Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association

DOIResolve DOI: http://doi.org/10.1101/gad.1375706
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TypeArticle
Volume20
Issue6
Pages734746; # of pages: 13
Subjectpha; Protein; Yeast
AbstractIn a variety of yeast cellular pathways, the Ste50p protein regulates the kinase function of the mitogen extracellular signal-regulated kinase kinase (MEKK) Ste11p. Both Ste11p and Ste50p contain sterile alpha motif (SAM) domains; these are interchangeable, and can be replaced by other protein -interacting modules. Furthermore, the function of the Ras association (RA) -like domain of Ste50p can be mimicked by a plasma membrane recruiting signal, and direct plasma membrane targeting of Ste11p bypasses the requirement of Ste50p for Ste11p function. Thus the regulatory role of Ste50p requires both the N-terminal SAM domain to bind Ste11p and the C-terminal RA-like domain to direct kinase localization. We have identified Opy2p, an integral membrane protein that can interact with Ste50p, as a new component in the Sho1p -Ste11p/Ste50p signaling branch of the high-osmolarity glycerol (HOG) pathway. We propose that Opy2p can serve as a membrane anchor for the Ste50p/Ste11p module in the activation of the HOG pathway
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47497
NPARC number3539509
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Record identifierd68c30ac-d7d6-4a46-81d3-29180b174716
Record created2009-03-01
Record modified2016-05-09
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