title: Erv14 cargo receptor participates in yeast salt tolerance via its interaction with the plasma-membrane Nha1 cation/proton antiporter.
abstract: 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.
authors.affiliation: Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca, Morelos 62250, Mexico. Electronic address: rosas.paul@gmail.com.
authors.forename: Paul
authors.initials: P
authors.lastname: Rosas-Santiago
authors.affiliation: Department of Membrane Transport, Institute of Physiology Czech Academy of Sciences, v.v.i., Videnska 1083, Prague 4 - Krc, 142 20, Czech Republic. Electronic address: Olga.Zimmermannova@fgu.cas.cz.
authors.forename: Olga
authors.initials: O
authors.lastname: Zimmermannova
authors.affiliation: Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca, Morelos 62250, Mexico. Electronic address: rosario@ibt.unam.mx.
authors.forename: Rosario
authors.initials: R
authors.lastname: Vera-Estrella
authors.affiliation: Department of Membrane Transport, Institute of Physiology Czech Academy of Sciences, v.v.i., Videnska 1083, Prague 4 - Krc, 142 20, Czech Republic. Electronic address: Hana.Sychrova@fgu.cas.cz.
authors.forename: Hana
authors.initials: H
authors.lastname: Sychrová
authors.affiliation: Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, Cuernavaca, Morelos 62250, Mexico. Electronic address: omar@ibt.unam.mx.
authors.forename: Omar
authors.initials: O
authors.lastname: Pantoja
mesh_terms: D001692:Biological Transport; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002414:Cations, Monovalent; D015966:Gene Expression Regulation, Fungal; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011188:Potassium / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011522:Protons; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D055049:Salt Tolerance; D012965:Sodium Chloride / Q000378:metabolism* / Q000494:pharmacology; D017923:Sodium-Hydrogen Exchangers / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D027682:Cation Transport Proteins; D002414:Cations, Monovalent; C493590:Erv14 protein, S cerevisiae; D008565:Membrane Proteins; C000631624:NHA1 protein, S cerevisiae; D011522:Protons; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D017923:Sodium-Hydrogen Exchangers; D012965:Sodium Chloride; D011188:Potassium
keywords: Erv14p; Mislocalization; Nha1p; Protein–protein interaction; Salt-tolerance; Yeast