The N-terminal RASSF family: a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation

Sherwood, V., Recino, A., Jeffries, A., Ward, A. and Chalmers, A. D. (2010) The N-terminal RASSF family: a new group of Ras-association-domain-containing proteins, with emerging links to cancer formation. Biochemical Journal, 425. pp. 303-311. ISSN 0264-6021

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Abstract

The RASSF (Ras-association domain family) has recently gained several new members and now contains ten proteins (RASSF1-10), several of which are potential tumour suppressors. The family can be split into two groups, the classical RASSF proteins (RASSF1-6) and the four recently added N-terminal RASSF proteins (RASSF7-10). The N-terminal RASSF proteins have a number of differences from the classical RASSF members and represent a newly defined set of potential Ras effectors. They have been linked to key biological processes, including cell death, proliferation, microtubule stability, promoter methylation, vesicle trafficking and response to hypoxia. Two members of the N-terminal RASSF family have also been highlighted as potential tumour suppressors. The present review will summarize what is known about the N-terminal RASSF proteins, addressing their function and possible links to cancer formation. It will also compare the N-terminal RASSF proteins with the classical RASSF proteins and ask whether the N-terminal RASSF proteins should be considered as genuine members or imposters in the RASSF family.

Item Type: Article
Uncontrolled Keywords: lung,hras1 minisatellite locus,cell-cycle progression,adenocarcinoma risk,gene-expression,binding domains,hippo pathway,tumour,suppressor,kinase aurora-a,n-terminal ras-association domain family (rassf7-10),breast-cancer,ubiquitin fold,microtubule stability,tumor-suppressor rassf1a
Faculty \ School: Faculty of Science > School of Pharmacy
Depositing User: Rachel Smith
Date Deposited: 07 Jun 2011 15:57
Last Modified: 21 Apr 2020 17:20
URI: https://ueaeprints.uea.ac.uk/id/eprint/31979
DOI: 10.1042/bj20091318

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