The lateral compartmentation of the yeast plasma membrane
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
20641012
DOI
10.1002/yea.1772
Knihovny.cz E-resources
- MeSH
- Models, Biological MeSH
- Cell Membrane chemistry metabolism ultrastructure MeSH
- Microscopy, Confocal MeSH
- Membrane Microdomains chemistry metabolism ultrastructure MeSH
- Saccharomyces cerevisiae Proteins metabolism MeSH
- Saccharomyces cerevisiae chemistry metabolism ultrastructure MeSH
- Amino Acid Transport Systems, Basic metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- CAN1 protein, S cerevisiae MeSH Browser
- Saccharomyces cerevisiae Proteins MeSH
- Amino Acid Transport Systems, Basic MeSH
The plasma membrane of Saccharomyces cerevisiae contains large microdomains enriched in ergosterol, which house at least nine integral proteins, including proton symporters. The domains adopt a characteristic structure of furrow-like invaginations typically seen in freeze-fracture pictures of fungal cells. Being stable for the time comparable with the cell cycle duration, they might be considered as fixed islands (rafts) in an otherwise fluid yeast plasma membrane. Rapidly moving endocytic marker proteins avoid the microdomains; the domain-accumulated proton symporters consequently show a reduced rate of substrate-induced endocytosis and turnover.
References provided by Crossref.org
Eisosomes promote the ability of Sur7 to regulate plasma membrane organization in Candida albicans
