Patchwork organization of the yeast plasma membrane into numerous coexisting domains
- PMID: 22544065
- DOI: 10.1038/ncb2487
Patchwork organization of the yeast plasma membrane into numerous coexisting domains
Abstract
The plasma membrane is made up of lipids and proteins, and serves as an active interface between the cell and its environment. Many plasma-membrane proteins are laterally segregated in the plane of the membrane, but the underlying mechanisms remain controversial. Here we investigate the distribution and dynamics of a representative set of plasma-membrane-associated proteins in yeast cells. These proteins were distributed non-homogeneously in patterns ranging from distinct patches to nearly continuous networks, and these patterns were in turn strongly influenced by the lipid composition of the plasma membrane. Most proteins segregated into distinct domains. However, proteins with similar or identical transmembrane sequences (TMSs) showed a marked tendency to co-localize. Indeed we could predictably relocate proteins by swapping their TMSs. Finally, we found that the domain association of plasma-membrane proteins has an impact on their function. Our results are consistent with self-organization of biological membranes into a patchwork of coexisting domains.
Similar articles
-
Periprotein lipidomes of Saccharomyces cerevisiae provide a flexible environment for conformational changes of membrane proteins.Elife. 2020 Apr 17;9:e57003. doi: 10.7554/eLife.57003. Elife. 2020. PMID: 32301705 Free PMC article.
-
Building a patchwork - The yeast plasma membrane as model to study lateral domain formation.Biochim Biophys Acta. 2015 Apr;1853(4):767-74. doi: 10.1016/j.bbamcr.2014.12.019. Epub 2014 Dec 22. Biochim Biophys Acta. 2015. PMID: 25541280 Review.
-
Eisosome-driven plasma membrane organization is mediated by BAR domains.Nat Struct Mol Biol. 2011 Jun 19;18(7):854-6. doi: 10.1038/nsmb.2080. Nat Struct Mol Biol. 2011. PMID: 21685922
-
Organized living: formation mechanisms and functions of plasma membrane domains in yeast.Trends Cell Biol. 2012 Mar;22(3):151-8. doi: 10.1016/j.tcb.2011.12.002. Epub 2012 Jan 12. Trends Cell Biol. 2012. PMID: 22245053 Review.
-
Eisosome proteins assemble into a membrane scaffold.J Cell Biol. 2011 Nov 28;195(5):889-902. doi: 10.1083/jcb.201104040. J Cell Biol. 2011. PMID: 22123866 Free PMC article.
Cited by
-
Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiol Mol Biol Rev. 2019 Oct 16;83(4):e00024-19. doi: 10.1128/MMBR.00024-19. Print 2019 Nov 20. Microbiol Mol Biol Rev. 2019. PMID: 31619504 Free PMC article. Review.
-
Inhibitor-Resistant Mutants Give Important Insights into Candida albicans ABC Transporter Cdr1 Substrate Specificity and Help Elucidate Efflux Pump Inhibition.Antimicrob Agents Chemother. 2022 Jan 18;66(1):e0174821. doi: 10.1128/AAC.01748-21. Epub 2021 Nov 15. Antimicrob Agents Chemother. 2022. PMID: 34780272 Free PMC article.
-
Periprotein lipidomes of Saccharomyces cerevisiae provide a flexible environment for conformational changes of membrane proteins.Elife. 2020 Apr 17;9:e57003. doi: 10.7554/eLife.57003. Elife. 2020. PMID: 32301705 Free PMC article.
-
Endogenous sphingomyelin segregates into submicrometric domains in the living erythrocyte membrane.J Lipid Res. 2014 Jul;55(7):1331-42. doi: 10.1194/jlr.M048538. Epub 2014 May 14. J Lipid Res. 2014. PMID: 24826836 Free PMC article.
-
Competing Lipid-Protein and Protein-Protein Interactions Determine Clustering and Gating Patterns in the Potassium Channel from Streptomyces lividans (KcsA).J Biol Chem. 2015 Oct 16;290(42):25745-55. doi: 10.1074/jbc.M115.669598. Epub 2015 Sep 2. J Biol Chem. 2015. PMID: 26336105 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
