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Rab8a is phosphorylated by LRRK2.Phosphorylation of Rab8a plays important role in the fusion and enlargement of lipid droplets.
C9ORF72 (Montrer C9ORF72 Protéines) causes suboptimal autophagy
GRAF1 (Montrer ARHGAP26 Protéines)-mediated removal of Rab8 from the cell surface restricts its activity during protrusion formation, thereby facilitating dynamic adjustment of the polarity axis.
the TNPO1 (Montrer TNPO1 Protéines)-Rab8-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
Ectopic expression of an N-terminal-truncated ARHGEF10 (Montrer ARHGEF10 Protéines) mutant led to the generation of large vesicle-like structures containing both Rab6 (Montrer RAB6A Protéines) and Rab8.
report the design of a bioavailable StRIP3 analogue that harbors two hydrophobic cross-links and exhibits increased binding affinity, combined with robust cellular uptake and extremely high proteolytic stability. Localization experiments reveal that this double-stapled peptide and its target protein Rab8a accumulate in the same cellular compartments
knockdown of another Parkinson's disease (PD) gene, LRRK2, which phosphorylates Rab8a, similarly impairs retromer trafficking, secretory autophagy and Golgi-derived vesicle secretion, thus demonstrating converging roles of two PD genes TMEM230 and LRRK2 on Rab8a function, and suggesting that retromer and secretory dysfunction play an important role in PD pathogenesis.
Rab8 can induce Rac1- and Tiam1 (Montrer TIAM1 Protéines)-dependent cortical actin polymerization and focal adhesion disassembly through the proteases MT1-MMP (Montrer MMP14 Protéines) and calpain, and Rho-GTPase (Montrer RACGAP1 Protéines)-dependent mechanisms
Data demonstrate that EHBP1L1 links Rab8 and the Bin1 (Montrer BIN1 Protéines)-dynamin (Montrer DNM1 Protéines) complex, which generates membrane curvature and excises the vesicle at the endocytic recycling compartment for apical transport.
Further exploration of the NINL-associated interactome identifies MICAL3 (Montrer MICAL3 Protéines), a protein known to interact with Rab8 and to play an important role in vesicle docking and fusion.
Results support participation of Rab8 in OCV trafficking and identify a novel role for the TZ protein Cc2d2a in fusion of incoming ciliary-directed vesicles, through organization of the vesicle fusion machinery at the periciliary membrane.
Cc2d2a, localized at the photoreceptor connecting cilium/transition zone, facilitates protein transport through a role in Rab8-dependent vesicle trafficking and fusion.
Data show that elipsa (Montrer TRAF3IP1 Protéines) encodes a coiled-coil polypeptide that localizes to cilia, and that it interacts genetically with Rabaptin5, a well-studied regulator of endocytosis, which in turn interacts with Rab8, a small GTPase (Montrer RACGAP1 Protéines), known to localize to cilia.
Disruption of Rab8a and Rab11a (Montrer RAB11A Protéines) causes formation of basolateral microvilli in neonatal enteropathy.
The small GTPase (Montrer RACGAP1 Protéines) Rab8a regulates lipid uptake and storage in skeletal muscle.
Rab8a and Rab11a (Montrer RAB11A Protéines) Are Dispensable for Rhodopsin (Montrer RHO Protéines) Transport in Mouse Photoreceptors
With CRISPR/Cas9-mediated gene editing to stably knock out and recover Rab8a in macrophage cell lines, this study matches Akt (Montrer AKT1 Protéines) signaling profiles with cytokine outputs, confirming that Rab8a is a novel regulator of the Akt (Montrer AKT1 Protéines)/mammalian target of rapamycin (mTOR (Montrer FRAP1 Protéines)) pathway downstream of multiple Toll (Montrer TLR4 Protéines)-like Receptors.
these results indicate an indispensable role for Rab8A in insulin (Montrer INS Protéines)-regulated GLUT4 (Montrer SLC2A4 Protéines) trafficking in C2C12 cells.
Results highlight a novel role of Rab8, downstream of IFT20, in the pathway that regulates T cell receptor (TCR) recycling, through recruiting VAMP-3 and promoting the fusion with the synaptic membrane of endosomes carrying TCR cargoes.
The small GTPase (Montrer RACGAP1 Protéines) Rab8 interacts with VAMP-3 (Montrer VAMP3 Protéines) to regulate the delivery of recycling T-cell receptors to the immune synapse.
Rab8a thus controls Wnt (Montrer WNT2 Protéines) delivery in producing cells and is crucial for Paneth cell maturation.
Rab8a acts as an activator of Fsp27 (Montrer CIDEC Protéines)-mediated LD fusion and growth.
The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all the RAS proteins. The putative effector-binding site of this protein is similar to that of the RAB/YPT proteins. However, this protein contains a C-terminal CAAX motif that is characteristic of many RAS superfamily members but which is not found in YPT1 and the majority of RAB proteins. Although this gene was isolated as a transforming gene from a melanoma cell line, no linkage between MEL and malignant melanoma has been demonstrable. This oncogene is located 800 kb distal to MY09B on chromosome 19p13.1.
, hematopoietic SH2 domain containing
, ras-related protein Rab-8A
, RAB8A, member RAS oncogene family
, member RAS oncogene family
, Ras-related protein Rab-8A
, mel transforming oncogene (RAB8 homolog)
, mel transforming oncogene (derived from cell line NK14)
, mel transforming oncogene (derived from cell line NK14)- RAB8 homolog
, oncogene c-mel
, ras-associated protein RAB8
, RAB8, member RAS oncogene family
, cell line NK14 derived transforming oncogene