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Myosin V attachment to cargo requires the tight association of two functional subdomains

The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdoma...

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Detalles Bibliográficos
Autores principales: Pashkova, Natasha, Catlett, Natalie L., Novak, Jennifer L., Wu, Guanming, Lu, Renne, Cohen, Robert E., Weisman, Lois S.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171732/
https://www.ncbi.nlm.nih.gov/pubmed/15684027
http://dx.doi.org/10.1083/jcb.200407146
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author Pashkova, Natasha
Catlett, Natalie L.
Novak, Jennifer L.
Wu, Guanming
Lu, Renne
Cohen, Robert E.
Weisman, Lois S.
author_facet Pashkova, Natasha
Catlett, Natalie L.
Novak, Jennifer L.
Wu, Guanming
Lu, Renne
Cohen, Robert E.
Weisman, Lois S.
author_sort Pashkova, Natasha
collection PubMed
description The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have distinct functions, namely, vacuole-specific and secretory vesicle–specific movement. Biochemical and genetic analyses demonstrate that subdomain I tightly associates with subdomain II, and that the interaction does not require additional proteins. Importantly, although neither subdomain alone is functional, simultaneous expression of the separate subdomains produces a functional complex in vivo. Our results suggest a model whereby intramolecular interactions between the globular tail subdomains help to coordinate the transport of multiple distinct cargoes by myosin V.
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spelling pubmed-21717322008-03-05 Myosin V attachment to cargo requires the tight association of two functional subdomains Pashkova, Natasha Catlett, Natalie L. Novak, Jennifer L. Wu, Guanming Lu, Renne Cohen, Robert E. Weisman, Lois S. J Cell Biol Research Articles The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have distinct functions, namely, vacuole-specific and secretory vesicle–specific movement. Biochemical and genetic analyses demonstrate that subdomain I tightly associates with subdomain II, and that the interaction does not require additional proteins. Importantly, although neither subdomain alone is functional, simultaneous expression of the separate subdomains produces a functional complex in vivo. Our results suggest a model whereby intramolecular interactions between the globular tail subdomains help to coordinate the transport of multiple distinct cargoes by myosin V. The Rockefeller University Press 2005-01-31 /pmc/articles/PMC2171732/ /pubmed/15684027 http://dx.doi.org/10.1083/jcb.200407146 Text en Copyright © 2005, 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 Research Articles
Pashkova, Natasha
Catlett, Natalie L.
Novak, Jennifer L.
Wu, Guanming
Lu, Renne
Cohen, Robert E.
Weisman, Lois S.
Myosin V attachment to cargo requires the tight association of two functional subdomains
title Myosin V attachment to cargo requires the tight association of two functional subdomains
title_full Myosin V attachment to cargo requires the tight association of two functional subdomains
title_fullStr Myosin V attachment to cargo requires the tight association of two functional subdomains
title_full_unstemmed Myosin V attachment to cargo requires the tight association of two functional subdomains
title_short Myosin V attachment to cargo requires the tight association of two functional subdomains
title_sort myosin v attachment to cargo requires the tight association of two functional subdomains
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171732/
https://www.ncbi.nlm.nih.gov/pubmed/15684027
http://dx.doi.org/10.1083/jcb.200407146
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