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Posttranscriptional and posttranslational regulation of actin.

08:00 EDT 12th October 2018 | BioPortfolio

Summary of "Posttranscriptional and posttranslational regulation of actin."

Actin is one of the most abundant intracellular proteins, essential in every eukaryotic cell type. Actin plays key roles in tissue morphogenesis, cell adhesion, muscle contraction, and developmental reprogramming. Most actin studies have focused on its regulation at the protein level, either directly or through differential interactions with over a hundred intracellular binding partners. However, numerous studies emerging in recent years demonstrate specific types of nucleotide-level regulation that strongly affect non-muscle actins during cell migration and adhesion and are potentially applicable to other members of the actin family. This regulation involves zipcode-mediated actin mRNA targeting to the cell periphery, proposed to mediate local synthesis of actin at the cell leading edge, as well as the recently discovered N-terminal arginylation that specifically targets non-muscle β-actin via a nucleotide-dependent mechanism. Moreover, a study published this year suggests that actin's essential roles at the organismal level may be entirely nucleotide-dependent. This review summarizes the emerging data on actin's nucleotide-level regulation. This article is protected by copyright. All rights reserved.

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This article was published in the following journal.

Name: Anatomical record (Hoboken, N.J. : 2007)
ISSN: 1932-8494
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A dioxygenase and alkylation repair homolog that mediates demethylation of ACTIN monomethylated at 'Lys-84' (K84me1). Demethylation of actin LYSINE 84 (K84me1) is required for maintaining actin and MYOSIN dynamics to support normal cleavage furrow ingression during CYTOKINESIS and CELL MIGRATION. It may also be involved in transcription regulation.

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Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization.

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