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Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins

Actin arginylation regulates lamella formation in motile fibroblasts, but the underlying molecular mechanisms are unknown. To understand how arginylation affects the actin cytoskeleton, we investigated the biochemical properties and the structural organization of actin filaments in wild-type and arg...

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Autores principales: Saha, Sougata, Mundia, Maureen M., Zhang, Fangliang, Demers, Ryan W., Korobova, Farida, Svitkina, Tatyana, Perieteanu, Alex A., Dawson, John F., Kashina, Anna
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854093/
https://www.ncbi.nlm.nih.gov/pubmed/20181827
http://dx.doi.org/10.1091/mbc.E09-09-0829
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author Saha, Sougata
Mundia, Maureen M.
Zhang, Fangliang
Demers, Ryan W.
Korobova, Farida
Svitkina, Tatyana
Perieteanu, Alex A.
Dawson, John F.
Kashina, Anna
author_facet Saha, Sougata
Mundia, Maureen M.
Zhang, Fangliang
Demers, Ryan W.
Korobova, Farida
Svitkina, Tatyana
Perieteanu, Alex A.
Dawson, John F.
Kashina, Anna
author_sort Saha, Sougata
collection PubMed
description Actin arginylation regulates lamella formation in motile fibroblasts, but the underlying molecular mechanisms are unknown. To understand how arginylation affects the actin cytoskeleton, we investigated the biochemical properties and the structural organization of actin filaments in wild-type and arginyltransferase (Ate1) knockout cells. We found that Ate1 knockout results in a dramatic reduction of the actin polymer levels in vivo accompanied by a corresponding increase in the monomer level. Purified nonarginylated actin has altered polymerization properties, and actin filaments from Ate1 knockout cells show altered interactions with several associated proteins. Ate1 knockout cells have severe impairment of cytoskeletal organization throughout the cell. Thus, arginylation regulates the ability of actin to form filaments in the whole cell rather than preventing the collapse of preformed actin networks at the cell leading edge as proposed in our previous model. This regulation is achieved through interconnected mechanisms that involve actin polymerization per se and through binding of actin-associated proteins.
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spelling pubmed-28540932010-06-30 Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins Saha, Sougata Mundia, Maureen M. Zhang, Fangliang Demers, Ryan W. Korobova, Farida Svitkina, Tatyana Perieteanu, Alex A. Dawson, John F. Kashina, Anna Mol Biol Cell Articles Actin arginylation regulates lamella formation in motile fibroblasts, but the underlying molecular mechanisms are unknown. To understand how arginylation affects the actin cytoskeleton, we investigated the biochemical properties and the structural organization of actin filaments in wild-type and arginyltransferase (Ate1) knockout cells. We found that Ate1 knockout results in a dramatic reduction of the actin polymer levels in vivo accompanied by a corresponding increase in the monomer level. Purified nonarginylated actin has altered polymerization properties, and actin filaments from Ate1 knockout cells show altered interactions with several associated proteins. Ate1 knockout cells have severe impairment of cytoskeletal organization throughout the cell. Thus, arginylation regulates the ability of actin to form filaments in the whole cell rather than preventing the collapse of preformed actin networks at the cell leading edge as proposed in our previous model. This regulation is achieved through interconnected mechanisms that involve actin polymerization per se and through binding of actin-associated proteins. The American Society for Cell Biology 2010-04-15 /pmc/articles/PMC2854093/ /pubmed/20181827 http://dx.doi.org/10.1091/mbc.E09-09-0829 Text en © 2010 by The American Society for Cell Biology
spellingShingle Articles
Saha, Sougata
Mundia, Maureen M.
Zhang, Fangliang
Demers, Ryan W.
Korobova, Farida
Svitkina, Tatyana
Perieteanu, Alex A.
Dawson, John F.
Kashina, Anna
Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
title Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
title_full Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
title_fullStr Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
title_full_unstemmed Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
title_short Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
title_sort arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2854093/
https://www.ncbi.nlm.nih.gov/pubmed/20181827
http://dx.doi.org/10.1091/mbc.E09-09-0829
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