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Updated: May 11, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
Actin carbonylation: from cell dysfunction to organism disorder
José Pedro Castro1, Tobias Jung, Tilman Grune
1Departamento de Biologia Experimental, Faculdade de Medicina da Universidade do Porto, 4200-319 Porto, Portugal; IBMC-Instituto de Biologia Molecular e Celular, 4150-180 Porto, Portugal; Institute of Nutrition, Friedrich Schiller Universität Jena, Dornburger Str. 24, 07743 Jena, Germany.
Abstract:
Protein carbonylation is an important event in the context of proteostasis because of its frequency, non-enzymatic nature and irreversible effects. The carbonylation of proteins disturbs their function and leads to protein aggregates, which may precede cellular senescence and cell death. Actin, an evolutionarily conserved cytoskeletal protein that is involved in important cellular processes, is one of the proteins most susceptible to carbonylation. Conditions resulting in oxidative stress are likely to lead to its carbonylation, loss of function and aggregate formation. In this review, we summarise actin susceptibility to carbonylation, as verified in cell free extracts, cell lines and animal models, and review its fate through the activation of cell mechanisms aimed at removing damaged proteins. Their insufficient activity may underlie age-related diseases and the ageing process. This article is part of a Special Issue entitled: Posttranslational Protein modifications in biology and Medicine.
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