Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation

Fangliang Zhang, Sougata Saha, Svetlana A. Shabalina, Anna Kashina

Research output: Contribution to journalArticle

123 Scopus citations

Abstract

The mammalian cytoskeletal proteins β- and γ-actin are highly homologous, but only β-actin is amino-terminally arginylated in vivo, which regulates its function. We examined the metabolic fate of exogenously expressed arginylated and nonarginylated actin isoforms. Arginylated γ-actin, unlike β-, was highly unstable and was selectively ubiquitinated and degraded in vivo. This instability was regulated by the differences in the nucleotide coding sequence between the two actin isoforms, which conferred different translation rates. γ-actin was translated more slowly than β-actin, and this slower processing resulted in the exposure of a normally hidden lysine residue for ubiquitination, leading to the preferential degradation of γ-actin upon arginylation. This degradation mechanism, coupled to nucleotide coding sequence, may regulate protein arginylation in vivo.

Original languageEnglish (US)
Pages (from-to)1534-1537
Number of pages4
JournalScience
Volume329
Issue number5998
DOIs
StatePublished - Sep 17 2010

ASJC Scopus subject areas

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