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Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation

Accurate chromosome segregation requires timely bipolar spindle formation during mitosis. The transforming acidic coiled-coil (TACC) family proteins and the ch-TOG family proteins are key players in bipolar spindle formation. They form a complex to stabilize spindle microtubules, mainly dependent on...

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Detalles Bibliográficos
Autores principales: Zheng, Fan, Li, Tianpeng, Jin, Dong-yan, Syrovatkina, Viktoriya, Scheffler, Kathleen, Tran, Phong T., Fu, Chuanhai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4161510/
https://www.ncbi.nlm.nih.gov/pubmed/25057016
http://dx.doi.org/10.1091/mbc.E14-03-0786
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author Zheng, Fan
Li, Tianpeng
Jin, Dong-yan
Syrovatkina, Viktoriya
Scheffler, Kathleen
Tran, Phong T.
Fu, Chuanhai
author_facet Zheng, Fan
Li, Tianpeng
Jin, Dong-yan
Syrovatkina, Viktoriya
Scheffler, Kathleen
Tran, Phong T.
Fu, Chuanhai
author_sort Zheng, Fan
collection PubMed
description Accurate chromosome segregation requires timely bipolar spindle formation during mitosis. The transforming acidic coiled-coil (TACC) family proteins and the ch-TOG family proteins are key players in bipolar spindle formation. They form a complex to stabilize spindle microtubules, mainly dependent on their localization to the centrosome (the spindle pole body [SPB] in yeast). The molecular mechanism underlying the targeting of the TACC–ch-TOG complex to the centrosome remains unclear. Here we show that the fission yeast Schizosaccharomyces pombe TACC orthologue alp7p is recruited to the SPB by csi1p. The csi1p-interacting region lies within the conserved TACC domain of alp7p, and the carboxyl-terminal domain of csi1p is responsible for interacting with alp7p. Compromised interaction between csi1p and alp7p impairs the localization of alp7p to the SPB during mitosis, thus delaying bipolar spindle formation and leading to anaphase B lagging chromosomes. Hence our study establishes that csi1p serves as a linking molecule tethering spindle-stabilizing factors to the SPB for promoting bipolar spindle assembly.
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spelling pubmed-41615102014-11-30 Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation Zheng, Fan Li, Tianpeng Jin, Dong-yan Syrovatkina, Viktoriya Scheffler, Kathleen Tran, Phong T. Fu, Chuanhai Mol Biol Cell Articles Accurate chromosome segregation requires timely bipolar spindle formation during mitosis. The transforming acidic coiled-coil (TACC) family proteins and the ch-TOG family proteins are key players in bipolar spindle formation. They form a complex to stabilize spindle microtubules, mainly dependent on their localization to the centrosome (the spindle pole body [SPB] in yeast). The molecular mechanism underlying the targeting of the TACC–ch-TOG complex to the centrosome remains unclear. Here we show that the fission yeast Schizosaccharomyces pombe TACC orthologue alp7p is recruited to the SPB by csi1p. The csi1p-interacting region lies within the conserved TACC domain of alp7p, and the carboxyl-terminal domain of csi1p is responsible for interacting with alp7p. Compromised interaction between csi1p and alp7p impairs the localization of alp7p to the SPB during mitosis, thus delaying bipolar spindle formation and leading to anaphase B lagging chromosomes. Hence our study establishes that csi1p serves as a linking molecule tethering spindle-stabilizing factors to the SPB for promoting bipolar spindle assembly. The American Society for Cell Biology 2014-09-15 /pmc/articles/PMC4161510/ /pubmed/25057016 http://dx.doi.org/10.1091/mbc.E14-03-0786 Text en © 2014 Zheng et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Zheng, Fan
Li, Tianpeng
Jin, Dong-yan
Syrovatkina, Viktoriya
Scheffler, Kathleen
Tran, Phong T.
Fu, Chuanhai
Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
title Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
title_full Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
title_fullStr Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
title_full_unstemmed Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
title_short Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation
title_sort csi1p recruits alp7p/tacc to the spindle pole bodies for bipolar spindle formation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4161510/
https://www.ncbi.nlm.nih.gov/pubmed/25057016
http://dx.doi.org/10.1091/mbc.E14-03-0786
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