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Sizes of actin networks sharing a common environment are determined by the relative rates of assembly.
Antkowiak, Adrien; Guillotin, Audrey; Boiero Sanders, Micaela; Colombo, Jessica; Vincentelli, Renaud; Michelot, Alphée.
Affiliation
  • Antkowiak A; Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
  • Guillotin A; Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
  • Boiero Sanders M; Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
  • Colombo J; Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
  • Vincentelli R; Unité Mixte de Recherche (UMR) 7257, Centre National de la Recherche Scientifique (CNRS) Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), Marseille, France.
  • Michelot A; Aix Marseille Univ, CNRS, IBDM, Turing Centre for Living Systems, Marseille, France.
PLoS Biol ; 17(6): e3000317, 2019 06.
Article in En | MEDLINE | ID: mdl-31181075
Within the cytoplasm of a single cell, several actin networks can coexist with distinct sizes, geometries, and protein compositions. These actin networks assemble in competition for a limited pool of proteins present in a common cellular environment. To predict how two distinct networks of actin filaments control this balance, the simultaneous assembly of actin-related protein 2/3 (Arp2/3)-branched networks and formin-linear networks of actin filaments around polystyrene microbeads was investigated with a range of actin accessory proteins (profilin, capping protein, actin-depolymerizing factor [ADF]/cofilin, and tropomyosin). Accessory proteins generally affected actin assembly rates for the distinct networks differently. These effects at the scale of individual actin networks were surprisingly not always correlated with corresponding loss-of-function phenotypes in cells. However, our observations agreed with a global interpretation, which compared relative actin assembly rates of individual actin networks. This work supports a general model in which the size of distinct actin networks is determined by their relative capacity to assemble in a common and competing environment.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Actins / Actin-Related Protein 2-3 Complex / Microfilament Proteins Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: PLoS Biol Journal subject: BIOLOGIA Year: 2019 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Actins / Actin-Related Protein 2-3 Complex / Microfilament Proteins Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: PLoS Biol Journal subject: BIOLOGIA Year: 2019 Document type: Article Affiliation country: Country of publication: