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We demonstrated that deficiency of GCase(GBA1) leads to a reduction of C18-ceramide species and altered intracellular localization of Rab8a, a small GTPase implicated in secretory autophagy, that contributed to impaired secretion of a-synuclein and accumulation of intracellular a-synuclein.
Our findings reveal a new function of LRRK2 mediated by Rab8a phosphorylation and related to various centrosomal defects.
Rab8a is phosphorylated by LRRK2.Phosphorylation of Rab8a plays important role in the fusion and enlargement of lipid droplets.
C9ORF72 causes suboptimal autophagy
GRAF1-mediated removal of Rab8 from the cell surface restricts its activity during protrusion formation, thereby facilitating dynamic adjustment of the polarity axis.
the TNPO1-Rab8-ciliary targeting signals complex mediates selective entry into and retention of cargos within cilia.
Ectopic expression of an N-terminal-truncated ARHGEF10 mutant led to the generation of large vesicle-like structures containing both Rab6 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-dependent cortical actin polymerization and focal adhesion disassembly through the proteases MT1-MMP and calpain, and Rho-GTPase-dependent mechanisms
Data demonstrate that EHBP1L1 links Rab8 and the Bin1-dynamin 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, a protein known to interact with Rab8 and to play an important role in vesicle docking and fusion.
The small GTPase Rab8 interacts with VAMP-3 to regulate the delivery of recycling T-cell receptors to the immune synapse.
the role of Rabin8 (a mammalian ortholog of Sec2p) with Rab8-nucleotide-exchange factor activity in autophagy in mammalian cells, was examined.
DLC3 is recruited to Rab8-positive membrane tubules and is required for the integrity of the Rab8 and Golgi compartments.
Rab8A GTPase Ser(111) phosphorylation is not directly regulated by PINK1 in vitro and demonstrate in cells the time course of Ser(111) phosphorylation of Rab8A, 8B and 13 is markedly delayed compared to phosphorylation of Parkin at Ser(65).
Intercellular transfer of transferrin receptor by a contact-, Rab8-dependent mechanism involving tunneling nanotubes.
High expression of RAB8A is associated with endometrial cancer.
Study established a direct interaction between alpha-synclein and Rab8a and provided unique insights into the molecular mechanisms of alpha-synclein toxicity
Rab8a and Drebrin E act as key proteins in the regulation of apical trafficking in intestinal epithelial cells.
While localization of the small GTPase Rab8a, which plays an important role in basal body docking, appears unaffected in talpid3-/- photoreceptors, overexpression of constitutively active Rab8a rescues outer segment formation, indicating that the role of Ta3 in early ciliogenesis lies upstream of Rab8a activation in photoreceptors.
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 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, known to localize to cilia.
Disruption of Rab8a and Rab11a causes formation of basolateral microvilli in neonatal enteropathy.
The small GTPase Rab8a regulates lipid uptake and storage in skeletal muscle.
Rab8a and Rab11a Are Dispensable for Rhodopsin 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 signaling profiles with cytokine outputs, confirming that Rab8a is a novel regulator of the Akt/mammalian target of rapamycin (mTOR) pathway downstream of multiple Toll-like Receptors.
these results indicate an indispensable role for Rab8A in insulin-regulated GLUT4 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.
Rab8a thus controls Wnt delivery in producing cells and is crucial for Paneth cell maturation.
Rab8a acts as an activator of Fsp27-mediated LD fusion and growth.
Simultaneous loss of Rab8a and Rab8b has little effect on ciliogenesis, whereas additional loss of Rab10 greatly affects ciliogenesis.
acidosis-induced NBCe1-A, but not NBCe1-B/C, trafficking is mediated by Rab8a.
AS160 and Rab8a regulate membrane recruitment of CD36.
Cdc42 and Rab8a are critical for intestinal stem cell division, survival, and differentiation in mice
Rab8a colocalizes with IL-1b and LC3 and controls IL-1b secretion
Rab13 and Rab8A are Rab-GTPases activated by insulin and downstream of AS160 they regulate traffic of GLUT4 vesicles.
These results suggest that the interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions.
GLUT4 vesicle recruitment and fusion are differentially regulated by Rac, AS160, and Rab8A in muscle cells.
Ahi1 is required for Rab8a localization, ciliogenesis and vesicle trafficking.
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