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PMID: 12477802 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Rvs161p and sphingolipids are required for actin repolarization following salt stress.

Eukaryotic cell ·Vol. 1 ·No. 6 ·2002-12-00 ·Pages 1021-31

Balguerie A, Bagnat M, Bonneu M, Aigle M, Breton AM

Abstract

In Saccharomyces cerevisiae, the actin cytoskeleton is depolarized by NaCl stress. In this study, the response was maximal after 30 min, and then actin patches repolarized. Rvs161p was required for actin repolarization because the rvs161delta mutant did not repolarize actin patches after growth in a salt medium. Mutations suppressing the rvs161delta-related salt sensitivity all occurred in genes required for sphingolipid biosynthesis: FEN1, SUR4, SUR2, SUR1, and IPT1. These suppressors also suppressed act1-1-related salt sensitivity and the defect in actin repolarization of the rvs161delta mutant, providing a link between sphingolipids and actin polarization. Indeed, deletion of the suppressor genes suppressed the rvs161delta defect in actin repolarization in two ways: either actin was not depolarized at the wild-type level in a set of suppressor mutants, or actin was repolarized in the absence of Rvs161p in the other suppressor mutants. Rvs161p was localized as cortical patches that concentrated at polarization sites, i.e., bud emergence and septa, and was found to be associated with lipid rafts. An important link between sphingolipids and actin polarization is that Rvs161p was required for actin repolarization and was found to be located in lipid rafts.

MeSH Terms
Actins/metabolism Cell Membrane/metabolism Cytoskeletal Proteins/metabolism,physiology Green Fluorescent Proteins Luminescent Proteins/metabolism Membrane Microdomains Microscopy, Fluorescence Models, Biological Mutation Plasmids/metabolism Recombinant Fusion Proteins/metabolism Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins/metabolism,physiology Salts/pharmacology Sodium Chloride/pharmacology Sphingolipids/metabolism,physiology Temperature Time Factors
Chemicals
Actins Cytoskeletal Proteins Luminescent Proteins RVS161 protein, S cerevisiae Recombinant Fusion Proteins Saccharomyces cerevisiae Proteins Salts Sphingolipids Green Fluorescent Proteins Sodium Chloride
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Balguerie Axelle
Institut de Biochimie et Génétique Cellulaires, CNRS UMR 5095, F-33077 Bordeaux Cedex, France.
Bagnat Michel
Bonneu Marc
Aigle Michel
Breton Annick M
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Article Info
Journal
Eukaryotic cell
Abbr.
Eukaryot Cell
ISSN
1535-9778
DOI
10.1128/EC.1.6.1021-1031.2002
Published
2002-12-00
Pages
1021-31
Language
English
Region
United States
NLM ID
101130731
PMCID
PMC138763
Subset
IM
External Links
PubMed source DOI: 10.1128/EC.1.6.1021-1031.2002 PMC Full Text View journal details
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