Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
06 07 2023
Historique:
received: 22 12 2022
accepted: 22 06 2023
medline: 10 7 2023
pubmed: 7 7 2023
entrez: 6 7 2023
Statut: epublish

Résumé

Cells control actin assembly by regulating reactions at actin filament barbed ends. Formins accelerate elongation, capping protein (CP) arrests growth and twinfilin promotes depolymerization at barbed ends. How these distinct activities get integrated within a shared cytoplasm is unclear. Using microfluidics-assisted TIRF microscopy, we find that formin, CP and twinfilin can simultaneously bind filament barbed ends. Three‑color, single-molecule experiments reveal that twinfilin cannot bind barbed ends occupied by formin unless CP is present. This trimeric complex is short-lived (~1 s), and results in dissociation of CP by twinfilin, promoting formin-based elongation. Thus, the depolymerase twinfilin acts as a pro-formin pro-polymerization factor when both CP and formin are present. While one twinfilin binding event is sufficient to displace CP from the barbed-end trimeric complex, ~31 twinfilin binding events are required to remove CP from a CP-capped barbed end. Our findings establish a paradigm where polymerases, depolymerases and cappers together tune actin assembly.

Identifiants

pubmed: 37414761
doi: 10.1038/s41467-023-39655-3
pii: 10.1038/s41467-023-39655-3
pmc: PMC10326068
doi:

Substances chimiques

Actins 0
Formins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

3981

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM143050
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM135060
Pays : United States

Commentaires et corrections

Type : UpdateOf

Informations de copyright

© 2023. The Author(s).

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Auteurs

Heidi Ulrichs (H)

Department of Physics, Emory University, Atlanta, GA, 30322, USA.
Department of Cell Biology, Emory University, Atlanta, GA, 30322, USA.

Ignas Gaska (I)

Department of Physics, Emory University, Atlanta, GA, 30322, USA.
Department of Cell Biology, Emory University, Atlanta, GA, 30322, USA.

Shashank Shekhar (S)

Department of Physics, Emory University, Atlanta, GA, 30322, USA. shekhar@emory.edu.
Department of Cell Biology, Emory University, Atlanta, GA, 30322, USA. shekhar@emory.edu.

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Classifications MeSH