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Characterization of the role of the tumor marker Nup88 in mitosis

Nuclear pore complexes are massive multiprotein channels responsible for traffic between the nucleus and cytoplasm, and are composed of approximately 30 proteins, termed nucleoporins (Nup). Our recent studies indicated that the nucleoporins Rae1 and Tpr play critical roles in maintaining the spindle...

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Autores principales: Hashizume, Chieko, Nakano, Hiroshi, Yoshida, Kimihisa, Wong, Richard W
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2890605/
https://www.ncbi.nlm.nih.gov/pubmed/20497554
http://dx.doi.org/10.1186/1476-4598-9-119
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author Hashizume, Chieko
Nakano, Hiroshi
Yoshida, Kimihisa
Wong, Richard W
author_facet Hashizume, Chieko
Nakano, Hiroshi
Yoshida, Kimihisa
Wong, Richard W
author_sort Hashizume, Chieko
collection PubMed
description Nuclear pore complexes are massive multiprotein channels responsible for traffic between the nucleus and cytoplasm, and are composed of approximately 30 proteins, termed nucleoporins (Nup). Our recent studies indicated that the nucleoporins Rae1 and Tpr play critical roles in maintaining the spindle bipolarity during cell division. In the present study, we found that another nucleoporin, Nup88, was localized on the spindles together with Nup214 during mitosis. Nup88 expression is linked to the progression of carcinogenesis, Nup88 has been proposed as a tumor marker. Overexpression of Nup88 enhanced multinucleated cell formation. RNAi-mediated knockdown of Nup88 disrupted Nup214 expression and localization and caused multipolar spindle phenotypes. Our data indicate that proper expression of Nup88 is critical for preventing aneuploidy formation and tumorigenesis.
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spelling pubmed-28906052010-06-24 Characterization of the role of the tumor marker Nup88 in mitosis Hashizume, Chieko Nakano, Hiroshi Yoshida, Kimihisa Wong, Richard W Mol Cancer Short communication Nuclear pore complexes are massive multiprotein channels responsible for traffic between the nucleus and cytoplasm, and are composed of approximately 30 proteins, termed nucleoporins (Nup). Our recent studies indicated that the nucleoporins Rae1 and Tpr play critical roles in maintaining the spindle bipolarity during cell division. In the present study, we found that another nucleoporin, Nup88, was localized on the spindles together with Nup214 during mitosis. Nup88 expression is linked to the progression of carcinogenesis, Nup88 has been proposed as a tumor marker. Overexpression of Nup88 enhanced multinucleated cell formation. RNAi-mediated knockdown of Nup88 disrupted Nup214 expression and localization and caused multipolar spindle phenotypes. Our data indicate that proper expression of Nup88 is critical for preventing aneuploidy formation and tumorigenesis. BioMed Central 2010-05-24 /pmc/articles/PMC2890605/ /pubmed/20497554 http://dx.doi.org/10.1186/1476-4598-9-119 Text en Copyright ©2010 Hashizume et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short communication
Hashizume, Chieko
Nakano, Hiroshi
Yoshida, Kimihisa
Wong, Richard W
Characterization of the role of the tumor marker Nup88 in mitosis
title Characterization of the role of the tumor marker Nup88 in mitosis
title_full Characterization of the role of the tumor marker Nup88 in mitosis
title_fullStr Characterization of the role of the tumor marker Nup88 in mitosis
title_full_unstemmed Characterization of the role of the tumor marker Nup88 in mitosis
title_short Characterization of the role of the tumor marker Nup88 in mitosis
title_sort characterization of the role of the tumor marker nup88 in mitosis
topic Short communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2890605/
https://www.ncbi.nlm.nih.gov/pubmed/20497554
http://dx.doi.org/10.1186/1476-4598-9-119
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