| 2007 |
Rab10 functions as a downstream target of the AS160 (TBC1D4) Rab GTPase-activating protein in insulin signaling; Rab10 knockdown attenuates insulin-induced GLUT4 redistribution to the plasma membrane and reduces GLUT4 exocytosis rate, while a GTP-hydrolysis-defective Rab10 mutant increases plasma-membrane GLUT4 in basal adipocytes. Knockdown of Rab10 partially blocks the basal increase in surface GLUT4 caused by AS160 knockdown, placing Rab10 downstream of AS160. |
siRNA knockdown, dominant-active/dominant-negative mutant overexpression, re-expression rescue, dual-knockdown epistasis in 3T3-L1 adipocytes |
Cell metabolism |
High |
17403373
|
| 2008 |
Among Rab8A, Rab8B, Rab10, and Rab14 (all AS160 GAP substrates present in GLUT4 vesicles), only Rab10 knockdown inhibited GLUT4 translocation in 3T3-L1 adipocytes; ~5% of total Rab10 resides in GLUT4 vesicles isolated from low-density microsomes; ~90% of Rab10 is in the GDP-bound (inactive) state in both basal and insulin-stimulated conditions. |
siRNA knockdown of individual Rab candidates, subcellular fractionation, pull-down GTP-loading assay |
The Biochemical journal |
High |
18076383
|
| 2011 |
Dennd4C is identified as the guanine nucleotide exchange factor (GEF) for Rab10 required for insulin-stimulated GLUT4 translocation; Dennd4C is present in isolated GLUT4 vesicles, and its knockdown markedly inhibits GLUT4 translocation, phenocopying Rab10 knockdown. |
siRNA knockdown, subcellular fractionation, ectopic expression in 3T3-L1 adipocytes |
The Journal of biological chemistry |
High |
21454697
|
| 2012 |
Rab10 directly facilitates GLUT4 storage vesicle (GSV) translocation to and docking at the plasma membrane, as visualized by dual-color TIRF microscopy and IRAP-pHluorin fusion assay; Myosin-Va associates with GSVs by interacting with Rab10, positioning peripherally recruited GSVs for ultimate fusion. Rab14 and Rab4/Rab8 regulate distinct, earlier endosomal recycling steps. |
Dual-color TIRF microscopy, IRAP-pHluorin fusion assay, co-immunoprecipitation, siRNA knockdown |
The Journal of cell biology |
High |
22908308
|
| 2015 |
Rab10 in its GTP-bound form binds to exocyst subunits Exoc6 and Exoc6b; knockdown of either Exoc6 or Exoc6b inhibits insulin-stimulated GLUT4 translocation in 3T3-L1 adipocytes, linking Rab10-GTP to the tethering machinery. |
GTP-Rab10 pulldown, co-immunoprecipitation, siRNA knockdown in 3T3-L1 adipocytes |
Biochemical and biophysical research communications |
Medium |
26299925
|
| 2016 |
SEC16A is a novel RAB10 effector required for insulin-stimulated GLUT4 translocation; SEC16A colocalizes with RAB10 in a perinuclear recycling endosome/TGN compartment, co-localization is augmented by insulin, and SEC16A knockdown phenocopies RAB10 knockdown. RAB10-SEC16A promotes mobilization of GLUT4 from a perinuclear compartment, acting independently of canonical COPII function. |
Co-localization imaging, siRNA knockdown, phenotypic rescue, vesicle fractionation in adipocytes |
The Journal of cell biology |
Medium |
27354378
|
| 2014 |
Rab10 interacts with RalA through recruitment of the Ral-GEF Rlf/Rgl2; active Rab10 increases RalA-GTP levels, and Rab10 and RalA co-reside in GLUT4-storage vesicles. Membrane-tethered Rlf compensates for Rab10 loss in GLUT4 translocation, placing RalA downstream of Rab10 in a G protein cascade governing insulin-stimulated glucose uptake. |
Pulldown assays, GTPase activation assays, rescue by constitutively membrane-targeted Rlf, siRNA knockdown in adipocytes |
Molecular biology of the cell |
Medium |
25103239
|
| 2020 |
The TBC1D4-RAB10 signaling module controls GLUT4 mobilization specifically from a trans-Golgi network (TGN) storage compartment; RAB10 is required for insulin-stimulated release from this intracellular sequestration site, and this function is distinct from copper-elicited ATP7A mobilization from the same TGN domain. |
siRNA/shRNA knockdown, live-cell imaging, cargo-specific stimulation experiments in adipocytes |
Molecular biology of the cell |
Medium |
33175605
|
| 2012 |
Rab10 is an ER-specific Rab GTPase that localizes to dynamic ER-associated structures tracking along microtubules; depletion or GDP-locked Rab10 mutant reduces ER tubules by impairing tubule outgrowth and fusion. Rab10 partitions to leading-edge ER domains enriched in phospholipid synthesis enzymes PIS and CEPT1; GDP-locked Rab10 inhibits formation and function of these Rab10/PIS/CEPT1 domains. |
Live-cell fluorescence microscopy, siRNA knockdown, dominant-negative mutant expression, colocalization with ER markers |
Nature cell biology |
High |
23263280
|
| 2006 |
In C. elegans intestinal epithelial cells, RAB-10 is required for basolateral endocytic recycling upstream of RME-1; rab-10 null mutants accumulate enlarged RAB-5-positive early endosomes, lose RME-1-positive recycling endosomes, and trap basolaterally recycling transmembrane cargo and fluid. GFP-RAB-10 localizes to endosomes and Golgi. |
Null mutant analysis, genetic epistasis, fluorescent reporter localization, cargo trafficking assays in C. elegans intestine |
Molecular biology of the cell |
High |
16394106
|
| 2006 |
In polarized MDCK cells, Rab10 is associated with common/sorting endosomes accessible from both apical and basolateral surfaces; dominant-negative and constitutively active Rab10 mutants increase recycling from basolateral sorting endosomes to common endosomes, without affecting apical recycling or later recycling compartments. |
Quantitative confocal microscopy of GFP-Rab10 mutants, endocytic probe internalization from both surfaces |
Molecular biology of the cell |
High |
16641372
|
| 2006 |
Rab10 localizes to Golgi during early polarization of MDCK cells; 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, indicating functional cooperation. |
GFP-tagged mutant expression, RNAi, immunofluorescence, biosynthetic transport assays in MDCK cells |
Traffic |
High |
17132146
|
| 2010 |
Rab10 regulates continuous replenishment of TLR4 from Golgi to the plasma membrane in macrophages; blockade of Rab10 decreases surface TLR4, diminishes LPS-induced inflammatory cytokine and interferon production, and reduces disease severity in an in vivo LPS-induced acute lung injury model. |
Dominant-negative and siRNA-based Rab10 inhibition, surface TLR4 measurement, cytokine ELISAs, in vivo mouse model |
Proceedings of the National Academy of Sciences of the United States of America |
High |
20643919
|
| 2008 |
Rab10 interacts with myosin Va, Vb, and Vc tails; this interaction requires the alternatively spliced exon D in myosin Va and Vb (and homologous region in Vc). Confirmed by yeast two-hybrid and FRET in vivo; Rab8a and Rab10 are mislocalized by dominant-negative myosin V tails. |
Yeast two-hybrid, FRET, dominant-negative myosin V tail overexpression, colocalization |
The Journal of biological chemistry |
High |
19008234
|
| 2013 |
Myosin Vb interaction with Rab10 (via exon D-encoded domain) determines biogenesis of Rab10-positive post-Golgi carriers; blocking MYO5B-Rab10 interaction impairs fission of Rab10 vesicles from trans-Golgi membranes, reduces transport carrier number, and inhibits axon development in hippocampal neurons and in vivo in vertebrate neocortical neurons and zebrafish retinal ganglion cells. |
Co-immunoprecipitation, dominant-negative constructs, shRNA knockdown, live imaging, in vivo analysis in rat and zebrafish |
Nature communications |
High |
23770993
|
| 2011 |
Lgl1 activates Rab10 by releasing GDP dissociation inhibitor (GDI) from Rab10; Lgl1 associates with plasmalemmal precursor vesicles (PPVs) and is enriched in developing axons. Rab10 lies downstream of Lgl1 in axon development and directional membrane insertion; both are required for neocortical neuronal polarization in vivo. |
Co-immunoprecipitation, GDI release assay, shRNA knockdown, epistasis by rescue, in vivo cortical electroporation |
Developmental cell |
High |
21856246
|
| 2014 |
JIP1 (MAPK8IP1) 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 PPVs during axonal growth; disruption of any component reduces anterograde PPV transport and causes neuronal polarity defects in vitro and in vivo. |
Co-immunoprecipitation, dominant-negative/constitutively active Rab10 variants, shRNA knockdown, live axonal transport imaging, in vivo cortical electroporation |
The Journal of neuroscience |
High |
24478353
|
| 2014 |
MARCKS (myristoylated alanine-rich C-kinase substrate) binds GTP-locked active Rab10 at the plasma membrane, and this interaction depends on the phosphorylation status of the MARCKS effector domain; silencing MARCKS or disrupting its interaction with Rab10 inhibits axonal growth, impairs docking/fusion of Rab10 vesicles with the plasma membrane, and prevents membrane insertion of axonal growth factor receptors. |
Co-immunoprecipitation, dominant-active Rab10 pull-down, shRNA knockdown, TIRF imaging, in vitro and in vivo neuronal assays |
Cell research |
High |
24662485
|
| 1993 |
Epitope-tagged Rab10 expressed in CHO and BHK cells concentrates on membranes in the perinuclear region with partial overlap with the Golgi marker β-COP, distinct from Rab8 which localizes to the cell periphery/ruffling areas, establishing that Rab10 and Rab8 occupy distinct cellular compartments despite 66% sequence identity. |
HA-epitope tagging, immunofluorescence in stably transfected CHO, BHK, and Swiss 3T3 cells |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
7688123
|
| 2010 |
Rab10 co-localizes with exocyst proteins at the base of primary cilia in renal epithelial cells in culture and in vivo, and physically interacts with the exocyst complex detected by anti-Sec8 co-immunoprecipitation, suggesting Rab10 mediates membrane transport to the primary cilium through exocyst interactions. |
Immunofluorescence colocalization, co-immunoprecipitation with anti-Sec8 antibody, in vivo renal tissue analysis |
American journal of physiology. Renal physiology |
Medium |
20576682
|
| 2016 |
LRRK2 directly phosphorylates Rab10 at a conserved threonine residue (Thr73) in the effector-binding switch-II motif; phosphorylation is ablated in kinase-inactive LRRK2[D2017A] knockin cells/tissues, establishing LRRK2 as the major Rab10 kinase; pathogenic mutations G2019S and R1441G increase Rab10 phosphorylation; Ser910/Ser935 phosphorylation of LRRK2 and 14-3-3 binding facilitate Rab10 phosphorylation in vivo. |
Phos-tag electrophoresis, knockin mouse models (kinase-dead and phosphomutant), LRRK2 kinase inhibitor treatment |
The Biochemical journal |
High |
27474410
|
| 2019 |
LRRK2-phosphorylated Rab10 (pT73) accumulates on depolarized mitochondria in a PINK1- and PRKN-dependent manner; Rab10 binds the autophagy receptor OPTN and promotes its accumulation on depolarized mitochondria to facilitate mitophagy. Pathogenic LRRK2 mutations (G2019S, R1441C) enhance Rab10 T73 phosphorylation, impairing Rab10-OPTN interaction and depolarization-induced mitophagy; phosphomimetic Rab10 T73E fails to rescue mitophagy in LRRK2-mutant cells. |
Co-immunoprecipitation, immunofluorescence, CCCP-induced depolarization, LRRK2 knockdown/inhibitor rescue, patient-derived cells |
Autophagy |
High |
30945962
|
| 2019 |
LRRK2-phosphorylated Rab10 is recruited to centrosome-localized RILPL1, causing centrosomal cohesion deficits and ciliogenesis defects; both RAB8 and RAB10 contribute to these defects, which are reverted by LRRK2 kinase inhibition and are observed in patient-derived peripheral cells and primary astrocytes from mutant LRRK2 mice. |
Immunofluorescence, phospho-specific antibodies, LRRK2 kinase inhibition, patient-derived cells, mutant LRRK2 mice |
Human molecular genetics |
High |
31428781
|
| 2021 |
LRRK2 kinase activity decreases the overall probability of ciliation without changing cilia formation rates; pathogenic LRRK2 blocks release of CP110 from the mother centriole by preventing TTBK2 recruitment, requiring both Rab10 and RILPL1. Deciliation probability relies on a distinct LRRK2 pathway independent of Rab10 and RILPL1. |
Live-cell fluorescence microscopy, R1441C LRRK2 MEFs, Rab10 and RILPL1 knockout cells, serum starvation/readdition ciliation assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
33653948
|
| 2021 |
LRRK2-phosphorylated Rab10 sequesters Myosin Va with RILPL2 at the peri-centriolar region; the globular tail domain of Myosin Va contains a high-affinity binding site for LRRK2-phosphorylated Rab10; pathogenic LRRK2 causes phosphoRab10-dependent RILPL2 and MyoVa relocalization to the peri-centriolar region, as confirmed by FLIP microscopy. RILPL2 overexpression blocks ciliogenesis independent of TTBK2 recruitment. |
Co-immunoprecipitation, FLIP (fluorescence loss in photobleaching), phospho-specific pulldown, dominant-active/pathogenic LRRK2 mutants |
Life science alliance |
High |
33727250
|
| 2020 |
Rab10 specifically regulates macropinocytosis in macrophages, dendritic cells, and microglia without affecting phagocytosis or clathrin-mediated endocytosis; 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, stalling macropinosome cargo recycling and promoting PI3K-Akt immunological responses. |
siRNA knockdown in primary mouse and human macrophages/microglia, LRRK2 kinase inhibition, live-cell imaging, EHBP1L1 competitive overexpression |
The EMBO journal |
High |
32853409
|
| 2016 |
Rab10 activity is required for lipophagy (autophagic engulfment of lipid droplets) in hepatocytes; Rab10 is recruited to nascent autophagic membranes at the lipid droplet surface during autophagy. Rab10 activation stimulates its association with EHBP1 and the membrane-deforming ATPase EHD2, forming a complex essential for engulfment of lipid droplets by growing autophagosomes; Rab10 knockdown or GTPase-defective variant causes lipid droplet accumulation and blocks LC3 recruitment. |
siRNA knockdown, GTPase-defective mutant expression, co-immunoprecipitation, immunofluorescence in hepatocytes |
Science advances |
High |
28028537
|
| 2010 |
RAB-10 and the calponin-homology domain protein EHBP-1 function together in endocytic recycling in C. elegans intestinal cells and interneurons; yeast two-hybrid identified EHBP-1 as a RAB-10 binding partner; EHBP-1-GFP colocalizes with RFP-RAB-10 on endosomal structures, and ehbp-1 loss-of-function mutants share specific endosome morphology and cargo localization defects with rab-10 mutants. |
Yeast two-hybrid, colocalization, genetic loss-of-function analysis in C. elegans |
Molecular biology of the cell |
High |
20573983
|
| 2014 |
In C. elegans, RAB-10 cooperates with the exocyst subunit SEC-10 and microtubules to form endosomal tubular networks required for basolateral recycling of clathrin-independent cargoes (hTAC, GLUT1, DAF-4); SEC-10 acts at an intermediate step between early endosomes and recycling endosomes; epistasis analysis places SEC-10 downstream of early endosomes and upstream of recycling endosomes, in a pathway dependent on RAB-10. |
RNAi knockdown, fluorescent cargo tracking, epistasis analysis, electron microscopy in C. elegans intestine |
Proceedings of the National Academy of Sciences of the United States of America |
High |
25301900
|
| 2009 |
Rab10 associates transiently with phagosomal membranes early (before Rab5 acquisition) and regulates phagosome maturation; Rab10 knockdown or dominant-negative expression delays phagosome maturation; constitutively active Rab10 partially rescues maturation of live Mycobacterium-containing phagosomes and enables EEA1 acquisition on normally arrested phagosomes. |
siRNA knockdown, dominant-negative and constitutively active Rab10 mutants, confocal microscopy, live-Mycobacterium infection assays |
Traffic |
High |
20028485
|
| 2013 |
In Drosophila follicle cells, Rab10 is targeted by the DENN-domain protein Crag to structures in the basal cytoplasm, where it restricts secretion of basement membrane proteins to the basal cell surface; Rab10 and Tango1-positive ER exit sites are planar polarized at the basal epithelial surface, coupling BM protein synthesis and polarized secretion to organ morphogenesis. |
Genetic loss-of-function, live imaging, immunofluorescence, epistasis with Crag and Tango1 in Drosophila follicle cells |
Developmental cell |
High |
23369713
|
| 2019 |
Rab10 localizes to tubular endosomes and its knockout completely abolishes tubular endosomal structures in HeLaM cells; Rab10 interacts with kinesin motors KIF13A and KIF13B (identified by in silico screening and validated); both the Rab10-binding homology domain and motor domain of KIF13A are required for Rab10-positive tubular endosome formation. |
CRISPR knockout, in silico screening followed by experimental validation, domain analysis with KIF13A truncations |
Journal of cell science |
High |
30700496
|
| 2021 |
Salmonella effector SopD contains a C-terminal GTPase-activating protein (GAP) domain that directly binds and inhibits Rab10 GTPase; during infection, Rab10 and its effectors MICAL-L1 and EHBP1 are recruited to invasion sites, and SopD-mediated inhibition of Rab10 promotes removal of Rab10 and recruitment of Dynamin-2 to drive plasma membrane scission and Salmonella-containing vacuole formation. |
Biochemical GAP assay, co-immunoprecipitation, infection assays, Dynamin-2 recruitment imaging |
Nature communications |
High |
34349110
|
| 2014 |
Rab10 GTPase mediates endocytosis of hyaluronan synthase HAS3 from the plasma membrane to early endosomes; Rab10 colocalized with HAS3 in intracellular vesicles and was co-immunoprecipitated with HAS3 from isolated endosomes; Rab10 silencing increases plasma membrane HAS3 and HA synthesis, whereas overexpression suppresses HA synthesis; reduced endocytosis of HAS3 enlarges the HA coat and impairs cell adhesion to type I collagen. |
siRNA silencing, overexpression, co-immunoprecipitation from endosomal fractions, HA synthesis assays, cell adhesion assay |
The Journal of biological chemistry |
Medium |
24509846
|
| 2022 |
RAB10 promotes endosomal recycling of the LDL receptor (LDLR) from RAB11-positive endosomes to the plasma membrane in hepatocytes, and also promotes recycling of the transferrin receptor from a distinct RAB4-positive compartment. |
Genome-wide CRISPR screen followed by targeted validation, receptor recycling assays, compartment marker colocalization |
Journal of lipid research |
Medium |
35753407
|
| 2023 |
Rab10 controls sorting of internalized TrkB receptors into signaling endosomes for retrograde axonal transport; Rab10 defines a membrane compartment that is rapidly mobilized toward the axon terminal upon BDNF stimulation, enabling fine-tuning of retrograde signaling from axon to soma. |
Primary mouse neuron cultures, live-cell imaging, BDNF stimulation assays, dominant-active/negative Rab10 mutants, retrograde transport tracking |
eLife |
High |
36897066
|
| 2022 |
Lysosomal positioning regulates Rab10 phosphorylation by LRRK2: pRab10 is restricted to perinuclear lysosomes, and anterograde transport of lysosomes to the cell periphery (via ARL8B/SKIP overexpression or JIP4 knockdown) blocks Rab10 recruitment and phosphorylation. Conversely, clustering lysosomes in the perinuclear area (via RILP overexpression) increases LRRK2-dependent Rab10 phosphorylation. Phosphatase PPM1H knockdown significantly increases pRab10 and lysosomal tubulation. |
LRRK2 lysosome-targeting constructs, ARL8B/SKIP overexpression, RILP overexpression, JIP4 and PPM1H siRNA knockdown, phospho-specific imaging |
Proceedings of the National Academy of Sciences of the United States of America |
High |
36256825
|
| 2022 |
RILPL1 localizes to the subdistal appendage of the mother centriole; LRRK2-phosphorylated Rab10 is recruited to RILPL1 at this location to cause centrosomal cohesion deficits and CDK5RAP2 displacement; centrosomal alterations require GTP-bound and phosphorylated Rab proteins and impair cell polarization (scratch wound assay), reverted by LRRK2 kinase inhibition. |
Transfected cell lines, patient-derived iPS cells, immunofluorescence, dominant/constitutive mutants, scratch wound assay, LRRK2 inhibitor treatment |
Biology open / iScience |
High |
35721463 35776681
|
| 2024 |
VPS13C interacts with phospho-Rab10 (pRab10) as a phospho-dependent interactor on lysosomes in human iPSC-derived 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 in iPSC-derived dopaminergic neurons, VPS13C knockout, phospho-Rab10 pulldown/interaction assays |
The Journal of cell biology |
High |
38358348
|
| 2024 |
Rab10 and Caveolin-1 (CAV1) mark intraluminal vesicles in migrasomes; transport of Rab10-CAV1 vesicles to migrasomes requires the motor protein Myosin Va and adaptor protein RILPL2; LRRK2-mediated phosphorylation of Rab10 regulates this transport. CSF-1 is transported to migrasomes via this mechanism to foster monocyte-macrophage differentiation during wound healing. |
Live-cell imaging, Co-IP, dominant-negative/phosphomimetic Rab10 mutants, LRRK2 kinase inhibition, wound-healing model |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
39008679
|
| 2015 |
RAB-10 in C. elegans controls dendritic branch distribution in the PVD sensory neuron by balancing the activities of molecular motors kinesin-1/UNC-116 and dynein; the exocyst complex cooperates with RAB-10 as a critical regulator of dendrite morphogenesis. |
Genetic loss-of-function, motor mutant epistasis, fluorescent reporter imaging in C. elegans |
PLoS genetics |
Medium |
26633194
|
| 2017 |
RAB-10 promotes autophagic flux in C. elegans by regulating autophagosome formation and maturation, and controls the size of ATG-9-positive structures; GTPase cycling of RAB-10 is required to control ATG-9 foci size. |
RNAi, GFP::LGG-1 and GFP::ATG-9 reporters, chloroquine flux assay, colocalization with lysosome markers in C. elegans |
Autophagy |
Medium |
28872980
|
| 2011 |
In human endothelial cells, Rab10 is enriched at the Golgi and is required for biogenesis of Weibel-Palade bodies (WPB); siRNA-mediated Rab10 suppression significantly reduces rapidly released von Willebrand factor upon secretagogue stimulation, placing Rab10 in WPB biogenesis at the Golgi. |
RNAi in HUVECs, VWF secretion assay, immunofluorescence colocalization with Golgi marker; initial hit identified by genome-wide RNAi screen in C. elegans |
Journal of thrombosis and haemostasis |
Medium |
21070595
|
| 2016 |
Rab10-mediated secretion pathway promotes pericellular basement membrane protein accumulation and fibril formation in Drosophila egg chamber; live imaging and genetic manipulation show BM fibrils are assembled in pericellular spaces and oriented by directed epithelial migration; manipulating the Rab10-based secretion pathway alters BM fibrillar structure and egg chamber morphogenesis. |
Live imaging, genetic loss-of-function, manipulation of secretion pathway in Drosophila |
Developmental cell |
Medium |
27404358
|
| 2015 |
RAB-10 and amphiphysin AMPH-1 bind to RAB-5 GAP TBC-2 and recruit it to endosomes; in the absence of RAB-10 or AMPH-1 binding, RAB-5 membrane association is abnormally high, trapping recycling cargo in early endosomes. This identifies RAB-10/AMPH-1-mediated TBC-2 recruitment as a mechanism for RAB-5 downregulation required for cargo exit from early endosomes. |
Genetic loss-of-function, epistasis, colocalization, cargo trafficking assays in C. elegans |
PLoS genetics |
Medium |
26393361
|
| 2020 |
LRRK2 phosphorylation of Rab10 is potently stimulated by lysosomotropic drugs (lysosomal stressors) through enhanced molecular proximity of LRRK2 and Rab GTPases on the cytosolic surface of LRRK2-coated enlarged lysosomes, downstream of Rab29-mediated LRRK2 activation; this is not due to increased LRRK2 enzymatic activity per se. |
Pharmacological lysosomal stress, proximity ligation, Rab29 epistasis, autophosphorylation assays in cell lines |
Neurobiology of disease |
Medium |
32919031
|
| 2017 |
RAB10 interacts with MGCRABGAP (a male germ cell-specific RabGAP containing a TBC domain) during spermiogenesis; MGCRABGAP exhibits GTPase-activating activity; MGCRABGAP-RAB10 complexes colocalize specifically in the manchette structure of spermatids, a critical structure for spermatid head formation. |
Co-immunoprecipitation, nano LC-MS/MS proteomics, GTPase activity assay, immunofluorescence colocalization |
International journal of molecular sciences |
Medium |
28067790
|
| 2019 |
Activated α2-macroglobulin (α2M*) induces LRP1 recycling to the plasma membrane through a Rab10-dependent exocytic pathway regulated by PI3K/Akt in retinal Müller glial cells; Rab10 knockdown reduces LRP1 accumulation at the plasma membrane and impairs α2M*-induced cell migration. |
siRNA knockdown, receptor trafficking assays, PI3K/Akt inhibition, live imaging in MIO-M1 cells |
Scientific reports |
Medium |
31519919
|