| 2007 |
Rab10 functions as a downstream target of the AS160 (TBC1D4) Rab GAP in the insulin-signaling pathway regulating GLUT4 translocation to the adipocyte plasma membrane. Overexpression of a GTP-hydrolysis-defective Rab10 mutant increased surface GLUT4 in basal adipocytes; Rab10 knockdown attenuated insulin-induced GLUT4 redistribution and reduced GLUT4 exocytosis rate; the basal increase in plasma-membrane GLUT4 caused by AS160 knockdown was partially blocked by simultaneous Rab10 knockdown. |
Dominant-negative and constitutively active Rab10 mutant overexpression, siRNA knockdown, flow cytometry of surface GLUT4, exocytosis rate measurement in 3T3-L1 adipocytes |
Cell Metabolism |
High |
17403373
|
| 2008 |
Among Rab GTPases present in GLUT4 vesicles and acting as AS160 GAP substrates (Rab8A, Rab8B, Rab10, Rab14), only knockdown of Rab10 inhibited GLUT4 translocation in 3T3-L1 adipocytes. Approximately 5% of total Rab10 resides in GLUT4 vesicles from low-density microsomes; ~90% of Rab10 is in the inactive GDP form in both basal and insulin-stimulated states. The constitutively active Rab10 Q68L mutant is still a substrate for the AS160 GAP domain. |
siRNA knockdown of individual Rabs, subcellular fractionation, GTP-loading assays, in vitro GAP assay |
The Biochemical Journal |
High |
18076383
|
| 2011 |
Dennd4C is identified as the primary guanine nucleotide exchange factor (GEF) for Rab10 required for insulin-stimulated GLUT4 translocation in adipocytes. Knockdown of Dennd4C markedly inhibited GLUT4 translocation; Dennd4C was found in isolated GLUT4 vesicles. |
siRNA knockdown of Dennd4C, GLUT4 translocation assay, subcellular fractionation of GLUT4 vesicles |
The Journal of Biological Chemistry |
High |
21454697
|
| 2012 |
Rab10 directly mediates GLUT4 storage vesicle (GSV) translocation to and docking at the plasma membrane in adipocytes. Myosin-Va associates with GSVs by interacting with Rab10, positioning peripherally recruited GSVs for ultimate fusion. Live TIRF microscopy with IRAP-pHluorin showed Rab10 as the Rab specifically marking GSVs undergoing insulin-stimulated plasma membrane fusion; Rab14 instead labels transferrin-receptor-positive endosomal compartments. |
Dual-color TIRF microscopy, IRAP-pHluorin fusion assay, siRNA knockdown, co-immunoprecipitation of Rab10 with Myosin-Va |
The Journal of Cell Biology |
High |
22908308
|
| 2012 |
Rab10 is an ER-specific Rab GTPase that regulates ER structure and dynamics. Rab10 localizes to dynamic ER-associated structures that track along microtubules and mark sites of new ER tubule growth. Depletion or GDP-locked Rab10 mutant expression results in fewer ER tubules due to reduced ability of dynamic tubules to grow out and fuse with adjacent ER. The Rab10 domain at the leading edge of dynamic ER tubules is highly enriched with phospholipid synthesis enzymes phosphatidylinositol synthase (PIS) and CEPT1; formation and function of this domain are inhibited by GDP-locked Rab10. |
Live-cell fluorescence microscopy of ER dynamics, siRNA knockdown, GDP-locked mutant expression, co-localization with PIS/CEPT1 |
Nature Cell Biology |
High |
23263280
|
| 2006 |
RAB-10 (C. elegans ortholog) is required for endocytic recycling in polarized intestinal epithelial cells. rab-10 null mutants accumulate abnormally enlarged RAB-5-positive early endosomes, lose RME-1-positive recycling endosomes, and accumulate basolaterally recycling transmembrane cargo, indicating RAB-10 functions upstream of RME-1 in basolateral recycling. GFP-RAB-10 localizes to endosomes and Golgi. |
rab-10 null mutant analysis, GFP-RAB-10 reporter localization, immunofluorescence for endosomal markers, cargo trafficking assays in C. elegans intestine |
Molecular Biology of the Cell |
High |
16394106
|
| 2006 |
Rab10 is specifically associated with common (basolateral sorting) endosomes in polarized MDCK cells. Expression of GTP-hydrolysis-defective or GDP-bound Rab10 mutants increased recycling from basolateral early endosomes without affecting apical recycling or later recycling compartments, indicating Rab10 mediates transport from basolateral sorting endosomes to common endosomes. |
GFP-tagged wild-type and mutant Rab10 expression, quantitative confocal microscopy, endocytic probe trafficking assays in polarized MDCK cells |
Molecular Biology of the Cell |
High |
16641372
|
| 2006 |
Rab10 functions in biosynthetic trafficking from the Golgi to the basolateral membrane in polarized MDCK cells. GFP-Rab10 localizes primarily to the Golgi during early polarization; activated Rab10 mutant inhibits biosynthetic transport from the Golgi and missorts basolateral cargo to the apical membrane. Simultaneous inhibition of Rab10 and Rab8a more strongly impairs basolateral sorting, suggesting cooperation. |
GFP-Rab10 localization, activated mutant expression, RNAi knockdown, biosynthetic transport assays in polarized MDCK cells |
Traffic |
Medium |
17132146
|
| 2008 |
Rab10 interacts with myosin Va, myosin Vb, and myosin Vc. The interaction requires the alternatively spliced exon D in myosin Va and Vb (and the homologous region in Vc). Both Rab8a and Rab10 are mislocalized by dominant-negative myosin V tails. The interaction was confirmed by yeast two-hybrid assays and FRET studies. |
Co-immunoprecipitation, yeast two-hybrid, FRET, dominant-negative myosin V tail expression, splice isoform analysis |
The Journal of Biological Chemistry |
High |
19008234
|
| 2010 |
Rab10 regulates continuous replenishment of TLR4 from Golgi to the plasma membrane in macrophages, which is essential for optimal macrophage activation following LPS stimulation. Blockade of Rab10 function leads to decreased membrane TLR4 expression and diminished production of inflammatory cytokines and interferons upon LPS stimulation. |
Dominant-negative Rab10 expression, siRNA knockdown, flow cytometry of surface TLR4, cytokine measurement, in vivo LPS-induced acute lung injury model |
PNAS |
High |
20643919
|
| 2010 |
RAB-10 (C. elegans) and its binding partner EHBP-1 (calponin homology domain protein) function together in endocytic recycling. Yeast two-hybrid identified EHBP-1 as a RAB-10 binding partner. GFP-EHBP-1 colocalizes with RFP-RAB-10 on endosomal structures; ehbp-1 loss-of-function mutants share with rab-10 mutants specific endosome morphology and cargo localization defects. |
Yeast two-hybrid screen, fluorescence co-localization in C. elegans, null mutant phenotypic analysis, cargo trafficking assays |
Molecular Biology of the Cell |
High |
20573983
|
| 2010 |
Rab10 associates with primary cilia in renal epithelia and colocalizes with exocyst proteins at the base of nascent cilia. Rab10 physically interacts with the exocyst complex as detected by co-immunoprecipitation with anti-Sec8 antibodies. |
Immunofluorescence microscopy, co-immunoprecipitation with anti-Sec8, live imaging in renal epithelial cells in culture and in vivo |
American Journal of Physiology - Renal Physiology |
Medium |
20576682
|
| 2011 |
Lgl1 activates Rab10 in developing axons by releasing GDP dissociation inhibitor (GDI) from Rab10, thereby promoting membrane trafficking of plasmalemmal precursor vesicles (PPVs) required for axon development and neuronal polarization. Rab10 lies downstream of Lgl1 in axon development; both are required for neocortical neuronal polarization in vivo. |
Co-immunoprecipitation, dominant-negative and knockdown experiments, directional membrane insertion assay, in vivo rat cortex knockdown |
Developmental Cell |
High |
21856246
|
| 2013 |
In Drosophila follicle cells, Crag targets Rab10 to structures in the basal cytoplasm, restricting basement membrane protein delivery to the basal surface during egg chamber elongation. Tango1 and Rab10 are planar polarized at the basal epithelial surface, coupling BM production to organ morphogenesis. |
Genetic epistasis, GFP reporter localization, loss-of-function analysis of Crag, Tango1 and Rab10 in Drosophila follicle cells |
Developmental Cell |
High |
23369713
|
| 2013 |
Rab10 interaction with myosin Vb (MYO5B) via the exon D-encoded domain determines the formation of Rab10-containing post-Golgi carriers and is required for axon development. Disrupting MYO5B(+D) expression or its interaction with Rab10 impairs fission of Rab10 vesicles from trans-Golgi membranes and inhibits axon development. |
Co-immunoprecipitation, splice isoform mutants, vesicle biogenesis assay, knockdown in hippocampal neurons, in vivo analysis in neocortical neurons and zebrafish retinal ganglion cells |
Nature Communications |
High |
23770993
|
| 2014 |
JIP1 (c-Jun N-terminal kinase-interacting protein 1) interacts with GTP-locked active Rab10 and directly connects Rab10 to kinesin-1 light chain (KLC), forming a kinesin-1/JIP1/Rab10 complex required for anterograde transport of plasmalemmal precursor vesicles (PPVs) during axon development and neuronal polarization. |
Co-immunoprecipitation, dominant-active Rab10 pulldown, siRNA knockdown of JIP1/KLC, anterograde transport assays in hippocampal neurons, in vivo rat neocortical transfection |
The Journal of Neuroscience |
High |
24478353
|
| 2014 |
MARCKS mediates membrane targeting of Rab10-positive PPVs during axon development. GTP-locked active Rab10 binds membrane-associated MARCKS; this affinity depends on the phosphorylation status of the MARCKS effector domain. MARCKS knockdown or disruption of Rab10-MARCKS interaction inhibits axon growth, impairs docking and fusion of Rab10 vesicles with the plasma membrane, and reduces membrane insertion of axonal receptors. |
Co-immunoprecipitation, GTP-locked Rab10 pulldown, MARCKS knockdown and phosphomutant expression, TIRF microscopy of vesicle docking/fusion, membrane insertion assays |
Cell Research |
High |
24662485
|
| 2014 |
Rab10-mediated endocytosis of hyaluronan synthase HAS3 regulates hyaluronan synthesis and cell adhesion. Rab10 co-localizes and co-immunoprecipitates with HAS3 from endosomal vesicles. Rab10 silencing increases plasma membrane HAS3 residence, increases HA secretion and cell surface HA coat, and blocks retrograde HAS3 trafficking from plasma membrane to early endosomes. |
Co-immunoprecipitation, co-localization microscopy, siRNA knockdown, HA synthesis assay, cell adhesion assay |
The Journal of Biological Chemistry |
Medium |
24509846
|
| 2014 |
Rab10 is a target of the AS160 (TBC1D4) GAP, and once activated (GTP-bound), Rab10 recruits the Ral GEF Rlf/Rgl2, increasing GTP binding of RalA. Rab10 and RalA co-reside in the same pool of Glut4-storage vesicles; RalA is epistatic downstream of Rab10 in insulin-stimulated Glut4 translocation. Membrane-tethered Rlf compensates for Rab10 loss in Glut4 translocation. |
Co-immunoprecipitation, GTP-loading assays, siRNA knockdown, epistasis rescue experiments, Glut4 translocation assay |
Molecular Biology of the Cell |
High |
25103239
|
| 2015 |
Rab10-GTP (but not GDP form) binds to exocyst subunits Exoc6 and Exoc6b. Both isotypes are found in 3T3-L1 adipocytes, and knockdown of Exoc6, Exoc6b, or both inhibits GLUT4 translocation, identifying Rab10-GTP association with Exoc6/6b as a molecular link between insulin signaling and the exocytic machinery. |
Pulldown of GTP-locked Rab10 with exocyst subunits, siRNA knockdown of Exoc6/6b, GLUT4 translocation assay |
Biochemical and Biophysical Research Communications |
Medium |
26299925
|
| 2015 |
RAB-10 and amphiphysin AMPH-1 bind to and recruit TBC-2 (a Rab-5 GAP) to endosomes. In the absence of RAB-10 or AMPH-1 binding to TBC-2, RAB-5 membrane association is abnormally high and recycling cargo is trapped in early endosomes. This identifies a mechanism by which RAB-10 and AMPH-1 down-regulate RAB-5 to enable cargo exit from early endosomes. |
Genetic epistasis in C. elegans, co-immunoprecipitation, fluorescence co-localization, null and loss-of-function mutant analysis |
PLOS Genetics |
High |
26393361
|
| 2015 |
SEC-10 (exocyst subunit) coordinates with RAB-10 and microtubules to form interconnected endosomal tubules required for basolateral recycling of clathrin-independent endocytic cargoes including hTAC, GLUT1, and DAF-4. Epistasis analysis indicates SEC-10 operates at an intermediate step between early endosomes and recycling endosomes; depletion of either SEC-10 or RAB-10 disrupts tubular endosome structure. |
siRNA/RNAi depletion, fluorescence microscopy, epistasis analysis, cargo recycling assays in C. elegans intestine |
PNAS |
High |
25301900
|
| 2016 |
Rab10 is essential for lipophagy in hepatocytes. During autophagy stimulation, Rab10 activity is amplified and Rab10 is recruited to nascent autophagic membranes at the lipid droplet surface. Rab10 activation is required for LC3 recruitment to autophagosomes and stimulates increased association with adaptor protein EHBP1 and membrane-deforming ATPase EHD2, which together drive engulfment of lipid droplets. |
siRNA knockdown, dominant-negative and GTPase-defective Rab10 mutant expression, co-immunoprecipitation of Rab10-EHBP1-EHD2 complex, fluorescence microscopy of LC3 recruitment, lipid droplet accumulation assay |
Science Advances |
High |
28028537
|
| 2016 |
SEC16A is a RAB10 effector required for insulin-stimulated GLUT4 trafficking. Colocalization of SEC16A with RAB10 is augmented by insulin stimulation; SEC16A knockdown attenuates insulin-induced GLUT4 translocation, phenocopying RAB10 knockdown. RAB10-SEC16A promotes insulin-stimulated mobilization of GLUT4 from a perinuclear recycling endosome/TGN compartment, promoting vesicle biogenesis independently of canonical COPII function. |
Co-localization microscopy, siRNA knockdown, GLUT4 translocation assay, COPII component analysis |
The Journal of Cell Biology |
High |
27354378
|
| 2016 |
Rab10-based secretion pathway promotes pericellular basement membrane protein accumulation and fibril formation in Drosophila egg chamber. Manipulation of the Rab10 secretion pathway demonstrates that BM fibrillar structure influences egg chamber morphogenesis. |
Live imaging, genetic manipulation of Rab10 pathway, fluorescent BM protein reporters in Drosophila |
Developmental Cell |
High |
27404358
|
| 2016 |
LRRK2 directly phosphorylates Rab10 at a conserved threonine/serine residue (Thr73) in the effector-binding switch-II motif. Phosphorylation of Rab10 is ablated in kinase-inactive LRRK2[D2017A] knockin MEFs and mouse lung, establishing LRRK2 as the major Rab10 kinase. Phospho-Ser910 and Ser935 and 14-3-3 binding play a role in facilitating LRRK2-mediated Rab10 phosphorylation in vivo. |
Phos-tag electrophoresis, kinase-inactive LRRK2 knockin MEFs and tissue, LRRK2 inhibitor treatment, phospho-specific antibody detection |
The Biochemical Journal |
High |
27474410
|
| 2019 |
Rab10 identifies a novel class of tubular endosomes in HeLaM cells. Knockout of Rab10 completely abolishes tubular endosomal structures. Kinesin motors KIF13A and KIF13B are novel Rab10-interacting proteins; both the Rab10-binding homology domain and the motor domain of KIF13A are required for Rab10-positive tubular endosome formation. |
CRISPR knockout of Rab10, in silico screening + validation, co-immunoprecipitation of KIF13A/B with Rab10, deletion mutant analysis, fluorescence microscopy |
Journal of Cell Science |
High |
30700496
|
| 2019 |
LRRK2-phosphorylated RAB10 (pT73) accumulates on depolarized mitochondria in a PINK1- and PRKN-dependent manner, binds the autophagy receptor OPTN (optineurin), and promotes OPTN accumulation on depolarized mitochondria to facilitate mitophagy. In LRRK2 mutant (G2019S, R1441C) patient cells, enhanced RAB10 phosphorylation reduces RAB10-OPTN interaction, mitochondrial accumulation of both proteins, and mitophagy. A phosphomimetic RAB10 mutant shows less OPTN interaction and fails to rescue mitophagy. |
Co-immunoprecipitation, immunofluorescence, mitophagy assay, patient-derived cells, LRRK2 knockdown/inhibition rescue, phosphomimetic mutant analysis |
Autophagy |
High |
30945962
|
| 2019 |
Phosphorylated RAB10 (by pathogenic LRRK2) is recruited to centrosome-localized RILPL1, contributing to ciliogenesis defects and centrosomal cohesion deficits in dividing cells. Both RAB8 and RAB10 contribute to LRRK2-mediated centrosomal cohesion deficits; effects are dependent on RAB8, RAB10, and RILPL1. |
Immunofluorescence for phospho-RAB10 at centrosomes, patient-derived peripheral cells, primary astrocytes from LRRK2 mutant mice, LRRK2 kinase inhibition, siRNA knockdown |
Human Molecular Genetics |
High |
31428781
|
| 2020 |
Rab10 specifically regulates macropinocytosis (not phagocytosis or clathrin-mediated endocytosis) in macrophages and dendritic cells. LRRK2 phosphorylates cytoplasmic PI(3,4,5)P3-positive GTP-Rab10 before EEA1/Rab5 recruitment to early macropinosomes. LRRK2 phosphorylation of Rab10 blocks EHBP1L1-mediated recycling tubules and cargo turnover of macropinosome cargo including CCR5, CD11b, MHCII. EHBP1L1 overexpression competitively inhibits LRRK2 phosphorylation of Rab10. Rab10 knockdown and LRRK2 kinase inhibition suppress maturation of CCR5-loaded signaling endosomes critical for CCL5-induced Akt activation and chemotaxis. |
siRNA knockdown, LRRK2 inhibition, endocytosis assays distinguishing macropinocytosis from phagocytosis and CME, phospho-Rab10 imaging, EHBP1L1 overexpression rescue, signaling and chemotaxis assays in primary macrophages/dendritic cells/microglia |
The EMBO Journal |
High |
32853409
|
| 2020 |
LRRK2 is required for RAB8a and RAB10 recruitment to phagosomes in human iPSC-derived macrophages and microglia. LRRK2 is recruited to LAMP1+/RAB9+ maturing phagosomes; LRRK2 kinase inhibition enhances LRRK2 residency at the phagosome. |
LRRK2 knockout and G2019S isogenic iPSC-derived macrophages/microglia, immunofluorescence for phagosome markers, LRRK2 kinase inhibitor treatment |
Stem Cell Reports |
Medium |
32359446
|
| 2020 |
The TBC1D4-RAB10 signaling module controls GLUT4 mobilization from a trans-Golgi network (TGN) storage compartment. GLUT4 is retained in a TGN element from which it is mobilized by insulin via RAB10; this compartment also contains newly synthesized lysosomal proteins and the ATP7A copper transporter, but insulin does not mobilize ATP7A and copper does not mobilize GLUT4, and RAB10 is not required for copper-elicited ATP7A mobilization. |
RAB10 siRNA knockdown, insulin and copper stimulation assays, fluorescence co-localization, cargo mobilization assays in adipocytes |
Molecular Biology of the Cell |
High |
33175605
|
| 2021 |
LRRK2 activity blocks ciliation by preventing CP110 release from the mother centriole, a step required for early ciliogenesis; this blockade requires Rab10 and RILPL1 proteins and is due to failure to recruit TTBK2 (a kinase needed for CP110 release). Deciliation probability does not change in cells lacking Rab10 or RILPL1, indicating a distinct LRRK2 pathway for deciliation. |
Live-cell fluorescence microscopy, R1441C LRRK2 MEF cells, Rab10 knockout, RILPL1 manipulation, LRRK2 kinase inhibition, CP110 and TTBK2 localization assays |
PNAS |
High |
33653948
|
| 2021 |
LRRK2-phosphorylated Rab10 sequesters Myosin Va and RILPL2 at the peri-centriolar region to block ciliogenesis. RILPL2 binds preferentially to LRRK2-phosphorylated Rab8A and Rab10; the globular tail domain of Myosin Va contains a high-affinity binding site for LRRK2-phosphorylated Rab10. PhosphoRab10 retains Myosin Va over pericentriolar membranes as measured by FLIP. |
Co-immunoprecipitation, fluorescence loss in photobleaching (FLIP), phospho-Rab10 pulldown, localization microscopy, ciliogenesis assay |
Life Science Alliance |
High |
33727250
|
| 2021 |
Salmonella effector SopD inhibits Rab10 via a C-terminal GTPase-activating protein (GAP) domain during host cell invasion. During infection, Rab10 and its effectors MICAL-L1 and EHBP1 are recruited to invasion sites; SopD-mediated inhibition of Rab10 promotes removal of Rab10 and recruitment of Dynamin-2 to drive plasma membrane scission and Salmonella-containing vacuole formation. |
SopD domain analysis, pulldown/Co-IP of SopD with Rab10, Rab10 knockdown, GAP domain mutagenesis, Dynamin-2 recruitment assay, infection-based plasma membrane scission assay |
Nature Communications |
High |
34349110
|
| 2021 |
Pathogenic LRRK2 (R1441C)-mediated centrosomal cohesion deficits require RILPL1-mediated centrosomal accumulation of phosphorylated Rab10. RILPL1 localizes to the subdistal appendage of the mother centriole, followed by phospho-Rab protein recruitment. These centrosomal alterations impair cell polarization as monitored by scratch wound assays and are reverted by LRRK2 kinase inhibition. |
Immunofluorescence for phospho-Rab10 at centrosomes, siRNA knockdown of Rab10/RILPL1, LRRK2 kinase inhibition, scratch wound polarization assay, RILPL2 and other Rab controls |
Biology Open |
Medium |
35776681
|
| 2022 |
Lysosomal positioning regulates Rab10 phosphorylation by LRRK2: pRab10 is restricted to perinuclear lysosomes, not peripheral lysosomes. Anterograde lysosomal transport (via ARL8B/SKIP overexpression or JIP4 knockdown) blocks Rab10 phosphorylation and the subsequent lysosomal tubulation/sorting process (LYTL). Perinuclear clustering of lysosomes (via RILP overexpression) increases LRRK2-dependent Rab10 phosphorylation. PPM1H phosphatase knockdown increases pRab10 and lysosomal tubulation. |
LRRK2 membrane targeting constructs, ARL8B/SKIP overexpression, JIP4 knockdown, RILP overexpression, PPM1H knockdown, pRab10 immunofluorescence, lysosomal tubulation assay |
PNAS |
High |
36256825
|
| 2022 |
RAB10 regulates hepatocyte LDL receptor (LDLR) recycling from RAB11-positive endosomes to the plasma membrane, and also promotes transferrin receptor recycling from RAB4-positive compartments. RAB10 loss reduces LDL uptake by impairing endosomal recycling of LDLR. |
CRISPR knockout, LDL uptake assay, LDLR recycling assay, endosomal marker co-localization, RAB11 and RAB4 compartment analysis |
Journal of Lipid Research |
Medium |
35753407
|
| 2023 |
Rab10 defines a membrane compartment in axon terminals that is rapidly mobilized towards the axon terminal upon BDNF stimulation, enabling fine-tuning of retrograde TrkB/BDNF signaling from axon terminals to the soma. Rab10 knockout impairs TrkB sorting to signalling endosomes and propagation of BDNF signalling in primary mouse neurons. |
Rab10 knockout in primary mouse neurons, live-cell imaging, TrkB sorting assay, retrograde transport assay, BDNF signalling readout |
eLife |
High |
36897066
|
| 2024 |
Rab10 and Caveolin-1 (CAV1) mark intraluminal vesicles in migrasomes. Transport of Rab10-CAV1 vesicles to migrasomes requires motor protein Myosin Va and adaptor protein RILPL2. LRRK2-mediated phosphorylation of Rab10 regulates this transport process. CSF-1 is transported to migrasomes via this mechanism to foster monocyte-macrophage differentiation in skin wound healing. |
Live-cell imaging, Rab10 and CAV1 co-localization, Myosin Va and RILPL2 knockdown/inhibition, LRRK2 kinase inhibition, wound healing model, cytokine delivery assay |
PNAS |
High |
39008679
|
| 2024 |
VPS13C interacts with phospho-Rab10 on lysosomes in a phosphorylation-dependent manner in human dopaminergic neurons. Loss of VPS13C disrupts lysosomal morphology, dynamics, motility, distribution, hydrolytic activity, and acidification, and decreases the phospho-Rab10-mediated lysosomal stress response. |
Live-cell microscopy of iPSC-derived dopaminergic neurons, VPS13C KO, phospho-Rab10 interaction assay, lysosomal function assays (pH, hydrolysis, motility) |
The Journal of Cell Biology |
High |
38358348
|
| 2007 |
RAB-10 (C. elegans) regulates recycling of the AMPAR subunit GLR-1 in neurons via a cholesterol-dependent, clathrin-independent endocytic pathway. Genetic epistasis showed that cholesterol depletion suppresses the rab-10 mutant GLR-1 accumulation phenotype (but not lin-10), while clathrin-endocytosis inhibition suppresses lin-10 but not rab-10, placing RAB-10 after clathrin-independent endocytosis. |
Genetic epistasis (rab-10, lin-10, unc-11, itsn-1 mutants), cholesterol depletion, GLR-1 localization assay, behavioral reversal frequency assay in C. elegans |
Molecular Biology of the Cell |
High |
17761527
|
| 2009 |
Rab10 associates transiently with phagosomes at very early time-points (before Rab5 acquisition) and plays a prominent role in phagolysosome formation. Rab10 knockdown or dominant-negative expression delays maturation of phagosomes; constitutively active Rab10 partially rescues live-Mycobacterium-containing phagosome maturation and promotes EEA-1 acquisition on Mycobacterium-containing vacuoles. |
siRNA knockdown, dominant-negative and constitutively active Rab10 mutants, confocal microscopy of phagosome markers, Mycobacterium infection assay |
Traffic |
Medium |
20028485
|
| 2017 |
RAB10 interacts with MGCRABGAP (a male germ cell-specific Rab GAP) during mammalian spermiogenesis. MGCRABGAP exhibits GTPase-activating activity and RAB10 is identified as a substrate/interactor. MGCRABGAP-RAB10 complexes co-localize specifically in the manchette structure during spermatid head formation. |
Co-immunoprecipitation, nano LC-MS/MS proteomics, immunofluorescence co-localization in spermatids, GAP activity assay |
International Journal of Molecular Sciences |
Medium |
28067790
|
| 2023 |
Age-related decline in RAB-10 functionality in C. elegans is caused by upregulation of SDPN-1/PACSIN during senescence, which suppresses RAB-10 activation by competing with DENN-4/GEF. KGB-1/JUN kinase enhances the inhibitory potency of SDPN-1, likely by altering its oligomerization. SDPN-1 knockdown alleviates age-related adherens junction and intestinal barrier defects. |
Age-synchronized C. elegans analysis, SDPN-1 and KGB-1 loss-of-function, RAB-10 activation assay, co-immunoprecipitation of SDPN-1 with DENN-4, barrier permeability assay |
Nature Aging |
Medium |
37640905
|
| 1993 |
HA-tagged Rab10 expressed in CHO and BHK cells is concentrated on membranes in the perinuclear region, partially overlapping with the Golgi marker β-COP, in contrast to Rab8 which localizes to the cell periphery. This establishes that Rab10 and Rab8, despite 66% identity, occupy distinct cellular compartments. |
Epitope-tagged (HA) expression, immunofluorescence microscopy, Golgi marker co-staining in stable CHO/BHK transfectants |
PNAS |
Medium |
7688123
|
| 2011 |
Rab10 is required for von Willebrand factor (VWF) secretion from endothelial cells. Rab10 (and Rab8A) are enriched at the Golgi where Weibel-Palade bodies (WPB) form; Rab10 siRNA knockdown significantly reduces the amount of rapidly-releasable VWF, implicating Rab10 in WPB biogenesis. |
C. elegans AP-1 genetic interaction screen, siRNA knockdown in human endothelial cells (HUVECs), VWF secretion assay, immunofluorescence localization |
Journal of Thrombosis and Haemostasis |
Medium |
21070595
|
| 2019 |
Rab10 regulates tubular endosome formation through KIF13A and KIF13B motors (identified as novel Rab10-interacting proteins). The Rab10-binding homology domain and the motor domain of KIF13A are both required for Rab10-positive tubular endosome formation. |
EGFP-Rab GTPase localization screen, CRISPR/Cas9 Rab10 knockout, in silico screen + Co-immunoprecipitation of KIF13A/B, deletion mutant analysis |
Journal of Cell Science |
High |
30700496
|