Monovalent-cation homeostasis, crucial for all living cells, is ensured by the activity of various types of ion transport systems located either in the plasma membrane or in the membranes of organelles. A key prerequisite for the functioning of ion-transporting proteins is their proper trafficking to the target membrane. The cornichon family of COPII cargo receptors is highly conserved in eukaryotic cells. By simultaneously binding their cargoes and a COPII-coat subunit, cornichons promote the incorporation of cargo proteins into the COPII vesicles and, consequently, the efficient trafficking of cargoes via the secretory pathway. In this review, we summarize current knowledge about cornichon proteins (CNIH/Erv14), with an emphasis on yeast and mammalian cornichons and their role in monovalent-cation homeostasis. Saccharomyces cerevisiae cornichon Erv14 serves as a cargo receptor of a large portion of plasma-membrane proteins, including several monovalent-cation transporters. By promoting the proper targeting of at least three housekeeping ion transport systems, Na+, K+/H+ antiporter Nha1, K+ importer Trk1 and K+ channel Tok1, Erv14 appears to play a complex role in the maintenance of alkali-metal-cation homeostasis. Despite their connection to serious human diseases, the repertoire of identified cargoes of mammalian cornichons is much more limited. The majority of current information is about the structure and functioning of CNIH2 and CNIH3 as auxiliary subunits of AMPAR multi-protein complexes. Based on their unique properties and easy genetic manipulation, we propose yeast cells to be a useful tool for uncovering a broader spectrum of human cornichons´ cargoes.

• MeSH
• COP-vezikuly metabolismus   MeSH
• homeostáza fyziologie   MeSH
• iontový transport fyziologie   MeSH
• lidé MeSH
• membránové proteiny metabolismus   MeSH
• proteiny přenášející kationty metabolismus   MeSH
• Saccharomyces cerevisiae - proteiny metabolismus   genetika   MeSH
• Saccharomyces cerevisiae * metabolismus   MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH
• Názvy látek
• Erv14 protein, S cerevisiae MeSH Prohlížeč
• membránové proteiny MeSH
• proteiny přenášející kationty MeSH
• Saccharomyces cerevisiae - proteiny MeSH

The transport activity and substrate specificity of two chimeras consisting of S. cerevisiae Nha1p's N-terminal regions (either first 125 or 184 AA) and the rest of the C. glabrata Cnh1p (up to the total protein length of 946 AA) were compared with those of the two native antiporters. Both chimeric transporters were functional upon expression in S. cerevisiae cells, their presence improved the ability of cells to grow in the presence of high external concentration of K(+), Na(+) or Rb(+) (as chlorides), but not in the presence of the smallest cation (Li(+)). Cation efflux confirmed the ability of chimeras to export cations and showed their significantly reduced transport capacity compared to the wild-type proteins. Despite the very high level of primary sequence identity (87 %) between the S. cerevisiae and C. glabrata plasma-membrane Na(+)/H(+) antiporters, various parts of these proteins are not exchangeable without affecting the antiporter's transport capacity.

• MeSH
• Candida glabrata účinky léků   genetika   růst a vývoj   metabolismus   MeSH
• chlorid draselný farmakologie   MeSH
• chlorid sodný farmakologie   MeSH
• fungální proteiny chemie   genetika   metabolismus   MeSH
• molekulární sekvence - údaje MeSH
• Na(+)-H(+) antiport chemie   genetika   metabolismus   MeSH
• proteiny přenášející kationty chemie   genetika   metabolismus   MeSH
• rekombinantní fúzní proteiny chemie   genetika   metabolismus   MeSH
• Saccharomyces cerevisiae - proteiny chemie   genetika   metabolismus   MeSH
• Saccharomyces cerevisiae účinky léků   genetika   růst a vývoj   metabolismus   MeSH
• sekvence aminokyselin MeSH
• sekvenční analýza DNA MeSH
• sekvenční seřazení MeSH
• tolerance k soli * MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• chlorid draselný MeSH
• chlorid sodný MeSH
• CNH1 protein, Candida albicans MeSH Prohlížeč
• fungální proteiny MeSH
• Na(+)-H(+) antiport MeSH
• NHA1 protein, S cerevisiae MeSH Prohlížeč
• proteiny přenášející kationty MeSH
• rekombinantní fúzní proteiny MeSH
• Saccharomyces cerevisiae - proteiny MeSH

BACKGROUND: The virulence of Candida species depends on many environmental conditions. Extracellular pH and concentration of alkali metal cations belong among important factors. Nevertheless, the contribution of transporters mediating the exchange of alkali metal cations for protons across the plasma membrane to the cell salt tolerance and other physiological properties of various Candida species has not been studied so far. RESULTS: The tolerance/sensitivity of four pathogenic Candida species to alkali metal cations was tested and the role of one of the cation transporters in that tolerance (presumed to be the plasma-membrane Na+/H+ antiporter) was studied. The genes encoding these antiporters in the most and least salt sensitive species, C. dubliniensis and C. parapsilosis respectively, were identified, cloned and functionally expressed in the plasma membranes of Saccharomyces cerevisiae cells lacking their own cation exporters. Both CpCnh1 and CdCnh1 antiporters had broad substrate specificity and transported Na+, K+, Li+, and Rb+. Their activity in S. cerevisiae cells differed; CpCnh1p provided cells with a much higher salt tolerance than the CdCnh1 antiporter. The observed difference in activity was confirmed by direct measurements of sodium and potassium efflux mediated by these antiporters. CONCLUSION: We have cloned two genes encoding putative Na+/H+ antiporters in C. parapsilosis and C. dubliniensis, and characterized the transport properties of encoded proteins. Our results show that the activity of plasma-membrane Na+/H+ antiporters is one of the factors determining the tolerance of pathogenic Candida species to high external concentrations of alkali metal cations.

• MeSH
• alkalické kovy metabolismus   MeSH
• Candida genetika   růst a vývoj   metabolismus   patogenita   MeSH
• draslík metabolismus   MeSH
• fluorescenční mikroskopie MeSH
• fungální proteiny genetika   metabolismus   MeSH
• kationty metabolismus   MeSH
• lithium metabolismus   MeSH
• membránové proteiny genetika   metabolismus   MeSH
• molekulární sekvence - údaje MeSH
• Na(+)-H(+) antiport genetika   metabolismus   MeSH
• proteiny přenášející kationty genetika   metabolismus   MeSH
• Saccharomyces cerevisiae - proteiny genetika   metabolismus   MeSH
• Saccharomyces cerevisiae genetika   růst a vývoj   metabolismus   MeSH
• sekundární struktura proteinů MeSH
• sekvence nukleotidů MeSH
• soli metabolismus   MeSH
• substrátová specifita MeSH
• superoxiddismutasa 1 MeSH
• superoxiddismutasa metabolismus   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• srovnávací studie MeSH
• Názvy látek
• alkalické kovy MeSH
• CNH1 protein, Candida albicans MeSH Prohlížeč
• draslík MeSH
• fungální proteiny MeSH
• kationty MeSH
• lithium MeSH
• membránové proteiny MeSH
• Na(+)-H(+) antiport MeSH
• NHA1 protein, S cerevisiae MeSH Prohlížeč
• proteiny přenášející kationty MeSH
• Saccharomyces cerevisiae - proteiny MeSH
• soli MeSH
• superoxiddismutasa 1 MeSH
• superoxiddismutasa MeSH

Yarrowia lipolytica plasma-membrane Na+/H+ antiporter, encoded by the YlNHA2 gene, is a very efficient exporter of surplus sodium from the cytosol. Its heterologous expression in Saccharomyces cerevisiae wild-type laboratory strains increased their sodium tolerance more efficiently than the expression of ZrSod2-22 antiporter from the osmotolerant yeast Zygosaccharomvces rouxii.

• MeSH
• antifungální látky farmakologie   MeSH
• exprese genu MeSH
• fungální proteiny genetika   metabolismus   MeSH
• klonování DNA MeSH
• Na(+)-H(+) antiport genetika   metabolismus   MeSH
• rekombinantní proteiny genetika   metabolismus   MeSH
• Saccharomyces cerevisiae účinky léků   genetika   růst a vývoj   metabolismus   MeSH
• soli farmakologie   MeSH
• Yarrowia enzymologie   genetika   MeSH
• Zygosaccharomyces enzymologie   genetika   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• antifungální látky MeSH
• fungální proteiny MeSH
• Na(+)-H(+) antiport MeSH
• rekombinantní proteiny MeSH
• soli MeSH