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The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly

The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their...

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Autores principales: Niepel, Mario, Strambio-de-Castillia, Caterina, Fasolo, Joseph, Chait, Brian T., Rout, Michael P.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171418/
https://www.ncbi.nlm.nih.gov/pubmed/16027220
http://dx.doi.org/10.1083/jcb.200504140
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author Niepel, Mario
Strambio-de-Castillia, Caterina
Fasolo, Joseph
Chait, Brian T.
Rout, Michael P.
author_facet Niepel, Mario
Strambio-de-Castillia, Caterina
Fasolo, Joseph
Chait, Brian T.
Rout, Michael P.
author_sort Niepel, Mario
collection PubMed
description The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their different roles within the cell. We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope–associated yeast spindle organizer. We further show that SPB function is compromised in mlp2 mutants. Cells lacking Mlp2p form significantly smaller SPBs, accumulate aberrant SPB component-containing structures inside the nucleus, and have stochastic failures of cell division. In addition, depletion of Mlp2p is synthetically lethal with mutants impaired in SPB assembly. Based on these data, we propose that Mlp2p links the SPB to the peripheral Mlp assembly, and that this linkage is required for efficient incorporation of components into the SPB.
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spelling pubmed-21714182008-03-05 The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly Niepel, Mario Strambio-de-Castillia, Caterina Fasolo, Joseph Chait, Brian T. Rout, Michael P. J Cell Biol Research Articles The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their different roles within the cell. We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope–associated yeast spindle organizer. We further show that SPB function is compromised in mlp2 mutants. Cells lacking Mlp2p form significantly smaller SPBs, accumulate aberrant SPB component-containing structures inside the nucleus, and have stochastic failures of cell division. In addition, depletion of Mlp2p is synthetically lethal with mutants impaired in SPB assembly. Based on these data, we propose that Mlp2p links the SPB to the peripheral Mlp assembly, and that this linkage is required for efficient incorporation of components into the SPB. The Rockefeller University Press 2005-07-18 /pmc/articles/PMC2171418/ /pubmed/16027220 http://dx.doi.org/10.1083/jcb.200504140 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
Niepel, Mario
Strambio-de-Castillia, Caterina
Fasolo, Joseph
Chait, Brian T.
Rout, Michael P.
The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
title The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
title_full The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
title_fullStr The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
title_full_unstemmed The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
title_short The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
title_sort nuclear pore complex–associated protein, mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171418/
https://www.ncbi.nlm.nih.gov/pubmed/16027220
http://dx.doi.org/10.1083/jcb.200504140
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