A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex

Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology...

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Autores principales: Evangelista, Marie, Klebl, Bert M., Tong, Amy H.Y., Webb, Bradley A., Leeuw, Thomas, Leberer, Ekkehard, Whiteway, Malcolm, Thomas, David Y., Boone, Charles
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174279/
https://www.ncbi.nlm.nih.gov/pubmed/10648568
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author Evangelista, Marie
Klebl, Bert M.
Tong, Amy H.Y.
Webb, Bradley A.
Leeuw, Thomas
Leberer, Ekkehard
Whiteway, Malcolm
Thomas, David Y.
Boone, Charles
author_facet Evangelista, Marie
Klebl, Bert M.
Tong, Amy H.Y.
Webb, Bradley A.
Leeuw, Thomas
Leberer, Ekkehard
Whiteway, Malcolm
Thomas, David Y.
Boone, Charles
author_sort Evangelista, Marie
collection PubMed
description Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p, and showed both sequence similarity and genetic redundancy with the COOH-terminal acidic domain of Bee1p (Las17p), which controls Arp2/3-mediated actin nucleation. These findings suggest that myosin-I proteins may participate in a diverse set of motility functions through a role in actin assembly.
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spelling pubmed-21742792008-05-01 A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex Evangelista, Marie Klebl, Bert M. Tong, Amy H.Y. Webb, Bradley A. Leeuw, Thomas Leberer, Ekkehard Whiteway, Malcolm Thomas, David Y. Boone, Charles J Cell Biol Original Article Type I myosins are highly conserved actin-based molecular motors that localize to the actin-rich cortex and participate in motility functions such as endocytosis, polarized morphogenesis, and cell migration. The COOH-terminal tail of yeast myosin-I proteins, Myo3p and Myo5p, contains an Src homology domain 3 (SH3) followed by an acidic domain. The myosin-I SH3 domain interacted with both Bee1p and Vrp1p, yeast homologues of human WASP and WIP, adapter proteins that link actin assembly and signaling molecules. The myosin-I acidic domain interacted with Arp2/3 complex subunits, Arc40p and Arc19p, and showed both sequence similarity and genetic redundancy with the COOH-terminal acidic domain of Bee1p (Las17p), which controls Arp2/3-mediated actin nucleation. These findings suggest that myosin-I proteins may participate in a diverse set of motility functions through a role in actin assembly. The Rockefeller University Press 2000-01-24 /pmc/articles/PMC2174279/ /pubmed/10648568 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Evangelista, Marie
Klebl, Bert M.
Tong, Amy H.Y.
Webb, Bradley A.
Leeuw, Thomas
Leberer, Ekkehard
Whiteway, Malcolm
Thomas, David Y.
Boone, Charles
A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
title A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
title_full A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
title_fullStr A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
title_full_unstemmed A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
title_short A Role for Myosin-I in Actin Assembly through Interactions with Vrp1p, Bee1p, and the Arp2/3 Complex
title_sort role for myosin-i in actin assembly through interactions with vrp1p, bee1p, and the arp2/3 complex
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174279/
https://www.ncbi.nlm.nih.gov/pubmed/10648568
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