Ato protein interactions in yeast plasma membrane revealed by fluorescence lifetime imaging (FLIM)
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
Grantová podpora
55005623
Howard Hughes Medical Institute - United States
PubMed
22579979
DOI
10.1016/j.bbamem.2012.05.005
PII: S0005-2736(12)00153-8
Knihovny.cz E-zdroje
- MeSH
- biologické modely MeSH
- buněčná membrána metabolismus MeSH
- fluorescenční spektrometrie metody MeSH
- FRAP MeSH
- mapování interakce mezi proteiny MeSH
- membránové proteiny metabolismus fyziologie MeSH
- membránové transportní proteiny metabolismus fyziologie MeSH
- regulace genové exprese u hub MeSH
- rezonanční přenos fluorescenční energie metody MeSH
- Saccharomyces cerevisiae - proteiny metabolismus fyziologie MeSH
- Saccharomyces cerevisiae chemie metabolismus MeSH
- signální transdukce MeSH
- subcelulární frakce metabolismus MeSH
- zelené fluorescenční proteiny metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- ATO1 protein, S cerevisiae MeSH Prohlížeč
- ATO2 protein, S cerevisiae MeSH Prohlížeč
- ATO3 protein, S cerevisiae MeSH Prohlížeč
- membránové proteiny MeSH
- membránové transportní proteiny MeSH
- Saccharomyces cerevisiae - proteiny MeSH
- zelené fluorescenční proteiny MeSH
Each of the three plasma membrane Ato proteins is involved in ammonium signalling and the development of yeast colonies. This suggests that although these proteins are homologous, they do not functionally substitute for each other, but may form a functional complex. Here, we present a detailed combined FRET, FLIM and photobleaching study, which enabled us to detect interactions between Ato proteins found in distinct compartments of yeast cells. We thus show that the proteins Ato1p and Ato2p interact and can form complexes when present in the plasma membrane. No interaction was detected between Ato1p and Ato3p or Ato2p and Ato3p. In addition, using specially prepared strains, we were able to detect an interaction between molecules of the same Ato protein, namely Ato1p-Ato1p and Ato3p-Ato3p, but not Ato2p-Ato2p.
Citace poskytuje Crossref.org
Membrane Protein Dimerization in Cell-Derived Lipid Membranes Measured by FRET with MC Simulations