• The crystal structure of Rab3A in the active configuration or bound to Rabphillin has been determined (19, 50) and Rab3D has been fit to the same model with 6 β-strands and 5 α-helices (45). (pancreapedia.org)
  • Rab3 GEP was purified from brain and acted on Rab3A, 3C and 3D (72). (pancreapedia.org)
  • The second Rab3 GEF, known as GRAB, interacts with inositol hexakisphosphate kinase and Rab3A and its protein expression is primarily in brain (41). (pancreapedia.org)
  • Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene. (wikipedia.org)
  • The different secretory processes are controlled by corresponding Rab proteins including Rab3A/B/C/D, Rab26, Rab27A/B and Rab37. (oncotarget.com)
  • Because of its potential importance in acinar cell digestive enzyme secretion Rab3 is an important subject for review. (pancreapedia.org)
  • Because of its localization and homology to the yeast protein Sec4, it was believed to play a role in the terminal steps of secretion. (pancreapedia.org)
  • Rab3 isoforms have been identified in different tissues and cell types where it has been suggested to play a role in secretion (Table 1). (pancreapedia.org)
  • Note that in some cases Rab3 inhibits and in others it stimulates secretion. (pancreapedia.org)
  • As a secretory small GTPase, Rab3D is a vital regulator for protein secretion. (oncotarget.com)
  • The latter is used for the addition of two geranylgeranyl groups to the cysteine residues which attach the Rab3 to membranes (35). (pancreapedia.org)
  • There are no known GEFs specific for individual Rab3 isoforms such as Rab3D. (pancreapedia.org)
  • We detected protein levels of Rab3D in nine cancer cell lines and twelve types of clinical cancer specimens. (oncotarget.com)
  • Rab3 was originally identified in brain and shown to be localized to synaptic vesicles (24). (pancreapedia.org)
  • Rab3 GEP knockout mice die at birth and embryonic synaptic transmitter release is impaired (64). (pancreapedia.org)
  • Structurally, Rab3 species contain conserved functional domains similar to other Rabs. (pancreapedia.org)
  • Rab proteins constitute the largest family of Ras-related small G proteins and play a role in regulating the specificity of membrane trafficking (63, 78). (pancreapedia.org)
  • These include four regions participating in guanine nucleotide binding, and effector region corresponding to the effector region in Ras, and a CXC prenylation motif at the C-terminal (45). (pancreapedia.org)
  • Subsequent molecular cloning revealed four members of the Rab3 family termed 3A (the form originally found in brain), 3B, 3C, and 3D. (pancreapedia.org)
  • There is no known specific Rab3 GDI, but rather a common family of Rab GDI isoforms which bind prenylated Rabs in the cytoplasm and participates in insertion and removal from membranes (75). (pancreapedia.org)
  • Rab3 GEP is identical to the human DENN/MADD protein and contains a death domain which can bind the TNFR1 (15). (pancreapedia.org)
  • The structure of the Rabs changes upon binding GTP and mutant Rab3 species have been described similar to Ras that are locked into active and inactive configurations (6). (pancreapedia.org)
  • We found that septin 2 protein levels were upregulated and colocalized strongly with CFTR in cystic cells. (bvsalud.org)
  • Application of VX-809, the CFTR corrector, restored CFTR and PC2 toward normal in the cilia, decreased the protein levels of septin 2, and drastically reduced septin 2 colocalization with CFTR. (bvsalud.org)
  • A single form of Rab3 exists in C. elegans and is believed to play a role in neurotransmitter release (47), while in sea urchin eggs a Rab3 is believed to play a role in cortical granule exocytosis (13). (pancreapedia.org)
  • Rab3B and 3 D have been found in exocrine, endocrine, epithelial and adipose cells (60). (pancreapedia.org)
  • In this study, we report that the GTP-binding protein Septin 2 interacts with Cyclophilin A. We highlight a dynamic series of Septin 2 phenotypes at the midbody, previously undescribed in human cells. (bvsalud.org)
  • Affinity enrichment mass spectrometry revealed that the primary ciliogenesis regulator, RILPL1 specifically interacts with the LRRK2-phosphorylated forms of Rab8A and Rab10, whereas RILPL2 binds to phosphorylated Rab8A, Rab10, and Rab12. (elifesciences.org)
  • A single form of Rab3 exists in C. elegans and is believed to play a role in neurotransmitter release (47), while in sea urchin eggs a Rab3 is believed to play a role in cortical granule exocytosis (13). (pancreapedia.org)
  • Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. (nih.gov)
  • Rab3B and 3 D have been found in exocrine, endocrine, epithelial and adipose cells (60). (pancreapedia.org)
  • Similar to other small G proteins, the guanine binding state of Rab3 proteins is regulated by guanine nucleotide exchange proteins or factors (GEPs or GEFs) and GTPase activating proteins (GAPs). (pancreapedia.org)
  • This gene encodes the catalytic subunit of a Rab GTPase activating protein. (nih.gov)
  • Because of its localization and homology to the yeast protein Sec4, it was believed to play a role in the terminal steps of secretion. (pancreapedia.org)
  • Ras-related protein Rab-3B is a protein that in humans is encoded by the RAB3B gene. (wikipedia.org)
  • Rab3 GEP knockout mice die at birth and embryonic synaptic transmitter release is impaired (64). (pancreapedia.org)
  • Subsequent molecular cloning revealed four members of the Rab3 family termed 3A (the form originally found in brain), 3B, 3C, and 3D. (pancreapedia.org)
  • Because of the presence of multiple forms of Rab3 in neuronal cells, the group of T. Sudhof prepared a mouse model in which all four isoforms of Rab3 were deleted. (pancreapedia.org)
  • RAB3B has been shown to interact with RPH3A. (wikipedia.org)
  • Rab3 was originally identified in brain and shown to be localized to synaptic vesicles (24). (pancreapedia.org)
  • Elevated IFN-γ decreased the SEPT11 protein levels in Ishikawa cells and HEECs. (bvsalud.org)
  • These results implicate LRRK2 in primary ciliogenesis and suggest that Rab-mediated protein transport and/or signaling defects at cilia may contribute to LRRK2-dependent pathologies. (elifesciences.org)