ArticleThe Journal of biological chemistry2013
EPI64B acts as a GTPase-activating protein for Rab27B in pancreatic acinar cells.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Rit1-TBC1D10B signaling modulates FcγR-mediated phagosome formation in RAW264 macrophages.Life science alliance · 2024Article
- Roles of G proteins and their GTPase-activating proteins in platelets.Bioscience reports · 2024Review
- Increased expression of TBC1D10B as a potential prognostic and immunotherapy relevant biomarker in liver hepatocellular carcinoma.Scientific reports · 2023Article
- BAG3 Regulation of RAB35 Mediates the Endosomal Sorting Complexes Required for Transport/Endolysosome Pathway and Tau Clearance.Biological psychiatry · 2022Article
- The RabGAPs EPI64A and EPI64B regulate the apical structure of epithelial cellsMolecular biology of the cell · 2022Article
- Regulation of VEGFR2 trafficking and signaling by Rab GTPase-activating proteins.Scientific reports · 2019Article
- Coordination of synaptic vesicle trafficking and turnover by the Rab35 signaling network.Small GTPases · 2019Review
- RAB27B requirement for stretch-induced exocytosis in bladder umbrella cells.American journal of physiology. Cell physiology · 2018Article
- Molecular architecture of mouse and human pancreatic zymogen granules: protein components and their copy numbers.Biophysics reports · 2018Article
- Genetic deletion of Rab27B in pancreatic acinar cells affects granules size and has inhibitory effects on amylase secretion.Biochemical and biophysical research communications · 2016Article
- Interplay between Rab27a effectors in pancreatic β-cells.World journal of diabetes · 2015Review
- Review
- Rab27A Is Present in Mouse Pancreatic Acinar Cells and Is Required for Digestive Enzyme Secretion.PloS one · 2015Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
The small GTPase Rab27B localizes to the zymogen granule membranes and plays an important role in regulating protein secretion by pancreatic acinar cells, as does Rab3D. A common guanine nucleotide exchange factor (GEF) for Rab3 and Rab27 has been reported; however, the GTPase-activating protein (GAP) specific for Rab27B has not been identified. In this study, the expression in mouse pancreatic acini of two candidate Tre-2/Bub2/Cdc16 (TBC) domain-containing proteins, EPI64 (TBC1D10A) and EPI64B (TBC1D10B), was first demonstrated. Their GAP activity on digestive enzyme secretion was examined by adenovirus-mediated overexpression of EPI64 and EPI64B in isolated pancreatic acini. EPI64B almost completely abolished the GTP-bound form of Rab27B, without affecting GTP-Rab3D. Overexpression of EPI64B also enhanced amylase release. This enhanced release was independent of Rab27A, but dependent on Rab27B, as shown using acini from genetically modified mice. EPI64 had a mild effect on both GTP-Rab27B and amylase release. Co-overexpression of EPI64B with Rab27B can reverse the inhibitory effect of Rab27B on amylase release. Mutations that block the GAP activity decreased the inhibitory effect of EPI64B on the GTP-bound state of Rab27B and abolished the enhancing effect of EPI64B on the amylase release. These data suggest that EPI64B can serve as a potential physiological GAP for Rab27B and thereby participate in the regulation of exocytosis in pancreatic acinar cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.