| Literature DB >> 19091744 |
Joseph Avruch1, Ramnik Xavier, Nabeel Bardeesy, Xian-Feng Zhang, Maria Praskova, Dawang Zhou, Fan Xia.
Abstract
The Rassf1-6 polypeptides each contain a Ras/Rap association domain, which enables binding to several GTP-charged Ras-like GTPases, at least in vitro or when overexpressed. The Ras/Rap association domains are followed by SARAH domains, which mediate Rassf heterodimerization with the Mst1/2 protein kinases. Rassf1A is unequivocally a tumor suppressor, and all Rassf proteins behave like tumor suppressors, exhibiting epigenetic silencing of expression in many human cancers and pro-apoptotic and/or anti-proliferative effects when re-expressed in tumor cell lines. Herein, we review the binding of the Rassf polypeptides to Ras-like GTPases and the Mst1/2 kinases and their role in Rassf function.Entities:
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Year: 2008 PMID: 19091744 PMCID: PMC2670104 DOI: 10.1074/jbc.R800073200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157