Ato protein interactions in yeast plasma membrane revealed by fluorescence lifetime imaging (FLIM)
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
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-resources
- MeSH
- Models, Biological MeSH
- Cell Membrane metabolism MeSH
- Spectrometry, Fluorescence methods MeSH
- Fluorescence Recovery After Photobleaching MeSH
- Protein Interaction Mapping MeSH
- Membrane Proteins metabolism physiology MeSH
- Membrane Transport Proteins metabolism physiology MeSH
- Gene Expression Regulation, Fungal MeSH
- Fluorescence Resonance Energy Transfer methods MeSH
- Saccharomyces cerevisiae Proteins metabolism physiology MeSH
- Saccharomyces cerevisiae chemistry metabolism MeSH
- Signal Transduction MeSH
- Subcellular Fractions metabolism MeSH
- Green Fluorescent Proteins metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- ATO1 protein, S cerevisiae MeSH Browser
- ATO2 protein, S cerevisiae MeSH Browser
- ATO3 protein, S cerevisiae MeSH Browser
- Membrane Proteins MeSH
- Membrane Transport Proteins MeSH
- Saccharomyces cerevisiae Proteins MeSH
- Green Fluorescent Proteins 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.
References provided by Crossref.org
Membrane Protein Dimerization in Cell-Derived Lipid Membranes Measured by FRET with MC Simulations