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Showing RAB3IP — RABIN8 is a alias.

RAB3IP

Rab-3A-interacting protein · UniProt Q96QF0

Length
476 aa
Mass
53.0 kDa
Annotated
2026-06-10
23 papers in source corpus 17 papers cited in narrative 17 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RAB3IP (Rabin8) is a guanine nucleotide exchange factor (GEF) that activates the Rab8 GTPase to drive polarized membrane transport, with a central role in ciliary membrane assembly (PMID:16473595, PMID:21273506, PMID:24072714). Originally identified through its specific interaction with the Rab3A effector domain (PMID:7532276), its catalytic specificity was resolved as a Rab8-selective GEF, and structural snapshots of the Rab8 exchange reaction captured the ternary GDP, nucleotide-free, and GTP product complexes that define its catalytic cycle (PMID:16473595, PMID:24072714). During ciliogenesis, Rabin8 is recruited to preciliary membranes via GTP-Rab11 binding to its C-terminal region and the TRAPPII complex binding to its N-terminal domain, where it nucleates a Rab11-to-Rab8 cascade for ciliary membrane formation (PMID:21273506). NDR2 kinase phosphorylates Rabin8 at Ser-272, switching its binding preference from pericentrosomal phosphatidylserine to the exocyst component Sec15, thereby coupling vesicle docking to local Rab8 activation (PMID:23435566); in photoreceptors this same phosphorylation governs Rabin8 integration into rhodopsin transport carriers and Rab11-to-Rab8 succession during Golgi-to-cilia trafficking (PMID:39774853). Centrosomal recruitment is organized by dedicated tethering and scaffolding factors: the TRAPPII subunit TRAPPC14 links Rabin8 to the mother centriole distal appendages (PMID:31467083), CENTLEIN binds the GEF domain to prevent pericentrosomal Rabin8 accumulation (PMID:37475549), and the ASAP1–Rab11a–FIP3 complex shapes the binding pocket that assembles the Rab11–Rabin8–Rab8 cascade for ciliary receptor trafficking (PMID:25673879). Beyond ciliogenesis, Rabin8 functions as an NDR1/2 substrate in dendritic spine development (PMID:22445341), suppresses starvation-induced autophagosome formation independently of its GEF activity through its C-terminal region and Ser-272 phosphorylation (PMID:25787272), and activates Rab8 to drive LFA1 vesicle transport and avidity modulation in lymphocytes (PMID:39170909).

Mechanistic history

Synthesis pass · year-by-year structured walk · 17 steps
  1. 1995 Medium

    Established RAB3IP as a Rab-interacting protein by identifying its specific association with the Rab3A effector domain and its Sec2p-like sequence, raising but not resolving the question of GEF activity.

    Evidence Yeast two-hybrid, GST pulldown, in vitro GTPase/exchange assays, and effector-domain point mutagenesis of Rab3A

    PMID:7532276

    Open questions at the time
    • No detectable in vitro exchange or GAP activity toward Rab3A
    • True physiological GTPase target unresolved at this stage
  2. 2002 Medium

    Identified an interaction with the cancer-associated SSX2 protein that drives nuclear relocalization of cytoplasmic RAB3IP, hinting at regulated subcellular partitioning.

    Evidence Yeast two-hybrid, GST pulldown, and immunofluorescence co-localization in transfected cells

    PMID:12007189

    Open questions at the time
    • Functional consequence of nuclear relocalization unknown
    • Connection to GEF function not established
  3. 2005 Medium

    Resolved the catalytic specificity question by defining Rabin8 as a GEF selective for Rab8 (not Rab3A or Rab5), linking it to polarized membrane transport.

    Evidence In vitro nucleotide exchange assays, live-cell imaging, and dominant-negative Rab8 co-expression

    PMID:16473595

    Open questions at the time
    • Upstream recruitment mechanism unaddressed
    • Physiological process driven by Rab8 activation not yet defined
  4. 2011 High

    Placed Rabin8 at the heart of ciliogenesis by showing GTP-Rab11 and the TRAPPII complex recruit it to the centrosome to activate Rab8 for ciliary membrane formation.

    Evidence Live imaging, TAP-MS, co-IP, zebrafish epistasis, and dominant-negative/knockdown experiments

    PMID:21273506

    Open questions at the time
    • Molecular trigger linking serum withdrawal to Rabin8 relocalization not detailed
    • Regulation of the Rab11-to-Rab8 handoff unresolved at this stage
  5. 2011 Low

    Suggested a Rab8-independent signaling role by linking Rabin8 to negative regulation of mTORC1 via Rheb.

    Evidence Co-immunoprecipitation, siRNA knockdown, and Western blotting for phospho-S6

    PMID:22649696

    Open questions at the time
    • Single co-IP with overexpression/knockdown; directness of Rheb interaction not established
    • No mechanistic follow-up on how Rabin8 affects mTORC1
  6. 2012 High

    Connected Rabin8 to neuronal morphogenesis by identifying it as an NDR1/2 kinase substrate controlling dendritic spine development.

    Evidence Chemical-genetic substrate identification (analog-sensitive NDR1/2), mass spectrometry, knockdown, and in vivo neuron imaging

    PMID:22445341

    Open questions at the time
    • Phospho-site and downstream effector mechanism in spines not defined here
    • Quantitative contribution of Rab8 GEF activity to spine phenotype unclear
  7. 2013 High

    Defined the molecular switch of ciliogenesis: NDR2 phosphorylation at Ser-272 converts Rabin8 binding from phosphatidylserine to the exocyst subunit Sec15 to promote local Rab8 activation.

    Evidence In vitro kinase assays, phospho-mimetic/non-phosphorylatable mutants, lipid and protein binding assays, and ciliogenesis readouts

    PMID:23435566

    Open questions at the time
    • Spatial/temporal control of NDR2 activation at the centrosome unresolved
    • How the PS-to-Sec15 switch couples to exocyst tethering mechanistically not fully detailed
  8. 2013 High

    Provided the structural and enzymatic basis of Rabin8 catalysis by capturing the full Rab8 nucleotide-exchange cycle.

    Evidence Crystal structure snapshots and in vitro enzymatic characterization of nucleotide exchange

    PMID:24072714

    Open questions at the time
    • Structures do not capture regulatory phosphorylation or partner-bound states
    • Allosteric regulation by upstream factors not addressed structurally
  9. 2015 Medium

    Revealed a GEF-independent function: Rabin8 suppresses autophagosome formation through its C-terminal region and Ser-272 phosphorylation, separable from Rab8 activation.

    Evidence siRNA knockdown, GEF-dead and non-phosphorylatable mutant rescue, autophagosome quantification by microscopy and Western blot

    PMID:25787272

    Open questions at the time
    • Direct effector of the C-terminal suppressive function not identified
    • Single lab; mechanism linking Ser-272 to autophagy machinery undefined
  10. 2015 Medium

    Defined how the Rab11-Rabin8-Rab8 cascade is assembled for ciliary receptor trafficking via the ASAP1-Rab11a-FIP3 targeting complex.

    Evidence Co-immunoprecipitation, FIP3 ablation with rhodopsin mislocalization readout, and epistasis in photoreceptors

    PMID:25673879

    Open questions at the time
    • Stoichiometry and dynamics of the targeting complex not resolved
    • Single lab
  11. 2019 High

    Identified TRAPPC14 as the TRAPPII subunit that directly binds Rabin8 and tethers it to mother-centriole distal appendages via FBF1/CEP83.

    Evidence MS interactome, co-sedimentation, direct binding assays, siRNA knockdown with localization/ciliogenesis readouts, and zebrafish validation

    PMID:31467083

    Open questions at the time
    • How TRAPPII tethering is temporally coordinated with NDR2 phosphorylation unresolved
    • Vesicle docking mechanism at distal appendages not fully reconstituted
  12. 2019 Medium

    Revealed a negative regulatory layer in which PINK1-driven Rab8a Ser111 phosphorylation disrupts the Rab8a-Rabin8 salt bridge and impairs nucleotide exchange.

    Evidence Molecular dynamics, free-energy calculations, and in vitro nucleotide exchange assays with Rab8a mutants

    PMID:31361120

    Open questions at the time
    • Cellular context where pSer111 antagonizes Rabin8 not established experimentally
    • Single lab; limited experimental replication beyond in vitro assay
  13. 2020 Medium

    Extended Rabin8 function to growth-factor secretion, showing the RABN-8/RAB-8 axis is required for EGFR-driven vulval tumor formation via EGL-17/FGF secretion in C. elegans.

    Evidence RNAi knockdown in the C. elegans multivulva model, genetic epistasis, and FGFR inhibitor rescue

    PMID:33092268

    Open questions at the time
    • Direct cargo trafficked by RABN-8/RAB-8 not identified
    • Conservation of the FGF-secretion role in mammals untested
  14. 2023 Medium

    Identified CENTLEIN as a direct GEF-domain partner controlling Rabin8 pericentrosomal turnover, placing it upstream of Rabin8-mediated Rab8 activation in ciliogenesis.

    Evidence Direct binding with deletion mapping, knockdown/knockout, rescue with full-length vs binding-deficient CENTLEIN, and activated RAB8A epistasis

    PMID:37475549

    Open questions at the time
    • Mechanism by which CENTLEIN prevents pericentrosomal Rabin8 accumulation unresolved
    • Single lab
  15. 2024 Medium

    Demonstrated a role in immune cell adhesion, with Rabin8 activating Rab8 to transport LFA1 vesicles and modulate LFA1-ICAM1 binding frequency independently of Rap1.

    Evidence Super-resolution and single-molecule imaging on supported lipid bilayers, Rab8 inactivation, and live-cell imaging

    PMID:39170909

    Open questions at the time
    • Upstream signal coupling LFA1 outside-in signaling to Rabin8 not defined
    • Single lab
  16. 2025 High

    Showed in vivo that NDR2 phosphorylation of Rabin8 at Ser-272 governs Rab11-to-Rab8 succession and Rabin8 integration into rhodopsin transport carriers at Golgi exit sites.

    Evidence Xenopus transgenic photoreceptors expressing Rabin8 mutants, co-IP with the R-SNARE VAMP7, and confocal/electron microscopy

    PMID:39774853

    Open questions at the time
    • How VAMP7 association is coordinated with Rab8 activation mechanistically unresolved
    • Generality of the Golgi-exit-site step beyond photoreceptors untested
  17. 2025 Medium

    Extended the NDR-Rabin8-Rab11 axis to stress-induced neuronal remodeling, where RABI-1/RAB-11.2 act downstream of SAX-1 in branch-specific dendrite elimination.

    Evidence C. elegans genetic epistasis, RNAi/mutant analysis, dendrite pruning and endocytosis assays (preprint)

    PMID:bio_10.1101_2025.06.09.658633

    Open questions at the time
    • Molecular cargo trafficked during branch elimination not identified
    • Preprint; single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the multiple recruitment, scaffolding, and phosphoregulatory inputs are integrated to set the timing and site of Rabin8-mediated Rab8 activation across its different cellular processes remains unresolved.
  • No unified model coordinating TRAPPII tethering, NDR2 phosphorylation, and Rab11 binding in time
  • GEF-independent functions (autophagy, mTORC1) lack defined molecular effectors
  • Disease relevance in humans not established by direct evidence in the corpus

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Localization
GO:0005815 microtubule organizing center 4 GO:0005929 cilium 3 GO:0031410 cytoplasmic vesicle 3 GO:0005829 cytosol 2 GO:0005794 Golgi apparatus 1
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 4 R-HSA-5653656 Vesicle-mediated transport 3 R-HSA-9612973 Autophagy 1
Partners
CENTLEINRAB11ARAB11FIP3RAB8ARHEBSSX2TRAPPC14VAMP7

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 Rabin3 (RAB3IP) was identified as a novel protein that interacts specifically with Rab3A and Rab3D (but not Rab3C, Rab2, Ran, or Ras) via the effector domain of Rab3A; point mutations F51L, V55E, and G56D in the effector domain of Rab3A abolish the interaction. The protein contains a region of sequence similarity to the yeast Sec2p GEF. However, in vitro the GST-Rabin3 fusion protein associates only weakly with recombinant Rab3A and possesses no detectable GTPase-activating protein or nucleotide exchange activity toward Rab3A. Yeast two-hybrid screen, GST pulldown, in vitro GTPase assays, point mutagenesis Molecular and cellular biology Medium 7532276
2002 RAB3IP (human Rabin3/Rabin8) physically interacts with the cancer-related protein SSX2 in vitro and in cells. GST pulldown confirmed direct interaction. Co-expression of RAB3IP and SSX2 causes relocalization of the normally cytoplasmic RAB3IP to the nucleus. The interaction maps to the N-terminal moiety of SSX2, and RAB3IP does not interact with SSX1, SSX3, or SSX4. Yeast two-hybrid, GST pulldown, immunofluorescence co-localization in transfected cells Genes, chromosomes & cancer Medium 12007189
2005 Rabin8 (human) and its rat equivalent Rabin3 function as guanine nucleotide exchange factors (GEFs) specifically for Rab8 but not for Rab3A or Rab5. Endogenous and ectopically expressed Rabin8 colocalizes with cortical actin; cytochalasin D and phorbol esters induce translocation of both Rabin8 and Rab8 to lamellipodia-like structures. Co-expression of Rabin8 with dominant-negative Rab8 causes relocalization of Rabin8 to vesicular structures enriched in cell protrusions, implicating both proteins in polarized membrane transport. In vitro nucleotide exchange assay, live cell imaging, co-expression of dominant-negative Rab8, fluorescence microscopy Methods in enzymology Medium 16473595
2011 Upon serum withdrawal, Rabin8 relocalizes to Rab11-positive vesicles that are transported to the centrosome to initiate ciliogenesis. Rab11-GTP associates with the Rabin8 C-terminal region and this interaction is required for Rabin8 preciliary membrane trafficking to the centrosome and for ciliogenesis. The TRAPPII complex associates with the Rabin8 N-terminal domain and TRAPPII subunits colocalize with centrosomal Rabin8 and are required for Rabin8 preciliary targeting and ciliogenesis. The BBSome binds Rabin8, which acts as a GEF activating Rab8 for ciliary membrane formation. Live fluorescence microscopy, tandem affinity purification/mass spectrometry, zebrafish epistasis, co-IP, dominant-negative and knockdown experiments Proceedings of the National Academy of Sciences of the United States of America High 21273506
2011 Rabin8 co-immunoprecipitates with the GTPase Rheb. Overexpression of Rabin8 suppresses phosphorylation of Ser235/Ser236 in ribosomal protein S6 (a readout of mTORC1 activity), while siRNA-mediated knockdown of Rabin8 increases this phosphorylation, indicating Rabin8 negatively regulates mTORC1 signaling. Co-immunoprecipitation, siRNA knockdown, Western blotting for pS6 Acta naturae Low 22649696
2012 NDR1/2 kinases phosphorylate Rabin8 in brain neurons, as identified by chemical genetics (analog-sensitive kinase allele). Rabin8, as an NDR1/2 substrate, regulates dendritic spine development; knockdown or dominant-negative NDR1/2 affects spine morphology, a phenotype linked to Rabin8 activity as a Rab8 GEF. Chemical genetic substrate identification (analog-sensitive NDR1/2), mass spectrometry, siRNA knockdown, dominant-negative expression, in vivo neuron imaging Neuron High 22445341
2013 NDR2 phosphorylates Rabin8 at Ser-272. This phosphorylation is crucial for ciliogenesis: the non-phosphorylatable S272A mutant causes accumulation of Rabin8/Rab11-containing vesicles at the pericentrosome and impairs preciliary membrane assembly. Mechanistically, Rabin8 binds GTP-bound Rab11 and phosphatidylserine (PS) on pericentrosomal vesicles; the phospho-mimetic S272E mutation decreases affinity for PS but increases affinity for the exocyst component Sec15. Thus NDR2-mediated phosphorylation switches Rabin8 binding specificity from PS to Sec15 to promote Rab8 activation and ciliary membrane formation. In vitro kinase assay, phospho-mimetic and non-phosphorylatable Rabin8 mutants, binding assays (lipid and protein), immunofluorescence, ciliogenesis assays The EMBO journal High 23435566
2013 Structural snapshots of the full Rabin8-catalyzed nucleotide exchange reaction for Rab8 were obtained, revealing three distinct enzyme-substrate complexes: Rab8·Rabin8·GDP (ternary), nucleotide-free Rab8·Rabin8 (binary), and Rab8·Rabin8·GTP (ternary product). Enzymatic characterization provided a mechanistic model for Rabin8/GRAB-mediated GEF activity. Structural analysis (crystal snapshots), in vitro enzymatic characterization of nucleotide exchange The Journal of biological chemistry High 24072714
2015 Rabin8 suppresses autophagosome formation independently of its Rab8-GEF activity: depletion of Rabin8 promotes nutrient starvation-induced autophagosome formation, and a Rabin8 GEF-domain mutant (lacking GEF activity) still rescues this phenotype, while depletion of Rab8 does not affect autophagosome formation. NDR kinase-dependent phosphorylation of Rabin8 at Ser-272 is involved in this suppressive function (non-phosphorylatable S272A fails to rescue). Rabin8's suppressive function in autophagy requires its non-conserved C-terminal region. siRNA knockdown, GEF-dead mutant expression, non-phosphorylatable mutant rescue assays, autophagosome quantification by microscopy and Western blot Journal of biochemistry Medium 25787272
2015 The Arf/Rab11 effector FIP3 (RAB11FIP3) coordinates the interactions of ASAP1 and Rab11a with Rabin8 within a targeting complex for ciliary receptor (rhodopsin) trafficking. FIP3 competes with rhodopsin for binding to ASAP1 and shapes the binding pocket for Rabin8 within the ASAP1-Rab11a-FIP3 complex, facilitating assembly and activation of the Rab11-Rabin8-Rab8 cascade during ciliary receptor trafficking. Co-immunoprecipitation, siRNA ablation of FIP3 with rhodopsin mislocalization readout, epistasis in photoreceptor cells Journal of cell science Medium 25673879
2019 TRAPPC14 (C7orf43/MAP11), a newly identified TRAPPII-specific subunit, directly binds Rabin8 and mediates Rabin8 association with the TRAPPII complex. TRAPPC14 knockdown diminishes Rabin8 preciliary centrosome accumulation. TRAPPC14 also interacts with distal appendage proteins FBF1 and CEP83, which are required for GFP-Rabin8 centrosomal accumulation, supporting a role for the TRAPPII complex in tethering preciliary vesicles containing Rabin8 to the mother centriole. MS-based interactome identification, co-sedimentation, direct binding assays, siRNA knockdown with ciliogenesis and localization readouts, zebrafish validation The Journal of biological chemistry High 31467083
2019 Phosphorylation of Rab8a at Ser111 (by PINK1 kinase) impairs Rabin8-mediated nucleotide exchange. Mechanistically, pS111 (or the phosphomimetic S111E) establishes an intramolecular interaction with Arg79 in Rab8a, which disrupts a key intermolecular salt bridge between Rab8a Arg79 and Rabin8 Asp187, drastically reducing binding affinity and nucleotide exchange rate (>80% decrease confirmed in vitro). Molecular dynamics simulations, free energy calculations, in vitro nucleotide exchange assay with Rab8a mutants Biochemistry Medium 31361120
2020 In C. elegans, RABN-8 (Rabin8 ortholog), as a GEF for RAB-8, is required for vulval tumor formation caused by hyperactivated EGFR signaling. Mechanistically, RABN-8 promotes secretion of EGL-17/FGF from vulval precursor cells, connecting the Rab8-Rabin8 trafficking axis to FGF-mediated signaling downstream of EGFR. RNAi knockdown in C. elegans multivulva model, genetic epistasis, FGFR inhibitor rescue International journal of molecular sciences Medium 33092268
2023 CENTLEIN directly binds RABIN8, with a 31-amino acid sequence in the 200–230 region of the RABIN8 GEF domain mediating the interaction. CENTLEIN depletion causes persistent accumulation of RABIN8 at the pericentrosome and primary cilium loss. Expression of full-length but not RABIN8-binding-deficient CENTLEIN rescues the ciliogenesis defect. Expression of activated RAB8A partially reverses cilium loss in CENTLEIN-null cells, placing CENTLEIN upstream of Rabin8-mediated Rab8 activation in ciliogenesis. Direct binding assay with deletion mapping, siRNA/CRISPR knockdown/knockout, rescue with full-length vs. deletion mutant CENTLEIN, activated RAB8A epistasis Acta biochimica et biophysica Sinica Medium 37475549
2024 Rabin8 acts as the guanine exchange factor activating Rab8 downstream of low-affinity LFA1-dependent outside-in signaling in lymphocytes. Rabin8-mediated Rab8 activation at the cell contact area drives intracellular transport and accumulation of LFA1-containing vesicles at the contact surface, modulating LFA1 avidity (increased frequency of LFA1-ICAM1 interactions without affecting binding lifetime) independent of Rap1. Super-resolution microscopy, single-molecule imaging on supported lipid bilayers, Rab8 inactivation, live cell imaging PNAS nexus Medium 39170909
2025 In Xenopus laevis transgenic rod photoreceptors, Rabin8 accumulates at Golgi exit sites (GESs)/trans-Golgi network and is integrated into rhodopsin transport carriers (RTCs) following NDR2-mediated phosphorylation at S272. Rabin8 mutants deficient in Rab11 binding prevent membrane association. Both GFP-Rabin8 and NDR2 kinase interact with the RTC-associated R-SNARE VAMP7 at the trans-Golgi and GESs. The phosphomimetic S272E mutant integrates into RTCs and supports subsequent Rab8 GEF activity, while the non-phosphorylatable S272A mutant causes GES enlargement and deformation and abnormal membrane advancement, bypassing RTCs—establishing that NDR2 phosphorylation of Rabin8 regulates Rab11-to-Rab8 succession in rhodopsin Golgi-to-cilia trafficking. Xenopus laevis transgenic photoreceptors expressing GFP-Rabin8 wild-type and mutants, co-immunoprecipitation with VAMP7, confocal and electron microscopy, phospho-mimetic and non-phosphorylatable mutant analysis Journal of cell science High 39774853
2025 In C. elegans, RABI-1 (Rabin8 ortholog) and RAB-11.2 mediate secondary dendrite branch elimination downstream of the NDR kinase SAX-1 during stress-induced neuronal remodeling. SAX-1 promotes endocytosis during remodeling, and RABI-1/RAB-11.2 effects on tertiary branch elimination are minimal, revealing branch-specific mechanistic requirements. C. elegans genetic epistasis, RNAi/mutant analysis, dendrite pruning quantification, endocytosis assays bioRxivpreprint Medium bio_10.1101_2025.06.09.658633

Source papers

Stage 0 corpus · 23 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Primary cilia membrane assembly is initiated by Rab11 and transport protein particle II (TRAPPII) complex-dependent trafficking of Rabin8 to the centrosome. Proceedings of the National Academy of Sciences of the United States of America 350 21273506
2012 Chemical genetic identification of NDR1/2 kinase substrates AAK1 and Rabin8 Uncovers their roles in dendrite arborization and spine development. Neuron 116 22445341
2019 LncRNA HOTAIR targets miR-126-5p to promote the progression of Parkinson's disease through RAB3IP. Biological chemistry 86 30738012
2013 NDR2-mediated Rabin8 phosphorylation is crucial for ciliogenesis by switching binding specificity from phosphatidylserine to Sec15. The EMBO journal 84 23435566
1995 Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A. Molecular and cellular biology 71 7532276
2013 Intermediates in the guanine nucleotide exchange reaction of Rab8 protein catalyzed by guanine nucleotide exchange factors Rabin8 and GRAB. The Journal of biological chemistry 55 24072714
2002 The cancer-related protein SSX2 interacts with the human homologue of a Ras-like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP. Genes, chromosomes & cancer 54 12007189
2015 The Arf and Rab11 effector FIP3 acts synergistically with ASAP1 to direct Rabin8 in ciliary receptor targeting. Journal of cell science 49 25673879
2018 Promotion of Cell Proliferation through Inhibition of Cell Autophagy Signalling Pathway by Rab3IP is Restrained by MicroRNA-532-3p in Gastric Cancer. Journal of Cancer 35 30519341
2021 MicroRNA‑126 protects SH‑SY5Y cells from ischemia/reperfusion injury‑induced apoptosis by inhibiting RAB3IP. Molecular medicine reports 34 34935056
2020 Long noncoding RNA NEAT1 knockdown inhibits MPP+-induced apoptosis, inflammation and cytotoxicity in SK-N-SH cells by regulating miR-212-5p/RAB3IP axis. Neuroscience letters 31 32442477
2019 The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8 for preciliary vesicle tethering at the mother centriole during ciliogenesis. The Journal of biological chemistry 25 31467083
2020 LINC00943 knockdown attenuates MPP+-induced neuronal damage via miR-15b-5p/RAB3IP axis in SK-N-SH cells. Neurological research 21 33208053
2015 Rabin8 suppresses autophagosome formation independently of its guanine nucleotide-exchange activity towards Rab8. Journal of biochemistry 11 25787272
2018 Rab3IP interacts with SSX2 and enhances the invasiveness of gastric cancer cells. Biochemical and biophysical research communications 10 30005870
2005 Purification and functional properties of a Rab8-specific GEF (Rabin3) in action remodeling and polarized transport. Methods in enzymology 10 16473595
2019 Phosphorylation of Ser111 in Rab8a Modulates Rabin8-Dependent Activation by Perturbation of Side Chain Interaction Networks. Biochemistry 8 31361120
2011 Rabin8 Protein Interacts with GTPase Rheb and Inhibits Phosphorylation of Ser235/Ser236 in Small Ribosomal Subunit Protein S6. Acta naturae 7 22649696
2020 Rab8 and Rabin8-Mediated Tumor Formation by Hyperactivated EGFR Signaling via FGFR Signaling. International journal of molecular sciences 5 33092268
2024 Low-affinity LFA1-dependent outside-in signaling mediates avidity modulation via the Rabin8-Rab8 axis. PNAS nexus 4 39170909
2025 Rabin8 phosphorylated by NDR2, the canine early retinal degeneration gene product, directs rhodopsin Golgi-to-cilia trafficking. Journal of cell science 3 39774853
2015 Biochemical analysis of Rabin8, the guanine nucleotide exchange factor for Rab8. Methods in cell biology 3 26360028
2023 A direct interaction between CENTLEIN and RABIN8 is required for primary cilium formation. Acta biochimica et biophysica Sinica 0 37475549

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