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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

SYSNO ASEP	0541555
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	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
Author(s)	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, ORCID}
Source Title	Molecular Microbiology - ISSN 0950-382X Roč. 115, č. 1 (2021), s. 41-57
Number of pages	17 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	alkali-metal-cation homeostasis ; cargo receptor ; COPII ; Erv14 ; Nha1 ; yeast
Subject RIV	EE - Microbiology, Virology
OECD category	Microbiology
R&D Projects	GA17-01953S GA ČR - Czech Science Foundation (CSF)
Method of publishing	Limited access
Institutional support	FGU-C - RVO:67985823
UT WOS	000571024900001
EID SCOPUS	85091179771
DOI	10.1111/mmi.14595
Annotation	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.
Workplace	Institute of Physiology
Contact	Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
Year of Publishing	2022
Electronic address	https://doi.org/10.1111/mmi.14595

Number of the records: 1