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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,
Jazyk angličtina Země Německo
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- buněčná membrána metabolismus MeSH
- cytoskeletální proteiny metabolismus MeSH
- fosfoproteiny metabolismus MeSH
- membránové mikrodomény metabolismus MeSH
- membránové proteiny metabolismus MeSH
- Saccharomyces cerevisiae - proteiny metabolismus MeSH
- Saccharomyces cerevisiae metabolismus MeSH
- Schizosaccharomyces pombe - proteiny metabolismus MeSH
- Schizosaccharomyces metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem 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.
Citace poskytuje Crossref.org
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