Rassf family of tumor suppressor polypeptides.
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.
Avruch
Joseph
J
Department of Molecular Biology, Massachusetts General Hospital, Boston, MA, USA. avruch@molbio.mgh.harvard.edu
Xavier
Ramnik
R
Bardeesy
Nabeel
N
Zhang
Xian-Feng
XF
Praskova
Maria
M
Zhou
Dawang
D
Xia
Fan
F
D045744:Cell Line, Tumor; D049109:Cell Proliferation; D019281:Dimerization; D044127:Epigenesis, Genetic; D020558:GTP Phosphohydrolases / Q000378:metabolism; D015972:Gene Expression Regulation, Neoplastic; D020868:Gene Silencing; D006801:Humans; D008954:Models, Biological; D005810:Multigene Family; D009369:Neoplasms / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding; D025521:Tumor Suppressor Proteins / Q000378:metabolism / Q000502:physiology*
D010455:Peptides; C411762:RASSF1 protein, human; D025521:Tumor Suppressor Proteins; D020558:GTP Phosphohydrolases