Cofilin - a protein controlling dynamics of actin filaments

Postȩpy higieny i medycyny doświadczalnej
Zofia Ostrowska, Joanna Moraczewska

Abstract

Cofilins are evolutionary conserved proteins present in all Eukaryotic cells. Their primary function is dynamic reorganization of actin cytoskeleton. Two cofilin isoforms are known: cofilin 1, present in all studied non-muscle cells and in embryonic muscle cells, and cofilin 2, which dominates in mature skeletal and cardiac muscles. Polypeptide chains of both isoforms fold into a structure homological to a conservative ADF (actin depolymerizing factor) domain, which is characteristic of actin depolymerizing factor. In cofilin molecule two actin-binding sites were found. One site binds monomeric and filamentous actin, the second one interacts only with the filament. Binding of cofilin to actin filament causes a change in the orientation of subunits, which results in filament severing. This increases number of ends which can either elongate or shorten the filament, depending on the conditions. Cofilin interactions with monomeric actin decreases availability of polymerization-competent actin subunits. Cofilin activity is controlled by phosphorylation, binding membrane phospholipids, local pH and oxidative stress. Under conditions of oxidative stress oxidation of cysteine residues leads to formation of dimers, which are able to cro...Continue Reading

Citations

Aug 27, 2019·Frontiers in Aging Neuroscience·Yingni SunHongwei Gao
Dec 29, 2019·Scientific Reports·Praachi B JainFlorence Janody
Jul 4, 2018·Proceedings of the National Academy of Sciences of the United States of America·Jiuli ZhouJixin Dong
Nov 12, 2020·Biology·Jaya Aseervatham
Apr 6, 2021·Frontiers in Oncology·Xin JiangYanhong Zhou

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