The University of Southampton
University of Southampton Institutional Repository

Family friction as ?Np73 antagonises p73 and p53

Family friction as ?Np73 antagonises p73 and p53
Family friction as ?Np73 antagonises p73 and p53
p53 and its homolog p73 are responsible for guarding the genome and regulating cellular responses to genotoxic damage. However, life is never simple and in fact multiple isoforms of each gene exist which may have opposing functions. ?Np73 is a truncated isoform of p73 which lacks the N-terminal transactivation domain and is up-regulated in a number of diverse primary tumour types. Although its exact cellular function is unclear upregulation of ?Np73 has been linked to various pro-tumour activities. Here we review the current literature surrounding this mysterious protein and reveal its potentially important functions in tumourigenesis and treatment resistance.

?np73, p53, p73
1357-2725
482-486
Bailey, Sarah G.
3907c846-1c65-490a-81f1-653fea9ff7f0
Cragg, Mark S.
ec97f80e-f3c8-49b7-a960-20dff648b78c
Townsend, Paul A.
a2680443-664e-46d0-b4dd-97456ba810db
Bailey, Sarah G.
3907c846-1c65-490a-81f1-653fea9ff7f0
Cragg, Mark S.
ec97f80e-f3c8-49b7-a960-20dff648b78c
Townsend, Paul A.
a2680443-664e-46d0-b4dd-97456ba810db

Bailey, Sarah G., Cragg, Mark S. and Townsend, Paul A. (2011) Family friction as ?Np73 antagonises p73 and p53. International Journal of Biochemistry & Cell Biology, 43 (4), 482-486. (doi:10.1016/j.biocel.2010.12.022). (PMID:21216303)

Record type: Article

Abstract

p53 and its homolog p73 are responsible for guarding the genome and regulating cellular responses to genotoxic damage. However, life is never simple and in fact multiple isoforms of each gene exist which may have opposing functions. ?Np73 is a truncated isoform of p73 which lacks the N-terminal transactivation domain and is up-regulated in a number of diverse primary tumour types. Although its exact cellular function is unclear upregulation of ?Np73 has been linked to various pro-tumour activities. Here we review the current literature surrounding this mysterious protein and reveal its potentially important functions in tumourigenesis and treatment resistance.

This record has no associated files available for download.

More information

Accepted/In Press date: January 2011
Published date: April 2011
Keywords: ?np73, p53, p73

Identifiers

Local EPrints ID: 173397
URI: http://eprints.soton.ac.uk/id/eprint/173397
ISSN: 1357-2725
PURE UUID: b87a6b5b-5e3f-4602-85a9-98087b618240
ORCID for Mark S. Cragg: ORCID iD orcid.org/0000-0003-2077-089X

Catalogue record

Date deposited: 03 Feb 2011 15:24
Last modified: 14 Mar 2024 02:41

Export record

Altmetrics

Contributors

Author: Sarah G. Bailey
Author: Mark S. Cragg ORCID iD
Author: Paul A. Townsend

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×