Cargando…
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...
Autores principales: | , , , , |
---|---|
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 |
_version_ | 1782144929929101312 |
---|---|
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. |
format | Text |
id | pubmed-2171418 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT niepelmario thenuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT strambiodecastilliacaterina thenuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT fasolojoseph thenuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT chaitbriant thenuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT routmichaelp thenuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT niepelmario nuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT strambiodecastilliacaterina nuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT fasolojoseph nuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT chaitbriant nuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly AT routmichaelp nuclearporecomplexassociatedproteinmlp2pbindstotheyeastspindlepolebodyandpromotesitsefficientassembly |