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Actin polymerization and cell motility are affected by NAA80-mediated posttranslational N-terminal acetylation of actin.
Aksnes, Henriette; Marie, Michael; Arnesen, Thomas; Drazic, Adrian.
Afiliação
  • Aksnes H; Department of Biomedicine, University of Bergen, Bergen, Norway.
  • Marie M; Department of Biomedicine, University of Bergen, Bergen, Norway.
  • Arnesen T; Department of Biomedicine, University of Bergen, Bergen, Norway.
  • Drazic A; Department of Biological Sciences, University of Bergen, Bergen, Norway.
Commun Integr Biol ; 11(4): e1526572, 2018.
Article em En | MEDLINE | ID: mdl-30534344
ABSTRACT
Actin is the most abundant protein in our cells, and also one of the most studied. Nevertheless, an important modifier of actin, the N-terminal acetyltransferase (NAT) for actin, remained unknown until now. The recent identification of the enzyme that catalyzes actin acetylation, has opened up for functional studies of unacetylated actin using knockout cells. This enzyme, called NAA80 (Nα-acetyltransferase 80) or NatH, belongs to the NAT family of enzymes, which together provides N-terminal acetylation for around 80 % of the human proteome. In many cases, N-terminal acetylation is essential. In the case of actin, the acetyl group that NAA80 attaches to actin plays an important role in actin's polymerization properties as well as in actin's function in cell migration.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Commun Integr Biol Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Commun Integr Biol Ano de publicação: 2018 Tipo de documento: Article