Membrane insertion mechanism of the caveola coat protein Cavin1.
Cavin1
caveolae
membrane curvature
membrane-shaping protein
protein–lipid interactions
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
21 06 2022
21 06 2022
Historique:
entrez:
13
6
2022
pubmed:
14
6
2022
medline:
16
6
2022
Statut:
ppublish
Résumé
Caveolae are small plasma membrane invaginations, important for control of membrane tension, signaling cascades, and lipid sorting. The caveola coat protein Cavin1 is essential for shaping such high curvature membrane structures. Yet, a mechanistic understanding of how Cavin1 assembles at the membrane interface is lacking. Here, we used model membranes combined with biophysical dissection and computational modeling to show that Cavin1 inserts into membranes. We establish that initial phosphatidylinositol (4, 5) bisphosphate [PI(4,5)P
Identifiants
pubmed: 35696574
doi: 10.1073/pnas.2202295119
pmc: PMC9231606
doi:
Substances chimiques
CAV1 protein, human
0
CAVIN1 protein, human
0
Caveolin 1
0
Phosphatidylinositol 4,5-Diphosphate
0
RNA-Binding Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2202295119Références
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