Epigallocatechin gallate inhibits SNARE-dependent membrane fusion by blocking trans-SNARE assembly.
EGCG
SNARE
exocytosis
insulin secretion
membrane fusion
synaptotagmin
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
12 2022
12 2022
Historique:
revised:
06
08
2022
received:
22
07
2022
accepted:
15
09
2022
pubmed:
17
9
2022
medline:
6
12
2022
entrez:
16
9
2022
Statut:
ppublish
Résumé
Insulin secretion is a signal-triggered process that requires membrane fusion between the secretory granules and plasma membrane in pancreatic β cells. The exocytosis of insulin is mediated by target-soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs) on the plasma membrane and vesicle-SNAREs on the vesicles, which assemble into a quaternary trans-SNARE complex to initiate the fusion. Expression of fusion proteins is reduced in the islets of patients with type II diabetes, indicating that SNARE-mediated fusion defect is closely related to insulin-based metabolic diseases. Previous studies have suggested that epigallocatechin gallate (EGCG) has an inhibitory effect on membrane fusion. In the present study, we performed in vitro reconstitution assays to unravel the molecular mechanisms of EGCG in SNARE-mediated insulin secretory vesicle fusion. Our data show that EGCG efficiently inhibits insulin secretory SNARE-mediated membrane fusion. Mechanistic studies indicated that EGCG blocks the formation of the trans-SNARE complex. Furthermore, calcium/synaptotagmin-7-stimulated fusion kinetics were largely reduced by EGCG, confirming that it is a potential regulator of SNARE-dependent insulin secretion. Our findings suggest that the trans-SNARE complex might be a promising target for controlling SNARE-dependent vesicle fusion.
Identifiants
pubmed: 36111501
doi: 10.1002/2211-5463.13488
pmc: PMC9714361
doi:
Substances chimiques
SNARE Proteins
0
epigallocatechin gallate
BQM438CTEL
Insulins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2111-2121Informations de copyright
© 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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