Počet záznamů: 1
C5 conserved region of hydrophilic C-terminal part of Saccharomyces cerevisiae Nha1 antiporter determines its requirement of Erv14 COPII cargo receptor for plasma-membrane targeting
- 1.
SYSNO ASEP 0541555 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název C5 conserved region of hydrophilic C-terminal part of Saccharomyces cerevisiae Nha1 antiporter determines its requirement of Erv14 COPII cargo receptor for plasma-membrane targeting Tvůrce(i) Papoušková, Klára (FGU-C) RID, ORCID
Moravcová, Michaela (FGU-C)
Masrati, G. (IL)
Ben-Tal, N. (IL)
Sychrová, Hana (FGU-C) RID, ORCID
Zimmermannová, Olga (FGU-C) RID, ORCIDZdroj.dok. Molecular Microbiology - ISSN 0950-382X
Roč. 115, č. 1 (2021), s. 41-57Poč.str. 17 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova alkali-metal-cation homeostasis ; cargo receptor ; COPII ; Erv14 ; Nha1 ; yeast Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP GA17-01953S GA ČR - Grantová agentura ČR Způsob publikování Omezený přístup Institucionální podpora FGU-C - RVO:67985823 UT WOS 000571024900001 EID SCOPUS 85091179771 DOI 10.1111/mmi.14595 Anotace Erv14, a conserved cargo receptor of COPII vesicles, helps the proper trafficking of many but not all transporters to the yeast plasma membrane, for example, three out of five alkali-metal-cation transporters in Saccharomyces cerevisiae. Among them, the Nha1 cation/proton antiporter, which participates in cell cation and pH homeostasis, is a large membrane protein (985 aa) possessing a long hydrophilic C-terminus (552 aa) containing six conserved regions (C1-C6) with unknown function. A short Nha1 version, lacking almost the entire C-terminus, still binds to Erv14 but does not need it to be targeted to the plasma membrane. Comparing the localization and function of ScNha1 variants shortened at its C-terminus in cells with or without Erv14 reveals that only ScNha1 versions possessing the complete C5 region are dependent on Erv14. In addition, our broad evolutionary conservation analysis of fungal Na+/H+ antiporters identified new conserved regions in their C-termini, and our experiments newly show C5 and other, so far unknown, regions of the C-terminus, to be involved in the functionality and substrate specificity of ScNha1. Taken together, our results reveal that also relatively small hydrophilic parts of some yeast membrane proteins underlie their need to interact with the Erv14 cargo receptor. Pracoviště Fyziologický ústav Kontakt Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Rok sběru 2022 Elektronická adresa https://doi.org/10.1111/mmi.14595
Počet záznamů: 1