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p73-Binding Partners and Their Functional Significance

p73 is one of the tumor-suppressor p53 family of nuclear transcription factor. As expected from the structural similarity between p53 and p73, p73 has a tumor-suppressive function. However, p73 was rarely mutated in human primary tumors. Under normal physiological conditions, p73 is kept at an extre...

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Detalles Bibliográficos
Autores principales: Ozaki, Toshinori, Kubo, Natsumi, Nakagawara, Akira
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195385/
https://www.ncbi.nlm.nih.gov/pubmed/22084676
http://dx.doi.org/10.1155/2010/283863
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author Ozaki, Toshinori
Kubo, Natsumi
Nakagawara, Akira
author_facet Ozaki, Toshinori
Kubo, Natsumi
Nakagawara, Akira
author_sort Ozaki, Toshinori
collection PubMed
description p73 is one of the tumor-suppressor p53 family of nuclear transcription factor. As expected from the structural similarity between p53 and p73, p73 has a tumor-suppressive function. However, p73 was rarely mutated in human primary tumors. Under normal physiological conditions, p73 is kept at an extremely low level to allow cells normal growth. In response to a certain subset of DNA damages, p73 is induced dramatically and transactivates an overlapping set of p53-target genes implicated in the promotion of cell cycle arrest and/or apoptotic cell death. Cells undergo cell cycle arrest and/or apoptotic cell death depending on the type and strength of DNA damages. p73 is regulated largely through the posttranslational modifications such as phosphorylation and acetylation. These chemical modifications are tightly linked to direct protein-protein interactions. In the present paper, the authors describe the functional significance of the protein-protein interactions in the regulation of proapoptotic p73.
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spelling pubmed-31953852011-11-14 p73-Binding Partners and Their Functional Significance Ozaki, Toshinori Kubo, Natsumi Nakagawara, Akira Int J Proteomics Review Article p73 is one of the tumor-suppressor p53 family of nuclear transcription factor. As expected from the structural similarity between p53 and p73, p73 has a tumor-suppressive function. However, p73 was rarely mutated in human primary tumors. Under normal physiological conditions, p73 is kept at an extremely low level to allow cells normal growth. In response to a certain subset of DNA damages, p73 is induced dramatically and transactivates an overlapping set of p53-target genes implicated in the promotion of cell cycle arrest and/or apoptotic cell death. Cells undergo cell cycle arrest and/or apoptotic cell death depending on the type and strength of DNA damages. p73 is regulated largely through the posttranslational modifications such as phosphorylation and acetylation. These chemical modifications are tightly linked to direct protein-protein interactions. In the present paper, the authors describe the functional significance of the protein-protein interactions in the regulation of proapoptotic p73. Hindawi Publishing Corporation 2010 2011-01-13 /pmc/articles/PMC3195385/ /pubmed/22084676 http://dx.doi.org/10.1155/2010/283863 Text en Copyright © 2010 Toshinori Ozaki et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Ozaki, Toshinori
Kubo, Natsumi
Nakagawara, Akira
p73-Binding Partners and Their Functional Significance
title p73-Binding Partners and Their Functional Significance
title_full p73-Binding Partners and Their Functional Significance
title_fullStr p73-Binding Partners and Their Functional Significance
title_full_unstemmed p73-Binding Partners and Their Functional Significance
title_short p73-Binding Partners and Their Functional Significance
title_sort p73-binding partners and their functional significance
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3195385/
https://www.ncbi.nlm.nih.gov/pubmed/22084676
http://dx.doi.org/10.1155/2010/283863
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