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Assembly of fission yeast eisosomes in the plasma membrane of budding yeast: import of foreign membrane microdomains
K. Vaskovicova, V. Stradalova, A. Efenberk, M. Opekarova, J. Malinsky,
Language English Country Germany
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Cell Membrane metabolism MeSH
- Cytoskeletal Proteins metabolism MeSH
- Phosphoproteins metabolism MeSH
- Membrane Microdomains metabolism MeSH
- Membrane Proteins metabolism MeSH
- Saccharomyces cerevisiae Proteins metabolism MeSH
- Saccharomyces cerevisiae metabolism MeSH
- Schizosaccharomyces pombe Proteins metabolism MeSH
- Schizosaccharomyces metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Eisosomes are plasma membrane-associated protein complexes organizing the membrane compartment of Can1 (MCC), a membrane microdomain of specific structure and function in ascomycetous fungi. By heterologous expression of specific components of Schizosaccharomyces pombe eisosomes in Saccharomyces cerevisiae we reconstitute structures exhibiting the composition and morphology of S. pombe eisosome in the host plasma membrane. We show S. pombe protein Pil1 (SpPil1) to substitute the function of its S. cerevisiae homologue in building plasma membrane-associated assemblies recognized by inherent MCC/eisosome constituents Sur7 and Seg1. Our data indicate that binding of SpPil1 to the plasma membrane of S. cerevisiae also induces formation of furrow-like invaginations characteristic for MCC. To the best of our knowledge, this is the first report of interspecies transfer of a functional plasma membrane microdomain. In the described system, we identify a striking difference between eisosome stabilizer proteins Seg1 and SpSle1. While Seg1 recruits both Pil1 and SpPil1 to the plasma membrane, SpSle1 recognizes only its natural counterpart, SpPil1. In the presence of Pil1, SpSle1 is segregated outside the Pil1-organized eisosomes and forms independent microdomains in the host membrane.
References provided by Crossref.org
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