing feedback loop controlling ciliary assembly.\",\n      \"evidence\": \"Phosphatase (CrPP1/CrPP6) depletion with pFLA8 quantification and IFT entry measurements in Chlamydomonas\",\n      \"pmids\": [\"30057303\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How length information is converted into kinase/phosphatase activity not established\", \"Phosphatase specificity in vivo not fully resolved\"]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Demonstrating direct KIF3B–CLC-5 binding and transport extended KIF3B function beyond cilia to membrane-protein trafficking and endocytic regulation in kidney cells.\",\n      \"evidence\": \"Yeast two-hybrid, GST pull-down, reciprocal co-IP, live imaging, siRNA, endocytosis assays\",\n      \"pmids\": [\"19940036\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Requirement for full KIF3A/KAP3 complex not dissected\", \"In vivo renal consequences not tested\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Mapping kAE1 and RNF33/TRIM60 binding to the KIF3B tail clarified how non-ciliary cargo and regulatory proteins engage the motor's non-motor domain.\",\n      \"evidence\": \"Co-IP, yeast two-hybrid, and deletion mapping of dileucine motif (kAE1) and RB/B30.2 domains (RNF33)\",\n      \"pmids\": [\"21871436\", \"21909995\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No in vivo transport rescue for either interaction\", \"Functional role of RNF33 binding (KAP3-independent) on transport not measured\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Showing KIF3A/KIF3B delivers MT1-MMP vesicles connected the motor to matrix degradation and surface receptor shedding in macrophages.\",\n      \"evidence\": \"siRNA knockdown, live vesicle imaging, surface expression and podosome ECM degradation assays\",\n      \"pmids\": [\"20505159\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"KIF3A and KIF3B contributions not individually separated\", \"Direct cargo adaptor not identified\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Demonstrating co-transport of NR2A/APC vesicles and rescue failure of a disease variant tied KIF3B to synaptic NMDAR delivery and plasticity, with a human psychiatric link.\",\n      \"evidence\": \"Heterozygous knockout mouse, vesicle co-IP, hippocampal electrophysiology, behavior, human variant rescue\",\n      \"pmids\": [\"31746486\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Causal contribution of KIF3B variant to disease in patients not established beyond cellular rescue\", \"Mechanism of NR2B degradation downstream of reduced transport not detailed\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Characterizing the neuronal morphological phenotype showed KIF3B acts as a constraint on dendritic spine density and branching in post-mitotic neurons.\",\n      \"evidence\": \"RNAi knockdown and overexpression in cortical neurons with morphology and PSD-95 imaging\",\n      \"pmids\": [\"33192305\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Pathway connecting transport activity to spine number not defined\", \"Relationship to NR2A transport function not integrated\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Identifying heterozygous KIF3B missense variants causing retinitis pigmentosa and polydactyly established KIF3B as a dominant ciliopathy gene.\",\n      \"evidence\": \"Patient exome sequencing, in vitro cilia length assay, zebrafish rhodopsin trafficking, feline GWAS/WGS\",\n      \"pmids\": [\"32386558\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular basis of cilia length increase not resolved at this stage\", \"Dominant-negative vs haploinsufficient mechanism unclear\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Connecting KIF3B to Talpid3 transport and PI3K termination explained how the motor shapes Shh and FGF gradients during limb patterning.\",\n      \"evidence\": \"Hypomorphic mouse genetics, bead transplantation, fractionation, immunofluorescence of Shh/PI3K/Talpid3\",\n      \"pmids\": [\"36220081\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Talpid3 transport inferred from loss-of-function, not reconstituted\", \"Direct KIF3B–Talpid3 binding not shown\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Allele-resolved rescue assays defined distinct molecular defects for disease mutations, separating rigor binding (E250Q), motility impairment (L523P), and load-dependent defects (A334T).\",\n      \"evidence\": \"Kif3a;Kif3b double-knockout 3T3 rescue, ciliogenesis, microtubule decoration, Golgi dispersal, complex formation assays\",\n      \"pmids\": [\"38665936\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab, cell-based assays only\", \"In vivo correspondence of each allele's defect not tested\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Structural definition of a tail beta-hairpin autoinhibition motif and the KAP3 cargo-adaptor platform explained how kinesin-2 motility is switched on by cargo engagement.\",\n      \"evidence\": \"Cryo-EM, single-molecule motility, and beta-hairpin mutagenesis (preprint)\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Preprint, not yet peer-reviewed\", \"Which physiological cargo adaptors occlude the motif in cells not enumerated\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Discovery of a KIF3B-enriched, TRIM46-associated kinesin-2 assembly distinct from the canonical heterotrimer indicated assembly-state diversity may underlie cargo selectivity.\",\n      \"evidence\": \"Biochemical fractionation, co-IP, imaging, and tail conformation structural analysis\",\n      \"pmids\": [\"41910726\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Stoichiometry and composition of the alternative assembly not fully defined\", \"Functional consequence for axon initial segment in vivo not established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How distinct cargo adaptors (e.g. 14-3-3ε, KAP3-linked factors) and tail conformations are selected to direct KIF3B to specific cargoes in different cell types remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No unified model linking adaptor identity to cargo specificity\", \"In vitro 14-3-3ε binding lacks functional transport validation\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003774\", \"supporting_discovery_ids\": [0, 1, 10, 15]},\n      {\"term_id\": \"GO:0140657\", \"supporting_discovery_ids\": [1, 15]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0, 3, 10]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [0, 1, 8]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [3, 4, 19]},\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [19]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [3, 4, 6, 7]},\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [3, 4, 7]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [0, 9]},\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"complexes\": [\"kinesin-2 (KIF3A/KIF3B/KAP3) heterotrimer\"],\n    \"partners\": [\"KIF3A\", \"KAP3\", \"CLC-5\", \"kAE1\", \"RNF33/TRIM60\", \"ITGB1\", \"TRIM46\", \"APC\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}