| 1996 |
Rab8 (wild-type and constitutively active Q67L mutant) expression in BHK fibroblasts promotes reorganization of actin filaments and microtubules, leading to formation of cell protrusions and preferential delivery of newly synthesized basolateral marker protein (VSV-G) into these outgrowths, demonstrating a role for Rab8 in linking polarized biosynthetic membrane traffic to cell morphology changes. |
Transient expression and stable cell lines with wild-type and mutant Rab8; VSV-G trafficking assay; fluorescence microscopy of actin and microtubule organization |
The Journal of cell biology |
High |
8858170
|
| 1993 |
Epitope-tagged Rab8, when stably expressed in CHO and Swiss 3T3 cells, localizes to the cell periphery with highest concentration in ruffling areas, distinct from the perinuclear localization of the closely related Rab10, establishing compartment-specific localization for Rab8. |
HA-epitope tagging, stable transfection, immunofluorescence microscopy |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
7688123
|
| 1996 |
Active GTP-bound Rab8 specifically interacts with a murine Rab8-interacting protein (rab8ip/GC kinase), a serine/threonine kinase with autophosphorylation activity, in a GTP-dependent manner; the complex co-immunoprecipitates from transfected cells and both proteins co-localize at the Golgi and basolateral plasma membrane in MDCK cells. |
Yeast two-hybrid screening, co-immunoprecipitation from transfected 293T cells, cell fractionation, immunofluorescence |
Proceedings of the National Academy of Sciences of the United States of America |
Medium |
8643544
|
| 2000 |
Active GTP-bound Rab8 interacts with the coiled-coil protein FIP-2, which also binds Huntingtin; co-expression of FIP-2 and Huntingtin enhances recruitment of Huntingtin to Rab8-positive vesicular structures, linking Rab8-mediated membrane trafficking to Huntingtin function. |
Yeast two-hybrid, co-immunoprecipitation, fluorescence microscopy of co-expressed proteins |
Current biology : CB |
Medium |
11137014
|
| 2001 |
Dominant-negative Rab8 (T22N) expressed in Xenopus rod photoreceptors causes accumulation of tubulo-vesicular structures at the base of the connecting cilium and rapid retinal degeneration, demonstrating that Rab8 is required for docking of rhodopsin-bearing post-Golgi membranes near the ciliary base. |
Transgenic Xenopus laevis expressing GFP-tagged wild-type, constitutively active (Q67L), and dominant-negative (T22N) Rab8; fluorescence microscopy; histology |
Molecular biology of the cell |
High |
11514620
|
| 2002 |
Rabin8 is a Rab8-specific guanine nucleotide exchange factor (GEF) that stimulates nucleotide exchange on Rab8 but not on Rab3A or Rab5; Rabin8 localizes to cortical actin and its expression induces actin remodeling and formation of polarized cell surface domains; dominant-negative Rab8 redistributes Rabin8 from cortical actin to Rab8-specific vesicles. |
Yeast two-hybrid, in vitro GEF activity assays, fluorescence microscopy, co-expression studies |
Molecular biology of the cell |
High |
12221131
|
| 2006 |
Endogenous and ectopic Rab8 associates with macropinosomes that form at ruffling membranes; these fuse into tubules recycled to the leading edge; depletion of Rab8 by RNAi inhibits protrusion formation while promoting cell-cell adhesion and stress fibers; Rab8 colocalizes with Rab11 and Arf6, is functionally linked to Arf6, and specifically binds synaptotagmin-like protein Slp1/JFC1. |
RNAi knockdown, dominant-negative mutant expression, co-localization fluorescence microscopy, binding assays, transferrin trafficking assays |
Journal of cell science |
High |
17105768
|
| 2007 |
Rab8-knockout mice show mislocalization of apical peptidases and transporters to lysosomes in small intestinal enterocytes, shortened microvilli, enlarged lysosomes, and microvillus inclusions, establishing that Rab8 is required for proper apical protein localization in intestinal epithelial cells. |
Rab8-deficient mouse knockout, immunofluorescence, electron microscopy, nutrient absorption assays |
Nature |
High |
17597763
|
| 2006 |
Optineurin interacts with Rab8 and, upon apoptotic stimulus (H2O2), the Rab8 GTPase activity is required for optineurin's translocation from the Golgi to the nucleus; a glaucoma-associated E50K mutant of optineurin loses this ability and compromises mitochondrial membrane integrity. |
Co-immunoprecipitation, fluorescence microscopy, dominant-negative Rab8, apoptosis assays (cytochrome c release) |
The Journal of biological chemistry |
Medium |
16569640
|
| 2008 |
Rab8A and myosin Vb are required for insulin-induced GLUT4 translocation in L6 muscle cells; overexpression of a myosin Vb fragment inhibits insulin-stimulated GLUT4 translocation and alters subcellular distribution of GTP-loaded Rab8A, placing them in a common pathway downstream of AS160. |
siRNA knockdown, overexpression of dominant-negative myosin Vb fragment, GLUT4 translocation assay, immunofluorescence |
American journal of physiology. Cell physiology |
Medium |
18701652
|
| 2007 |
Rab8 (via JRAB/MICAL-L2) specifically mediates transport of E-cadherin to the plasma membrane independently of Rab13; Rab8 and Rab13 compete for binding to JRAB/MICAL-L2 and associate with it at different compartments (perinuclear recycling/storage and plasma membrane respectively) to coordinate AJ and TJ assembly. |
siRNA knockdown, co-immunoprecipitation, Ca²⁺-switch model, fluorescence microscopy |
Molecular biology of the cell |
Medium |
18094055
|
| 2010 |
Rab11-GTP binds directly to Rabin8 and kinetically stimulates its GEF activity toward Rab8; Rab11 enriches at the base of primary cilia and dominant-negative Rab11 or RNAi of Rab11 blocks ciliogenesis, placing Rab11 upstream of Rabin8-Rab8 in a vesicular trafficking cascade required for primary ciliogenesis. |
GEF kinetic assays in vitro, GST pulldown, dominant-negative expression, RNAi, immunofluorescence microscopy |
Proceedings of the National Academy of Sciences of the United States of America |
High |
20308558
|
| 2010 |
Insulin promotes GTP loading of Rab8A in rat L6 muscle cells; Rab8A is activated upstream of Rab13 in response to insulin; both Rab8A and Rab13 are targets of the AS160 GAP activity, and overexpression of Rab8A or Rab13 reverses constitutively active AS160-mediated suppression of surface GLUT4. |
Rab-GTP pull-down activation assay, siRNA knockdown, constitutively active AS160 overexpression, surface GLUT4 quantification |
Proceedings of the National Academy of Sciences of the United States of America |
High |
21041651
|
| 2011 |
Rab8A stably associates with exocytotic vesicles in a Rab6-dependent manner; Rab8A function is required for docking and fusion of exocytotic carriers but not for their budding or motility; Rab8A and ELKS act in the same pathway linked by MICAL3, whose monooxygenase activity is required for vesicle-docking complex remodeling. |
Live-cell imaging of vesicle dynamics, siRNA knockdown, co-localization, dominant-negative constructs, MICAL3 monooxygenase-dead mutant |
Current biology : CB |
High |
21596566
|
| 2012 |
Rabin8 interacts with Sec15 (exocyst subunit) in a conformation-dependent manner enhanced by constitutively active Rab8; Sec15 co-localizes with Rab8 along the primary cilium; inhibition of Sec15 causes ciliogenesis defects, establishing a Rabin8-Rab8-Sec15 interaction that couples Rab8 activation to effector recruitment for ciliary vesicle trafficking. |
Co-immunoprecipitation, immunofluorescence microscopy, constitutively active Rab8 expression, Sec15 siRNA knockdown, ciliogenesis assay |
The Journal of biological chemistry |
High |
22433857
|
| 2012 |
Cdc42 deficiency impairs Rab8a activation and its association with multiple effectors, and prevents Rab8a vesicle trafficking to the midbody, impeding cytokinesis; Rab8a is also required for Cdc42-GTP activity in intestinal epithelium, and haploinsufficiency of both Cdc42 and Rab8a causes abnormal crypt morphogenesis. |
Conditional intestinal epithelium-specific knockout mice, immunofluorescence, Rab8a activation assays, genetic interaction (double haploinsufficiency) |
The Journal of clinical investigation |
High |
22354172
|
| 2012 |
AS160 is the GTPase-activating protein (GAP) for Rab8a; AS160 forms a ternary complex with Fsp27 and Rab8a; GDP-bound Rab8a (inactivated by AS160) promotes lipid droplet fusion; MSS4 (a GEF) antagonizes this activity through Rab8a, establishing an AS160-Rab8a-MSS4 regulatory circuit controlling lipid droplet fusion. |
In vitro GAP activity assays, co-immunoprecipitation, pulldown, lipid droplet fusion assays in adipocytes, siRNA knockdown in ob/ob mouse livers |
Developmental cell |
High |
25158853
|
| 2012 |
AS160 mediates insulin- and AMPK-stimulated surface translocation of CD36 in cardiomyocytes; Rab8a GTPase specifically mediates CD36 membrane recruitment upon insulin/AICAR stimulation, established by overexpression and knockdown studies. |
AS160 overexpression and siRNA knockdown, Rab8a overexpression and knockdown, surface CD36 quantification by immunofluorescence and flow cytometry |
Journal of lipid research |
Medium |
22315395
|
| 2012 |
Optineurin acts as an adaptor to bring together Rab8 and its GAP TBC1D17; TBC1D17 catalytic activity inhibits Rab8-mediated endocytic recycling of transferrin receptor by preventing Rab8 recruitment to endocytic recycling tubules; the glaucoma-associated E50K optineurin mutant causes enhanced inhibition of Rab8 by TBC1D17. |
Co-immunoprecipitation, siRNA knockdown, dominant-negative and catalytic-dead mutants, fluorescence microscopy of transferrin receptor trafficking |
Journal of cell science |
High |
22854040
|
| 2013 |
Rab8a-knockout mice (single and double with Rab8b) show mislocalization of apical markers to lysosomes; Rab8a and Rab8b have compensatory roles in apical transport but do not significantly affect basolateral/dendritic transport; additional knockdown of Rab10 in double-KO cells greatly reduces ciliated cells, indicating Rab8a/b and Rab10 cooperate for ciliogenesis. |
Single and double knockout mice, immunofluorescence, electron microscopy, Rab10 siRNA in double-KO cells, ciliation quantification |
Journal of cell science |
High |
24213529
|
| 2013 |
Rab8A directly interacts with PI3Kγ through PI3Kγ's Ras-binding domain; Rab8a recruits PI3Kγ to LPS-induced dorsal ruffles on macrophages to regulate Akt/mTOR signaling downstream of surface TLR4, biasing cytokine output to suppress inflammation. |
Co-immunoprecipitation, GST pulldown with PI3Kγ Ras-binding domain, CRISPR/siRNA knockdown, cytokine measurement, phospho-Akt assays |
Nature communications |
High |
25022365
|
| 2013 |
Rab8a regulates LDL cholesterol recycling to the plasma membrane: NPC1 is required to recruit Rab8a to cholesterol-containing late endosomes; Rab8a and Myosin5b cooperate to dock cholesterol-containing carriers to cortical actin near focal adhesions; Rab8a-dependent cholesterol delivery stimulates cell migration. |
BODIPY-cholesterol live cell imaging, siRNA knockdown of Rab8a/NPC1/Myo5b, immunofluorescence, migration assays |
Developmental cell |
High |
24209575
|
| 2013 |
Structural snapshots of the complete nucleotide exchange reaction of Rab8 catalyzed by Rabin8/GRAB were obtained, including ternary Rab8·GEF·GDP, binary nucleotide-free Rab8·GEF, and ternary Rab8·GEF·GTP complexes, providing mechanistic detail of GEF-catalyzed nucleotide exchange. |
X-ray crystallography and enzymatic kinetic characterization of exchange intermediates |
The Journal of biological chemistry |
High |
24072714
|
| 2014 |
MyoVa is an effector of Rab8A in insulin-stimulated GLUT4 vesicle exocytosis in muscle cells; the MyoVa cargo-binding C-terminal tail binds preferentially to GTP-locked Rab8A in an insulin- and PI3K-dependent manner; MyoVa-CT overexpression and MyoVa siRNA both inhibit insulin-stimulated GLUT4 surface translocation. |
GST pulldown assays, co-localization fluorescence microscopy, TIRF microscopy, siRNA knockdown, dominant-negative MyoVa-CT overexpression |
Molecular biology of the cell |
High |
24478457
|
| 2014 |
MYO5B (myosin Vb) uncoupling from RAB8A (and RAB11A) elicits microvillus inclusion disease phenotype; microvilli establishment requires interaction between RAB8A and MYO5B; loss of RAB8A–MYO5B interaction leads to loss of microvilli while loss of RAB11A–MYO5B interaction induces microvillus inclusions. |
Stable MYO5B knockdown in CaCo2-BBE cells, expression of MVID-associated MYO5B-P660L mutant, surface biotinylation, dual immunofluorescence |
The Journal of clinical investigation |
High |
24892806
|
| 2015 |
Rab8a mediates anterograde transport of Gpr177 (wntless, the Wnt-specific transporter); Gpr177 binds Rab8a, and depletion of Rab8a compromises Gpr177 trafficking and Wnt secretion, reducing Wnt/β-catenin signaling, severely impairing Paneth cell maturation, and decreasing plasma membrane localization of Gpr177. |
Co-immunoprecipitation, Rab8a knockout mouse intestinal organoids, immunogold electron microscopy, surface protein biotinylation, Wnt signaling reporter assays |
Development (Cambridge, England) |
High |
26015543
|
| 2015 |
GSK3β phosphorylates Dzip1 at S520 in G0 phase, increasing Dzip1 binding to GDI2 and promoting release of Rab8-GDP at the cilium base; Dzip1 preferentially binds Rab8-GDP and promotes its dissociation from GDI2 at the pericentriolar region; loss of Dzip1 causes failed ciliary localization of Rab8, establishing a GSK3β-Dzip1-Rab8 cascade regulating post-mitotic ciliogenesis. |
In vitro phosphorylation assay, FRET, immunoprecipitation, sucrose gradient centrifugation of basal bodies, mass spectrometry phosphopeptide identification, GST pulldown, shRNA knockdown |
PLoS biology |
High |
25860027
|
| 1998 |
Rab8, which ends in a CVLL motif, can be prenylated by either GGTaseII (REP-dependent) or GGTaseI (REP-independent) in cell-free assays; in vivo labeling experiments show GGTaseII is the predominant enzyme for Rab8 prenylation in human cells, as a REP-binding-deficient Rab8 Y78D mutant shows ~60-70% reduced prenylation. |
Cell-free prenylation assays, metabolic [³H]mevalonate labeling, GGTaseI inhibitor GGTI-298 treatment, REP-binding-deficient mutant Y78D |
The Biochemical journal |
High |
9677305
|
| 2016 |
EHBP1L1 directly binds GTP-loaded Rab8 and Bin1; EHBP1L1-Bin1-dynamin complex at the endocytic recycling compartment is required for apical (but not basolateral) protein transport; EHBP1L1-deficient mice show truncated microvilli in small intestine, establishing EHBP1L1 as a Rab8 effector for apical transport. |
Co-immunoprecipitation, GST pulldown, knockdown in intestinal organoids, EHBP1L1 knockout mice, immunofluorescence |
The Journal of cell biology |
High |
26833786
|
| 2016 |
GRAF1-mediated clathrin-independent endocytosis removes active Rab8 from the plasma membrane at protrusions; GRAF1 depletion leads to elevated GTP-loaded Rab8 accumulated at static protrusion tips and impairs multi-directional spreading and 3D lumen formation, indicating that endocytic turnover of Rab8 controls cell polarization. |
GRAF1 siRNA knockdown, Rab8-GTP level measurement, live-cell imaging, 3D culture lumen assay |
Journal of cell science |
Medium |
28137756
|
| 2018 |
LRRK2 phosphorylates Rab8a at T72 in its switch II domain; pathogenic LRRK2 mutations increase centrosomal localization of phospho-Rab8a, causing centrosomal cohesion deficits and polarity defects; these defects are mimicked by co-expression of wild-type LRRK2 with wild-type but not phospho-deficient Rab8a, and are reversed by LRRK2 kinase inhibition or Rab8a RNAi. |
In vitro kinase assays, co-immunoprecipitation, GTP binding/retention assays, immunofluorescence, siRNA, patient-derived peripheral cells, SH-SY5Y stable cell lines |
Molecular neurodegeneration |
High |
29357897
|
| 2018 |
TLR activation of LRP1 results in LRP1 phosphorylation at Y4507, which allows LRP1 to activate and recruit Rab8a together with the PI3Kγ p110γ/p101 effector complex on macropinosomal membranes; in LRP1-deficient cells, TLR-induced Rab8a activation is abolished, altering Akt/mTOR signaling and producing a pro-inflammatory cytokine bias. |
CRISPR knockout of LRP1, co-immunoprecipitation, phospho-LRP1 analysis, Rab8a activation assay, cytokine measurement |
Cell reports |
High |
30208326
|
| 2019 |
Pathogenic LRRK2 G2019S expression or loss of RAB8A both impair endolysosomal trafficking and EGFR degradation, causing EGFR accumulation in a RAB4-positive compartment with deficits in recycling; up-regulation of the RAB11-Rabin8-RAB8A cascade or expression of active/phosphodeficient RAB8A variants rescue G2019S LRRK2-mediated trafficking defects, placing RAB8A downstream of LRRK2 in endolysosomal regulation. |
Immunofluorescence, pulldown assays, RAB8A siRNA knockdown, dominant-negative and constitutively active RAB8A variants, EGFR trafficking assay |
The Journal of biological chemistry |
Medium |
30709905
|
| 2019 |
RAB8 and RAB10 both contribute to LRRK2-mediated centrosomal cohesion deficits and ciliogenesis defects; pathogenic LRRK2 causes centrosomal accumulation of both phospho-RAB8 and phospho-RAB10, and both effects are dependent on RILPL1; these defects are observed in patient-derived peripheral cells and primary astrocytes from mutant LRRK2 mice. |
Immunofluorescence in patient-derived cells, primary LRRK2 mouse astrocytes, LRRK2 kinase inhibitor treatment, phospho-RAB8/RAB10 detection |
Human molecular genetics |
High |
31428781
|
| 2020 |
Crystal structure of phospho-Rab8a (pT72) in complex with the RH2 domain of RILPL2 reveals a heterotetramer where RILPL2 forms an X-shaped α-helical dimer bridging two pRab8a molecules; conserved Arg residues in the RILPL2 X-cap orient toward pT72; similar X-cap residues in JIP3 and JIP4 also interact with LRRK2-phosphorylated Rabs, defining a general recognition mode for phospho-Rab GTPases. |
X-ray crystallography, structure-function mutagenesis, biochemical binding assays |
Structure (London, England : 1993) |
High |
32017888
|
| 2020 |
Cryo-EM structure of the C9ORF72-SMCR8-WDR41 complex shows that SMCR8 Arg147 acts as an arginine finger analogous to FLCN, and biochemical assays demonstrate GAP activity of the C9ORF72-SMCR8 complex toward Rab8a and Rab11a. |
Cryo-EM structure at 3.2 Å, biochemical GAP activity assays, Arg147 mutagenesis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32303654
|
| 2020 |
The bMERB domain of EHBP1 forms an intramolecular auto-inhibitory complex with the central calponin homology (CH) domain, preventing actin binding; Rab8 family member binding to bMERB relieves this inhibition and frees the CH domain to interact with actin, promoting membrane tubulation. Crystal structures of the auto-inhibited CH:bMERB and active bMERB:Rab8 complexes were determined. |
X-ray crystallography, biochemical binding assays, actin sedimentation assays, structure-based mutagenesis |
Nature communications |
High |
32826901
|
| 2021 |
Salmonella effector SopD has GAP activity for Rab8 (inhibiting Rab8 and stimulating inflammation) and also activates Rab8 by displacing it from its GDI (suppressing inflammation); the crystal structure of SopD bound to Rab8 at 2.3 Å reveals a unique contact interface underlying these dual activities. |
GAP activity assay, GDI displacement assay, crystal structure at 2.3 Å, Salmonella infection models |
Nature microbiology |
High |
33603205
|
| 2021 |
LRRK2 gain-of-function mutations induce sequestration of Rab8a to lysosomes in cells; pharmacological inhibition of LRRK2 kinase activity reverses this lysosomal sequestration; LRRK2 mutations drive co-association of endocytosed transferrin with Rab8a-positive lysosomes, and iPSC-derived microglia from LRRK2 G2019S patients mistraffic transferrin to lysosomes, altering iron uptake. |
LRRK2 kinase inhibitor treatment, immunofluorescence, transferrin trafficking assay, iPSC-derived microglia, G2019S knock-in mice with LPS challenge |
PLoS biology |
Medium |
34914695
|
| 2023 |
Rab8a acts as a mitochondrial receptor for lipid droplets in skeletal muscle, forming a tethering complex with LD-associated PLIN5; AMPK increases GTP-bound Rab8a upon starvation, promoting LD-mitochondrion interaction; the Rab8a-PLIN5 complex recruits ATGL to couple fatty acid mobilization from LDs with mitochondrial β-oxidation; Rab8a deficiency impairs fatty acid utilization and decreases exercise endurance in mice. |
Co-immunoprecipitation, LD-mitochondrion proximity assay, AMPK activation, Rab8a KO mouse exercise model, ATGL recruitment assay |
Developmental cell |
High |
36800997
|
| 2010 |
Rab8 interacts with distinct motifs in the C-termini of α2B- and β2-adrenergic receptors via GST pulldown and co-immunoprecipitation; GDP-bound Rab8(T22N) arrests α2B-AR but not β2-AR in the trans-Golgi network and attenuates ERK1/2 activation by α2B-AR; knockdown of Rab8 more potently inhibits α2B-AR cell surface expression. |
Co-immunoprecipitation, GST fusion protein pulldown, dominant-negative Rab8, shRNA knockdown, ERK1/2 activation assay, receptor surface expression quantification |
The Journal of biological chemistry |
Medium |
20424170
|
| 2012 |
Optineurin mediates the interaction between Rab8 and TBC1D17 (a RabGAP); a non-catalytic region of TBC1D17 interacts directly with optineurin; through catalytic activity, TBC1D17 inhibits Rab8 recruitment to endocytic recycling tubules and impairs transferrin receptor recycling; a glaucoma-associated optineurin mutant E50K causes enhanced inhibition of Rab8 by TBC1D17. |
Co-immunoprecipitation, GST pulldown, siRNA knockdown, dominant-negative constructs, transferrin receptor trafficking assay, fluorescence microscopy |
Journal of cell science |
High |
22854040
|
| 2011 |
DCDC5 interacts with cytoplasmic dynein, Rab8, and Rabin8; DCDC5 knockdown impairs entry of Golgi-derived Rab8-positive vesicles to the midbody and increases multinucleated cells, demonstrating that DCDC5 mediates dynein-dependent transport of Rab8-positive vesicles during cytokinesis. |
Co-immunoprecipitation, RNAi knockdown, live-cell imaging of Rab8 vesicles, mitosis/cytokinesis quantification |
Journal of cell science |
Medium |
22159412
|
| 2014 |
LAX binds active GTP-bound Rab8 via its N-terminus and also binds the cytoplasmic tail of CTLA-4; TRIM requires LAX for Rab8 binding; together they form a CTLA-4/TRIM/LAX/Rab8 complex; disruption of LAX/Rab8 binding reduces CTLA-4-containing vesicle numbers near the TGN and decreases CTLA-4 surface expression on T cells. |
Co-immunoprecipitation, siRNA knockdown of LAX and Rab8, surface CTLA-4 quantification, vesicle counting by fluorescence microscopy |
Molecular and cellular biology |
Medium |
24515439
|
| 2016 |
Rab8 activation induces Rac1/Tiam1-mediated cortical actin polymerization and RhoA-dependent stress fiber disassembly; Rab8 promotes focal adhesion disassembly in a microtubule-, calpain-, and MT1-MMP-dependent manner; Rab8 is required for EGF-induced cell polarization and chemotaxis. |
High-content fluorescence microscopy analysis, Rac1/RhoA activity assays, Rab8 depletion/activation, inhibitor studies (calpain, MT1-MMP), chemotaxis assays |
Journal of cell science |
Medium |
26940916
|
| 2017 |
TMEM230 depletion inhibits Rab8a-mediated secretory vesicle trafficking, impairs extracellular secretion of p62 and lysosomal hydrolases, disrupts retromer cargo CI-M6PR trafficking, and impairs autophagic cargo degradation; LRRK2 knockdown similarly impairs these Rab8a-dependent functions. |
siRNA knockdown of TMEM230 and LRRK2, secretion assays, immunofluorescence, retromer localization |
Human molecular genetics |
Medium |
28115417
|
| 2019 |
RAB8A GTPase localizes to the spindle periphery and cortex in mouse oocytes; RAB8A depletion decreases cytoplasmic and cortical actin filaments, causing spindle migration defects, polar body extrusion failure, and Golgi distribution disruption; RAB8A promotes actin assembly through the ROCK-LIMK signaling pathway and interacts with Golgi marker GM130. |
Confocal microscopy, RAB8A morpholino/siRNA depletion, mass spectrometry, co-immunoprecipitation with GM130, ROCK inhibitor, actin quantification |
Biology of reproduction |
Medium |
30285101
|
| 2009 |
Rab8 depletion in primary human macrophages decreases the fraction of ABCA1 at the plasma membrane and inhibits efflux of lipoprotein-derived endosomal cholesterol to apoA-I; Rab8 overexpression increases ABCA1 protein levels and reduces cholesterol deposition, establishing Rab8 as a regulator of ABCA1 surface delivery and cholesterol efflux. |
Adenoviral overexpression, siRNA knockdown, ABCA1 surface localization quantification, cholesterol efflux assay to apoA-I |
Arteriosclerosis, thrombosis, and vascular biology |
Medium |
19304576
|
| 2012 |
EPI64's RabGAP domain has GAP activity toward Rab8a; EPI64 binds JFC1 (Slp1, an effector of Rab8a-GTP) via its C-terminal region; EPI64 expression lowers Rab8-GTP levels and coexpression of Rab8a suppresses EPI64-induced vacuole formation, suggesting that EPI64 recruits Rab8a-GTP via JFC1 for deactivation. |
Co-localization, co-immunoprecipitation, Rab8-GTP level assay, mutant EPI64 lacking GAP activity, Rab8a co-expression rescue |
Molecular biology of the cell |
Medium |
22219378
|
| 2013 |
Rab8 interacts with the C-terminal tail of mGluR1a in an agonist-dependent manner; Rab8 expression attenuates mGluR1a-mediated inositol phosphate formation and calcium release in a PKC-dependent manner while increasing mGluR1a cell surface expression by decreasing receptor endocytosis. |
Co-immunoprecipitation, dominant-negative/constitutively active Rab8, inositol phosphate assay, calcium imaging, surface receptor quantification |
The Journal of neuroscience : the official journal of the Society for Neuroscience |
Medium |
23175844
|
| 2013 |
Slp4 interacts with Rab8 preferentially in its GTP-bound form via the Slp-homology domain; Slp4 and Rab8 colocalize at the plasma membrane in transfected cells and in the center of activated platelets; both Slp4 and Rab8 enhance dense granule release and the Slp4 effect is dependent on Rab8 binding. |
GST pulldown, co-immunoprecipitation, live microscopy, permeabilized platelet secretion assay |
Journal of thrombosis and haemostasis : JTH |
Medium |
23140275
|