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Cooperation between MDM2 and MDMX in the regulation of p53

Cooperation between MDM2 and MDMX in the regulation of p53
Cooperation between MDM2 and MDMX in the regulation of p53
Murine double minute-2 (MDM2) was first described as a p53-associated protein and potential oncogene in the early 1990s. Its paralogue MDMX was subsequently identified in a screen for p53-binding proteins. Extensive evidence now confirms both proteins to be oncogenic in both mice and humans, largely through their ability to negatively regulate the tumour-suppressor activities of p53. It is now clear that the two proteins form heterodimers, and act in concert to regulate p53 activity in proliferating and stressed cells. In this chapter I firstly review the several mechanisms whereby MDM2 and MDMX are potentially able to regulate p53 function independently of each other. I then examine how heterodimerisation between the two molecules influences how they regulate the abundance and activity of both p53, and each other. I conclude by examining current models of how the dynamic equilibrium between p53 and its two negative regulators is maintained in proliferating cells, and is targeted by multiple signalling pathways to control the magnitude and duration of the p53-dependent transcriptional response to genotoxic stress.
978-1-4419-8230-8
83-97
Landes Bioscience
Blaydes, Jeremy
e957f999-fd91-4f77-ad62-5b4ef069b15b
Hupp, T.R.
Ayed, A.
Blaydes, Jeremy
e957f999-fd91-4f77-ad62-5b4ef069b15b
Hupp, T.R.
Ayed, A.

Blaydes, Jeremy (2010) Cooperation between MDM2 and MDMX in the regulation of p53. In, Hupp, T.R. and Ayed, A. (eds.) p53. Austin, USA. Landes Bioscience, pp. 83-97.

Record type: Book Section

Abstract

Murine double minute-2 (MDM2) was first described as a p53-associated protein and potential oncogene in the early 1990s. Its paralogue MDMX was subsequently identified in a screen for p53-binding proteins. Extensive evidence now confirms both proteins to be oncogenic in both mice and humans, largely through their ability to negatively regulate the tumour-suppressor activities of p53. It is now clear that the two proteins form heterodimers, and act in concert to regulate p53 activity in proliferating and stressed cells. In this chapter I firstly review the several mechanisms whereby MDM2 and MDMX are potentially able to regulate p53 function independently of each other. I then examine how heterodimerisation between the two molecules influences how they regulate the abundance and activity of both p53, and each other. I conclude by examining current models of how the dynamic equilibrium between p53 and its two negative regulators is maintained in proliferating cells, and is targeted by multiple signalling pathways to control the magnitude and duration of the p53-dependent transcriptional response to genotoxic stress.

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Published date: 2010

Identifiers

Local EPrints ID: 66670
URI: http://eprints.soton.ac.uk/id/eprint/66670
ISBN: 978-1-4419-8230-8
PURE UUID: dc0e79e8-dc34-4b62-b127-3c2a68fcd9bc
ORCID for Jeremy Blaydes: ORCID iD orcid.org/0000-0001-8525-0209

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Date deposited: 08 Jul 2009
Last modified: 12 Sep 2020 01:34

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Contributors

Author: Jeremy Blaydes ORCID iD
Editor: T.R. Hupp
Editor: A. Ayed

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