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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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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. |
format | Online Article Text |
id | pubmed-4161510 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
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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