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Molecular architecture and assembly of the yeast kinetochore MIND complex

The MIND multiprotein complex is a conserved, essential component of eukaryotic kinetochores and is a constituent of the tripartite KMN network that directly attaches the kinetochore to the mitotic spindle. The primary microtubule-binding complex in this network, NDC80, has been extensively characte...

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Detalles Bibliográficos
Autores principales: Maskell, Daniel P., Hu, Xiao-Wen, Singleton, Martin R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935576/
https://www.ncbi.nlm.nih.gov/pubmed/20819936
http://dx.doi.org/10.1083/jcb.201002059
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author Maskell, Daniel P.
Hu, Xiao-Wen
Singleton, Martin R.
author_facet Maskell, Daniel P.
Hu, Xiao-Wen
Singleton, Martin R.
author_sort Maskell, Daniel P.
collection PubMed
description The MIND multiprotein complex is a conserved, essential component of eukaryotic kinetochores and is a constituent of the tripartite KMN network that directly attaches the kinetochore to the mitotic spindle. The primary microtubule-binding complex in this network, NDC80, has been extensively characterized, but very little is known about the structure or function of the MIND complex. In this study, we present biochemical, hydrodynamic, electron microscopy, and small-angle x-ray scattering data that provide insight into the overall architecture and assembly of the MIND complex and the physical relationship of the complex with other components of the KMN network. We propose a model for the overall structure of the complex and provide data on the interactions with NDC80, Spc105p, and thus the mitotic spindle.
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spelling pubmed-29355762011-03-06 Molecular architecture and assembly of the yeast kinetochore MIND complex Maskell, Daniel P. Hu, Xiao-Wen Singleton, Martin R. J Cell Biol Research Articles The MIND multiprotein complex is a conserved, essential component of eukaryotic kinetochores and is a constituent of the tripartite KMN network that directly attaches the kinetochore to the mitotic spindle. The primary microtubule-binding complex in this network, NDC80, has been extensively characterized, but very little is known about the structure or function of the MIND complex. In this study, we present biochemical, hydrodynamic, electron microscopy, and small-angle x-ray scattering data that provide insight into the overall architecture and assembly of the MIND complex and the physical relationship of the complex with other components of the KMN network. We propose a model for the overall structure of the complex and provide data on the interactions with NDC80, Spc105p, and thus the mitotic spindle. The Rockefeller University Press 2010-09-06 /pmc/articles/PMC2935576/ /pubmed/20819936 http://dx.doi.org/10.1083/jcb.201002059 Text en © 2010 Maskell et al. 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Maskell, Daniel P.
Hu, Xiao-Wen
Singleton, Martin R.
Molecular architecture and assembly of the yeast kinetochore MIND complex
title Molecular architecture and assembly of the yeast kinetochore MIND complex
title_full Molecular architecture and assembly of the yeast kinetochore MIND complex
title_fullStr Molecular architecture and assembly of the yeast kinetochore MIND complex
title_full_unstemmed Molecular architecture and assembly of the yeast kinetochore MIND complex
title_short Molecular architecture and assembly of the yeast kinetochore MIND complex
title_sort molecular architecture and assembly of the yeast kinetochore mind complex
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935576/
https://www.ncbi.nlm.nih.gov/pubmed/20819936
http://dx.doi.org/10.1083/jcb.201002059
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