Distinct functional interactions between actin isoforms and nonsarcomeric myosins.

Despite their near sequence identity, actin isoforms cannot completely replace each other in vivo and show marked differences in their tissue-specific and subcellular localization. Little is known about isoform-specific differences in their interactions with myosin motors and other actin-binding pro...

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Autores principales:	Mirco Müller, Ralph P Diensthuber, Igor Chizhov, Peter Claus, Sarah M Heissler, Matthias Preller, Manuel H Taft, Dietmar J Manstein
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0bc98f18476241ca8c1beb72883b3d93
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spelling	oai:doaj.org-article:0bc98f18476241ca8c1beb72883b3d932021-11-18T09:02:34ZDistinct functional interactions between actin isoforms and nonsarcomeric myosins.1932-620310.1371/journal.pone.0070636https://doaj.org/article/0bc98f18476241ca8c1beb72883b3d932013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23923011/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Despite their near sequence identity, actin isoforms cannot completely replace each other in vivo and show marked differences in their tissue-specific and subcellular localization. Little is known about isoform-specific differences in their interactions with myosin motors and other actin-binding proteins. Mammalian cytoplasmic β- and γ-actin interact with nonsarcomeric conventional myosins such as the members of the nonmuscle myosin-2 family and myosin-7A. These interactions support a wide range of cellular processes including cytokinesis, maintenance of cell polarity, cell adhesion, migration, and mechano-electrical transduction. To elucidate differences in the ability of isoactins to bind and stimulate the enzymatic activity of individual myosin isoforms, we characterized the interactions of human skeletal muscle α-actin, cytoplasmic β-actin, and cytoplasmic γ-actin with human myosin-7A and nonmuscle myosins-2A, -2B and -2C1. In the case of nonmuscle myosins-2A and -2B, the interaction with either cytoplasmic actin isoform results in 4-fold greater stimulation of myosin ATPase activity than was observed in the presence of α-skeletal muscle actin. Nonmuscle myosin-2C1 is most potently activated by β-actin and myosin-7A by γ-actin. Our results indicate that β- and γ-actin isoforms contribute to the modulation of nonmuscle myosin-2 and myosin-7A activity and thereby to the spatial and temporal regulation of cytoskeletal dynamics. FRET-based analyses show efficient copolymerization abilities for the actin isoforms in vitro. Experiments with hybrid actin filaments show that the extent of actomyosin coupling efficiency can be regulated by the isoform composition of actin filaments.Mirco MüllerRalph P DiensthuberIgor ChizhovPeter ClausSarah M HeisslerMatthias PrellerManuel H TaftDietmar J MansteinPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 7, p e70636 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mirco Müller Ralph P Diensthuber Igor Chizhov Peter Claus Sarah M Heissler Matthias Preller Manuel H Taft Dietmar J Manstein Distinct functional interactions between actin isoforms and nonsarcomeric myosins.
description	Despite their near sequence identity, actin isoforms cannot completely replace each other in vivo and show marked differences in their tissue-specific and subcellular localization. Little is known about isoform-specific differences in their interactions with myosin motors and other actin-binding proteins. Mammalian cytoplasmic β- and γ-actin interact with nonsarcomeric conventional myosins such as the members of the nonmuscle myosin-2 family and myosin-7A. These interactions support a wide range of cellular processes including cytokinesis, maintenance of cell polarity, cell adhesion, migration, and mechano-electrical transduction. To elucidate differences in the ability of isoactins to bind and stimulate the enzymatic activity of individual myosin isoforms, we characterized the interactions of human skeletal muscle α-actin, cytoplasmic β-actin, and cytoplasmic γ-actin with human myosin-7A and nonmuscle myosins-2A, -2B and -2C1. In the case of nonmuscle myosins-2A and -2B, the interaction with either cytoplasmic actin isoform results in 4-fold greater stimulation of myosin ATPase activity than was observed in the presence of α-skeletal muscle actin. Nonmuscle myosin-2C1 is most potently activated by β-actin and myosin-7A by γ-actin. Our results indicate that β- and γ-actin isoforms contribute to the modulation of nonmuscle myosin-2 and myosin-7A activity and thereby to the spatial and temporal regulation of cytoskeletal dynamics. FRET-based analyses show efficient copolymerization abilities for the actin isoforms in vitro. Experiments with hybrid actin filaments show that the extent of actomyosin coupling efficiency can be regulated by the isoform composition of actin filaments.
format	article
author	Mirco Müller Ralph P Diensthuber Igor Chizhov Peter Claus Sarah M Heissler Matthias Preller Manuel H Taft Dietmar J Manstein
author_facet	Mirco Müller Ralph P Diensthuber Igor Chizhov Peter Claus Sarah M Heissler Matthias Preller Manuel H Taft Dietmar J Manstein
author_sort	Mirco Müller
title	Distinct functional interactions between actin isoforms and nonsarcomeric myosins.
title_short	Distinct functional interactions between actin isoforms and nonsarcomeric myosins.
title_full	Distinct functional interactions between actin isoforms and nonsarcomeric myosins.
title_fullStr	Distinct functional interactions between actin isoforms and nonsarcomeric myosins.
title_full_unstemmed	Distinct functional interactions between actin isoforms and nonsarcomeric myosins.
title_sort	distinct functional interactions between actin isoforms and nonsarcomeric myosins.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/0bc98f18476241ca8c1beb72883b3d93
work_keys_str_mv	AT mircomuller distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT ralphpdiensthuber distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT igorchizhov distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT peterclaus distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT sarahmheissler distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT matthiaspreller distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT manuelhtaft distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins AT dietmarjmanstein distinctfunctionalinteractionsbetweenactinisoformsandnonsarcomericmyosins
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Distinct functional interactions between actin isoforms and nonsarcomeric myosins.

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