The activity of Saccharomyces cerevisiae Na+, K+/H+ antiporter Nha1 is negatively regulated by 14-3-3 protein binding at serine 481

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00517811" target="_blank" >RIV/61388963:_____/19:00517811 - isvavai.cz</a>

Alternative codes found

RIV/67985823:_____/19:00517832 RIV/61388971:_____/19:00517832 RIV/00216208:11310/19:10403509

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0167488919301478?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0167488919301478?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbamcr.2019.118534" target="_blank" >10.1016/j.bbamcr.2019.118534</a>

Result language

angličtina

Original language name

The activity of Saccharomyces cerevisiae Na+, K+/H+ antiporter Nha1 is negatively regulated by 14-3-3 protein binding at serine 481

Original language description

Na+/H+ antiporters are involved in ensuring optimal intracellular concentrations of alkali-metal cations and protons in most organisms. In Saccharomyces cerevisiae, the plasma-membrane Na+, K+/H+ antiporter Nha1 mediates Na+ and K+ efflux, which is important for cell growth in the presence of salts. Nha1 belongs among housekeeping proteins and, due to its ability to export K+, it has many physiological functions. The Nha1 transport activity is regulated through its long, hydrophilic and unstructured C-terminus (554 of 985 aa). Although Nha1 has been previously shown to interact with the yeast 14-3-3 isoform (Bmh2), the binding site remains unknown. In this work, we identified the residues through which Nha1 interacts with the 14-3-3 protein. Biophysical characterization of the interaction between the C-terminal polypeptide of Nha1 and Bmh proteins in vitro revealed that the 14-3-3 protein binds to phosphorylated Ser481 of Nha1, and the crystal structure of the phosphopeptide containing Ser481 bound to Bmh1 provided the structural basis of this interaction. Our data indicate that 14-3-3 binding induces a disorder-to-order transition of the C-terminus of Nha1, and in vivo experiments showed that the mutation of Ser481 to Ala significantly increases cation efflux activity via Nha1, which renders cells sensitive to low K+ concentrations. Hence, 14-3-3 binding is apparently essential for the negative regulation of Nha1 activity, which should be low under standard growth conditions, when low amounts of toxic salts are present and yeast cells need to accumulate high amounts of K+.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochimica Et Biophysica Acta-Molecular Cell Research

ISSN

0167-4889

e-ISSN

—

Volume of the periodical

1866

Issue of the periodical within the volume

12

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

14

Pages from-to

118534

UT code for WoS article

000498748700016

EID of the result in the Scopus database

2-s2.0-85071569389