Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 150 (2004), 3281-3288; DOI  10.1099/mic.0.27264-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vay, H. A.
Right arrow Articles by Levin, D. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vay, H. A.
Right arrow Articles by Levin, D. E.
Agricola
Right arrow Articles by Vay, H. A.
Right arrow Articles by Levin, D. E.
Microbiology 150 (2004), 3281-3288; DOI  10.1099/mic.0.27264-0
© 2004 Society for General Microbiology

Mutational analysis of the cytoplasmic domain of the Wsc1 cell wall stress sensor

Heather A. Vay, Bevin Philip{dagger} and David E. Levin

Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, Baltimore, 615 N Wolfe St, MD 21205, USA

Correspondence
David E. Levin
levin{at}jhmi.edu

Wsc1 is a member of a family of highly O-glycosylated cell surface proteins that reside in the plasma membrane of Saccharomyces cerevisiae and function as sensors of cell wall stress. These proteins activate the cell wall integrity signalling pathway by stimulating the small G-protein Rho1, protein kinase C (Pkc1) and a MAP kinase cascade. The cytoplasmic domains of Wsc1 family members interact with the Rom2 guanine nucleotide exchange factor to stimulate GTP-binding of Rho1. Here, a mutational analysis of the cytoplasmic domain of Wsc1 is presented. The data identify two regions of the Wsc1 cytoplasmic tail that are conserved with other family members as important for Rom2 interaction. These regions are separated by an inhibitory region, which includes a cluster of seryl residues that appear to be phosphorylated. Mutational analysis of these residues supports a model in which Wsc1 interaction with Rom2 is negatively regulated by phosphorylation.


Abbreviations: {lambda}PPase, {lambda} protein phosphatase

{dagger}Present address: Wyeth Pharmaceuticals, Cambridge, MA 02140, USA.




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
R. Serrano, H. Martin, A. Casamayor, and J. Arino
Signaling Alkaline pH Stress in the Yeast Saccharomyces cerevisiae through the Wsc1 Cell Surface Sensor and the Slt2 MAPK Pathway
J. Biol. Chem., December 29, 2006; 281(52): 39785 - 39795.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2004 Society for General Microbiology.