The building blocks of caveolae revealed: caveolins finally take center stage.
caveolae
caveolins
cell membranes
cryo-electron microscopy
membrane proteins
protein structure
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
26 04 2023
26 04 2023
Historique:
received:
06
02
2023
revised:
07
04
2023
accepted:
14
04
2023
medline:
28
4
2023
pubmed:
21
4
2023
entrez:
21
04
2023
Statut:
ppublish
Résumé
The ability of cells to divide, migrate, relay signals, sense mechanical stimuli, and respond to stress all rely on nanoscale invaginations of the plasma membrane known as caveolae. The caveolins, a family of monotopic membrane proteins, form the inner layer of the caveolar coat. Caveolins have long been implicated in the generation of membrane curvature, in addition to serving as scaffolds for signaling proteins. Until recently, however, the molecular architecture of caveolins was unknown, making it impossible to understand how they operate at a mechanistic level. Over the past year, two independent lines of evidence - experimental and computational - have now converged to provide the first-ever glimpse into the structure of the oligomeric caveolin complexes that function as the building blocks of caveolae. Here, we summarize how these discoveries are transforming our understanding of this long-enigmatic protein family and their role in caveolae assembly and function. We present new models inspired by the structure for how caveolins oligomerize, remodel membranes, interact with their binding partners, and reorganize when mutated. Finally, we discuss emerging insights into structural differences among caveolin family members that enable them to support the proper functions of diverse tissues and organisms.
Identifiants
pubmed: 37082988
pii: 232932
doi: 10.1042/BST20221298
pmc: PMC10212548
doi:
Substances chimiques
Membrane Proteins
0
Caveolin 1
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
855-869Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL144131
Pays : United States
Informations de copyright
© 2023 The Author(s).
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