| 1998 |
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. |
Gene targeting (knockout mouse), immunocytochemistry for KIF3B in nodal cilia, video microscopy of cilia motility and fluid flow, lefty-2 expression analysis |
Cell |
High |
9865700
|
| 2014 |
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. |
Phosphorylation site identification, site-directed mutagenesis, in vivo IFT assays, co-immunoprecipitation of kinesin-II with IFT-B, cellular fractionation |
Developmental cell |
High |
25175706
|
| 2018 |
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. |
Phosphatase depletion (siRNA), quantification of pFLA8 levels vs. flagellar length, IFT entry measurements, Chlamydomonas genetics |
Current biology : CB |
High |
30057303
|
| 2009 |
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. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation (endogenous), confocal live-cell imaging, siRNA knockdown, whole-cell chloride current measurement, endocytosis assays |
American journal of physiology. Renal physiology |
High |
19940036
|
| 2010 |
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. |
siRNA knockdown, live-cell imaging of vesicle movement along microtubules, surface expression assay, ECM degradation assay at podosomes |
Blood |
Medium |
20505159
|
| 2011 |
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. |
Yeast two-hybrid, co-immunoprecipitation, deletion mapping |
Molecular and cellular biochemistry |
Medium |
21909995
|
| 2011 |
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. |
Co-immunoprecipitation, siRNA knockdown, immunofluorescence colocalization in kidney tissue and cells |
Biochemical and biophysical research communications |
Medium |
21871436
|
| 2019 |
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. |
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 |
The EMBO journal |
High |
31746486
|
| 2020 |
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. |
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 |
American journal of human genetics |
Medium |
32386558
|
| 2022 |
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. |
KIF3B hypomorphic mouse genetics, bead transplantation experiments, subcellular fractionation, immunofluorescence of Shh/PI3K/Talpid3 distribution |
Developmental cell |
Medium |
36220081
|
| 2024 |
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. |
Kif3a;Kif3b double-knockout 3T3 cell rescue assay, ciliogenesis quantification, fluorescent tagging/microtubule decoration assay, Golgi dispersal assay, complex formation assessment |
Frontiers in molecular biosciences |
Medium |
38665936
|
| 2020 |
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. |
RNAi knockdown and overexpression in primary cortical neurons, confocal imaging of dendritic morphology, immunostaining for PSD-95 |
Frontiers in cellular neuroscience |
Medium |
33192305
|
| 2021 |
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. |
siRNA knockdown in breast cancer cell lines, western blot for pathway components, in vivo xenograft |
Frontiers in oncology |
Low |
33542902
|
| 2023 |
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. |
Multi-group sequencing, siRNA knockdown, co-immunoprecipitation of KIF3B with ITGB1, Hippo pathway component western blot, in vitro and in vivo radiosensitivity assays |
Cell death & disease |
Low |
38065955
|
| 2025 |
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. |
Cryo-electron microscopy, mutagenesis, molecular dynamics simulations |
bioRxivpreprint |
Medium |
|
| 2024 |
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. |
Cryo-EM structural analysis, single-molecule motility assays, cell biological assays, mutagenesis of beta-hairpin motif |
bioRxivpreprint |
Medium |
|
| 2026 |
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. |
Biochemical fractionation, co-immunoprecipitation, cellular imaging, structural analysis of tail conformations |
The Journal of cell biology |
Medium |
41910726
|
| 2025 |
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. |
In vitro binding assay, acceptor photobleaching-FRET, split-APEX2 proximity assay |
bioRxivpreprint |
Low |
|
| 1999 |
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. |
Immunoblotting, immunohistochemistry/immunofluorescence on retinal sections with subunit-specific antibodies |
Experimental eye research |
Low |
10548469
|
| 2017 |
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. |
siRNA knockdown, immunofluorescence during cell cycle stages, quantification of multipolar divisions and multi-nucleate cells |
Experimental cell research |
Low |
28161539
|