Erv14 cargo receptor participates in yeast salt tolerance via its interaction with the plasma-membrane Nha1 cation/proton antiporter
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
26440927
DOI
10.1016/j.bbamem.2015.09.024
PII: S0005-2736(15)00328-4
Knihovny.cz E-resources
- Keywords
- Erv14p, Mislocalization, Nha1p, Protein–protein interaction, Salt-tolerance, Yeast,
- MeSH
- Biological Transport MeSH
- Sodium Chloride metabolism pharmacology MeSH
- Potassium metabolism pharmacology MeSH
- Protein Interaction Domains and Motifs MeSH
- Cations, Monovalent MeSH
- Membrane Proteins chemistry genetics metabolism MeSH
- Protein Multimerization MeSH
- Sodium-Hydrogen Exchangers chemistry genetics metabolism MeSH
- Cation Transport Proteins chemistry genetics metabolism MeSH
- Protons * MeSH
- Gene Expression Regulation, Fungal * MeSH
- Recombinant Fusion Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae Proteins chemistry genetics metabolism MeSH
- Saccharomyces cerevisiae drug effects genetics metabolism MeSH
- Protein Structure, Secondary MeSH
- Salt Tolerance MeSH
- Protein Binding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Sodium Chloride MeSH
- Potassium MeSH
- Erv14 protein, S cerevisiae MeSH Browser
- Cations, Monovalent MeSH
- Membrane Proteins MeSH
- Sodium-Hydrogen Exchangers MeSH
- NHA1 protein, S cerevisiae MeSH Browser
- Cation Transport Proteins MeSH
- Protons * MeSH
- Recombinant Fusion Proteins MeSH
- Saccharomyces cerevisiae Proteins MeSH
The yeast Nha1p Na(+), K(+)/H(+) antiporter has a house-keeping role in pH and cation homeostasis. It is also needed to alleviate excess Na(+) or K(+) from the cytoplasm under high external concentrations of these cations. Erv14p, a putative cargo receptor for transmembrane proteins is required for trafficking of Nha1p from the endoplasmic reticulum to the plasma membrane. Sensitivity to high Na(+) concentrations of the erv14 mutant associated to the intracellular mislocalization of Nha1p-GFP, together with a lower Na(+) efflux, indicate the involvement of this mutual association to accomplish the survival of the yeast cell upon sodium stress. This observation is supported by the protein-protein interaction between Erv14p and Nha1p detected by the mating-based Split Ubiquitin System and co-immunoprecipitation assays. Our results indicate that even though Erv14p interacts with Nha1p through the TMD, the C-terminal is important not only for the efficient delivery of Nha1p to the plasma membrane but also for its dimerization to accomplish its role in yeast salt tolerance.
References provided by Crossref.org
The Role of Cornichons in the Biogenesis and Functioning of Monovalent-Cation Transport Systems