Mechanism of actin capping protein recruitment and turnover during clathrin-mediated endocytosis.
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
01 01 2024
01 01 2024
Historique:
received:
30
06
2023
revised:
11
10
2023
accepted:
01
11
2023
pmc-release:
15
05
2024
medline:
16
11
2023
pubmed:
15
11
2023
entrez:
15
11
2023
Statut:
ppublish
Résumé
Clathrin-mediated endocytosis depends on polymerization of a branched actin network to provide force for membrane invagination. A key regulator in branched actin network formation is actin capping protein (CP), which binds to the barbed end of actin filaments to prevent the addition or loss of actin subunits. CP was thought to stochastically bind actin filaments, but recent evidence shows CP is regulated by a group of proteins containing CP-interacting (CPI) motifs. Importantly, how CPI motif proteins function together to regulate CP is poorly understood. Here, we show Aim21 and Bsp1 work synergistically to recruit CP to the endocytic actin network in budding yeast through their CPI motifs, which also allosterically modulate capping strength. In contrast, twinfilin works downstream of CP recruitment, regulating the turnover of CP through its CPI motif and a non-allosteric mechanism. Collectively, our findings reveal how three CPI motif proteins work together to regulate CP in a stepwise fashion during endocytosis.
Identifiants
pubmed: 37966720
pii: 276410
doi: 10.1083/jcb.202306154
pmc: PMC10651396
pii:
doi:
Substances chimiques
Actin Capping Proteins
0
Actins
0
Clathrin
0
Saccharomyces cerevisiae Proteins
0
AIM21 protein, S cerevisiae
0
Bsp1 protein, S cerevisiae
0
Adaptor Proteins, Vesicular Transport
0
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2023 Lamb et al.
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