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Cited by 105

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Tetramer formation of tumor suppressor protein p53: Structure, function, and applications

Kamada, Rui, Toguchi, Yu, Nomura, Takao, Imagawa, Toshiaki, Sakaguchi, Kazuyasu·2016·Peptide Science
DOI 10.1002/bip.22772
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Abstract

Tetramer formation of p53 is essential for its tumor suppressor function. p53 not only acts as a tumor suppressor protein by inducing cell cycle arrest and apoptosis in response to genotoxic stress, but it also regulates other cellular processes, including autophagy, stem cell self‐renewal, and reprogramming of differentiated cells into stem cells, immune system, and metastasis. More than 50% of human tumors have TP53 gene mutations, and most of them are missense mutations that presumably reduce tumor suppressor activity of p53. This review focuses on the role of the tetramerization (oligomerization), which is modulated by the protein concentration of p53, posttranslational modifications, and/or interactions with its binding proteins, in regulating the tumor suppressor function of p53. Functional control of p53 by stabilizing or inhibiting oligomer formation and its bio‐applications are also discussed. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 598–612, 2016.

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Metadata

Authors
Kamada, R., Toguchi, Y., Nomura, T., Imagawa, T., & Sakaguchi, K.
Affiliations
  • Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science Hokkaido University Sapporo 060‐0810 Japan
  • Center for Research and Education on Drug Discovery Faculty of Pharmaceutical Sciences, Hokkaido University Sapporo 060‐0812 Japan
Venue
Peptide Science
Publisher
Wiley
Published
2016-07
Volume
106
Issue
4
Pages
598-612
ISSN
0006-3525
DOI
10.1002/bip.22772
Cited by
105
References
15
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 21 d)

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