Erv14 cargo receptor participates in yeast salt tolerance via its interaction with the plasma-membrane Nha1 cation/proton antiporter
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
26440927
DOI
10.1016/j.bbamem.2015.09.024
PII: S0005-2736(15)00328-4
Knihovny.cz E-zdroje
- Klíčová slova
- Erv14p, Mislocalization, Nha1p, Protein–protein interaction, Salt-tolerance, Yeast,
- MeSH
- biologický transport MeSH
- chlorid sodný metabolismus farmakologie MeSH
- draslík metabolismus farmakologie MeSH
- interakční proteinové domény a motivy MeSH
- kationty jednomocné MeSH
- membránové proteiny chemie genetika metabolismus MeSH
- multimerizace proteinu MeSH
- Na(+)-H(+) antiport chemie genetika metabolismus MeSH
- proteiny přenášející kationty chemie genetika metabolismus MeSH
- protony * MeSH
- regulace genové exprese u hub * MeSH
- rekombinantní fúzní proteiny chemie genetika metabolismus MeSH
- Saccharomyces cerevisiae - proteiny chemie genetika metabolismus MeSH
- Saccharomyces cerevisiae účinky léků genetika metabolismus MeSH
- sekundární struktura proteinů MeSH
- tolerance k soli MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- chlorid sodný MeSH
- draslík MeSH
- Erv14 protein, S cerevisiae MeSH Prohlížeč
- kationty jednomocné MeSH
- membránové proteiny MeSH
- Na(+)-H(+) antiport MeSH
- NHA1 protein, S cerevisiae MeSH Prohlížeč
- proteiny přenášející kationty MeSH
- protony * MeSH
- rekombinantní fúzní proteiny MeSH
- Saccharomyces cerevisiae - proteiny 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.
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