Rab2A is a pivotal switch protein that promotes either secretion or ER-associated degradation of (pro)insulin in insulin-secreting cells
Open accessAbstract
Rab2A, a small GTPase localizing to the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), regulates COPI-dependent vesicular transport from the ERGIC. Rab2A knockdown inhibited glucose-stimulated insulin secretion and concomitantly enlarged the ERGIC in insulin-secreting cells. Large aggregates of polyubiquitinated proinsulin accumulated in the cytoplasmic vicinity of a unique large spheroidal ERGIC, designated the LUb-ERGIC. Well-known components of ER-associated degradation (ERAD) also accumulated at the LUb-ERGIC, creating a suitable site for ERAD-mediated protein quality control. Moreover, chronically high glucose levels, which induced the enlargement of the LUb-ERGIC and ubiquitinated protein aggregates, impaired Rab2A activity by promoting dissociation from its effector, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), in response to poly (ADP-ribosyl)ation of GAPDH. The inactivation of Rab2A relieved glucose-induced ER stress and inhibited ER stress-induced apoptosis. Collectively, these results suggest that Rab2A is a pivotal switch that controls whether insulin should be secreted or degraded at the LUb-ERGIC and Rab2A inactivation ensures alleviation of ER stress and cell survival under chronic glucotoxicity.
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Rab2a is involved in DCG cargo sorting.
“The involvement of Rab2a in DCG cargo sorting has been previously reported (Edwards et al., 2009; Sugawara et al., 2014; Sumakovic et al., 2009; Zhang et al., 2015).”
From Intestinal microbiota modulates adrenomedullary response through Nod1 sensing in chromaffin cells (2021) · cites this paper as Sugawara et al., 2014
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- Authors
- Sugawara, T., Kano, F., & Murata, M.
- Affiliations
- The University of Tokyo (JP)
- Japan Science and Technology Agency (JP)
- Corresponding author
- Murata, Masayuki
- Venue
- Scientific Reports
- Published
- 2014-11-07
- Volume
- 4
- Issue
- 1
- Pages
- 6952-6952
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC5381769
- OpenAlex
- W1965316998
- Cited by
- 34
- References
- 49
- Citations by year
- 2026: 3 · 2024: 2 · 2023: 3 · 2022: 7 · 2021: 6 · 2019: 3 · 2018: 4 · 2017: 2 · 2016: 4
- FWCI
- 1.00
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Scientific Reports (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- Japan Science and Technology Agency
- Precursory Research for Embryonic Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Keywords
- RAB2A, small GTPases, ERGIC, proinsulin, insulin secretion, ER-associated degradation, glucose-stimulated insulin secretion, endoplasmic reticulum stress, glucotoxicity, glyceraldehyde-3-phosphate dehydrogenase, poly(ADP-ribosyl)ation, insulin-secreting cells, protein quality control
- MeSH terms
- Animals, Biological Transport, Endoplasmic Reticulum, Glucose, Golgi Apparatus, Proinsulin, Signal Transduction, Apoptosis, rab GTP-Binding Proteins, rab2 GTP-Binding Protein, COP-Coated Vesicles, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating), Polyubiquitin, RNA, Small Interfering, Cell Line, Tumor, Insulin-Secreting Cells, Mice, Endoplasmic Reticulum Stress, Endoplasmic Reticulum-Associated Degradation, Protein Aggregates
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