Mitotic Kinases and p53 Signaling

Mitosis is tightly regulated and any errors in this process often lead to aneuploidy, genomic instability, and tumorigenesis. Deregulation of mitotic kinases is significantly associated with improper cell division and aneuploidy. Because of their importance during mitosis and the relevance to ca...

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Main Authors: Geun-Hyoung Ha, Eun-Kyoung Yim Breuer
Format: Article
Language:English
Published: Hindawi Limited 2012-01-01
Series:Biochemistry Research International
Online Access:http://dx.doi.org/10.1155/2012/195903
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spelling doaj-66f235bf67bf47ce8af0425f252f4fc72020-11-24T23:47:23ZengHindawi LimitedBiochemistry Research International2090-22472090-22552012-01-01201210.1155/2012/195903195903Mitotic Kinases and p53 SignalingGeun-Hyoung Ha0Eun-Kyoung Yim Breuer1Department of Radiation Oncology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153, USADepartment of Radiation Oncology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153, USAMitosis is tightly regulated and any errors in this process often lead to aneuploidy, genomic instability, and tumorigenesis. Deregulation of mitotic kinases is significantly associated with improper cell division and aneuploidy. Because of their importance during mitosis and the relevance to cancer, mitotic kinase signaling has been extensively studied over the past few decades and, as a result, several mitotic kinase inhibitors have been developed. Despite promising preclinical results, targeting mitotic kinases for cancer therapy faces numerous challenges, including safety and patient selection issues. Therefore, there is an urgent need to better understand the molecular mechanisms underlying mitotic kinase signaling and its interactive network. Increasing evidence suggests that tumor suppressor p53 functions at the center of the mitotic kinase signaling network. In response to mitotic spindle damage, multiple mitotic kinases phosphorylate p53 to either activate or deactivate p53-mediated signaling. p53 can also regulate the expression and function of mitotic kinases, suggesting the existence of a network of mutual regulation, which can be positive or negative, between mitotic kinases and p53 signaling. Therefore, deciphering this regulatory network will provide knowledge to overcome current limitations of targeting mitotic kinases and further improve the results of targeted therapy.http://dx.doi.org/10.1155/2012/195903
collection DOAJ
language English
format Article
sources DOAJ
author Geun-Hyoung Ha
Eun-Kyoung Yim Breuer
spellingShingle Geun-Hyoung Ha
Eun-Kyoung Yim Breuer
Mitotic Kinases and p53 Signaling
Biochemistry Research International
author_facet Geun-Hyoung Ha
Eun-Kyoung Yim Breuer
author_sort Geun-Hyoung Ha
title Mitotic Kinases and p53 Signaling
title_short Mitotic Kinases and p53 Signaling
title_full Mitotic Kinases and p53 Signaling
title_fullStr Mitotic Kinases and p53 Signaling
title_full_unstemmed Mitotic Kinases and p53 Signaling
title_sort mitotic kinases and p53 signaling
publisher Hindawi Limited
series Biochemistry Research International
issn 2090-2247
2090-2255
publishDate 2012-01-01
description Mitosis is tightly regulated and any errors in this process often lead to aneuploidy, genomic instability, and tumorigenesis. Deregulation of mitotic kinases is significantly associated with improper cell division and aneuploidy. Because of their importance during mitosis and the relevance to cancer, mitotic kinase signaling has been extensively studied over the past few decades and, as a result, several mitotic kinase inhibitors have been developed. Despite promising preclinical results, targeting mitotic kinases for cancer therapy faces numerous challenges, including safety and patient selection issues. Therefore, there is an urgent need to better understand the molecular mechanisms underlying mitotic kinase signaling and its interactive network. Increasing evidence suggests that tumor suppressor p53 functions at the center of the mitotic kinase signaling network. In response to mitotic spindle damage, multiple mitotic kinases phosphorylate p53 to either activate or deactivate p53-mediated signaling. p53 can also regulate the expression and function of mitotic kinases, suggesting the existence of a network of mutual regulation, which can be positive or negative, between mitotic kinases and p53 signaling. Therefore, deciphering this regulatory network will provide knowledge to overcome current limitations of targeting mitotic kinases and further improve the results of targeted therapy.
url http://dx.doi.org/10.1155/2012/195903
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