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An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes
Eukaryotic cells may divide via the critical cellular process of cell division/mitosis, resulting in two daughter cells with the same genetic information. A large number of dedicated proteins are involved in this process and spatiotemporally assembled into three distinct super-complex structures/org...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4212687/ https://www.ncbi.nlm.nih.gov/pubmed/25400627 http://dx.doi.org/10.3389/fmicb.2014.00573 |
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author | Zheng, Yueyuan Guo, Junjie Li, Xu Xie, Yubin Hou, Mingming Fu, Xuyang Dai, Shengkun Diao, Rucheng Miao, Yanyan Ren, Jian |
author_facet | Zheng, Yueyuan Guo, Junjie Li, Xu Xie, Yubin Hou, Mingming Fu, Xuyang Dai, Shengkun Diao, Rucheng Miao, Yanyan Ren, Jian |
author_sort | Zheng, Yueyuan |
collection | PubMed |
description | Eukaryotic cells may divide via the critical cellular process of cell division/mitosis, resulting in two daughter cells with the same genetic information. A large number of dedicated proteins are involved in this process and spatiotemporally assembled into three distinct super-complex structures/organelles, including the centrosome/spindle pole body, kinetochore/centromere and cleavage furrow/midbody/bud neck, so as to precisely modulate the cell division/mitosis events of chromosome alignment, chromosome segregation and cytokinesis in an orderly fashion. In recent years, many efforts have been made to identify the protein components and architecture of these subcellular organelles, aiming to uncover the organelle assembly pathways, determine the molecular mechanisms underlying the organelle functions, and thereby provide new therapeutic strategies for a variety of diseases. However, the organelles are highly dynamic structures, making it difficult to identify the entire components. Here, we review the current knowledge of the identified protein components governing the organization and functioning of organelles, especially in human and yeast cells, and discuss the multi-localized protein components mediating the communication between organelles during cell division. |
format | Online Article Text |
id | pubmed-4212687 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-42126872014-11-14 An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes Zheng, Yueyuan Guo, Junjie Li, Xu Xie, Yubin Hou, Mingming Fu, Xuyang Dai, Shengkun Diao, Rucheng Miao, Yanyan Ren, Jian Front Microbiol Microbiology Eukaryotic cells may divide via the critical cellular process of cell division/mitosis, resulting in two daughter cells with the same genetic information. A large number of dedicated proteins are involved in this process and spatiotemporally assembled into three distinct super-complex structures/organelles, including the centrosome/spindle pole body, kinetochore/centromere and cleavage furrow/midbody/bud neck, so as to precisely modulate the cell division/mitosis events of chromosome alignment, chromosome segregation and cytokinesis in an orderly fashion. In recent years, many efforts have been made to identify the protein components and architecture of these subcellular organelles, aiming to uncover the organelle assembly pathways, determine the molecular mechanisms underlying the organelle functions, and thereby provide new therapeutic strategies for a variety of diseases. However, the organelles are highly dynamic structures, making it difficult to identify the entire components. Here, we review the current knowledge of the identified protein components governing the organization and functioning of organelles, especially in human and yeast cells, and discuss the multi-localized protein components mediating the communication between organelles during cell division. Frontiers Media S.A. 2014-10-29 /pmc/articles/PMC4212687/ /pubmed/25400627 http://dx.doi.org/10.3389/fmicb.2014.00573 Text en Copyright © 2014 Zheng, Guo, Li, Xie, Hou, Fu, Dai, Diao, Miao and Ren. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Zheng, Yueyuan Guo, Junjie Li, Xu Xie, Yubin Hou, Mingming Fu, Xuyang Dai, Shengkun Diao, Rucheng Miao, Yanyan Ren, Jian An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
title | An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
title_full | An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
title_fullStr | An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
title_full_unstemmed | An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
title_short | An integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
title_sort | integrated overview of spatiotemporal organization and regulation in mitosis in terms of the proteins in the functional supercomplexes |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4212687/ https://www.ncbi.nlm.nih.gov/pubmed/25400627 http://dx.doi.org/10.3389/fmicb.2014.00573 |
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