Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling

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Title Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling
Author Schroder, Wayne Ashley; Buck, Marion; Cloonan, Nicole; Hancock, John F.; Suhrbier, Andreas; Sculley, Tom Brian; Bushell, Gillian Robin
Journal Name Cellular Signalling
Year Published 2007
Place of publication United States
Publisher Elsevier Inc.
Abstract Human Sin1 (SAPK-interacting protein 1) is a member of a conserved family of orthologous proteins that have an essential role in signal transduction in yeast and Dictyostelium. This study demonstrates that most Sin1 orthologues contain both a Raf-like Ras-binding domain (RBD) and a pleckstrin homology (PH) domain. These domains are functional in the human Sin1 protein, with the PH domain involved in lipid and membrane binding by Sin1, and the RBD able to bind activated H-and K-Ras. Sin1 and Ras co-immunoprecipitated and co-localised, showing that these proteins associate with each other in vivo. Overexpression of Sin1 inhibited the activation of ERK, Akt and JNK signalling pathways by Ras. In contrast, siRNA knockdown of endogenous Sin1 protein expression in HEK293 cells enhanced the activation of ERK1/2 by Ras. These data suggest that Sin1 is a mammalian Ras-inhibitor.
Peer Reviewed Yes
Published Yes
Publisher URI http://www.elsevier.com/wps/find/journaldescription.cws_home/525462/description#description
Alternative URI http://dx.doi.org/10.1016/j.cellsig.2007.01.013
Volume 19
Page from 1279
Page to 1289
ISSN 0898-6568
Date Accessioned 2007-06-19
Language en_AU
Faculty Faculty of Science, Environment, Engineering and Technology
Subject PRE2009-Protein Targeting and Signal Transduction
URI http://hdl.handle.net/10072/17399
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1

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