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Rassf Family of Tumor Suppressor Polypeptides*

By Joseph Avruch, Ramnik Xavier, Nabeel Bardeesy, Xian-feng Zhang, Maria Praskova, Dawang Zhou and Fan Xia


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

Topics: Minireviews
Publisher: American Society for Biochemistry and Molecular Biology
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Provided by: PubMed Central
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