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The mitogen-activated protein kinase Slt2 modulates arsenite transport through the aquaglyceroporin Fps1.

Journal article
Authors Doryaneh Ahmadpour
Ewa Maciaszczyk-Dziubinska
Roja Babazadeh
Sita Dahal
Magdalena Migocka
Mikael Andersson
Robert Wysocki
Markus J. Tamás
Stefan Hohmann
Published in FEBS letters
Volume 590
Issue 20
Pages 3649-3659
ISSN 1873-3468
Publication year 2016
Published at Department of Chemistry and Molecular Biology
Pages 3649-3659
Language en
Links dx.doi.org/10.1002/1873-3468.12390
Subject categories Cell Biology, Molecular biology, Cell and molecular biology, Biochemistry and Molecular Biology

Abstract

Arsenite is widely present in nature; therefore, cells have evolved mechanisms to prevent arsenite influx and promote efflux. In yeast (Saccharomyces cerevisiae), the aquaglyceroporin Fps1 mediates arsenite influx and efflux. The mitogen-activated protein kinase (MAPK) Hog1 has previously been shown to restrict arsenite influx through Fps1. In this study, we show that another MAPK, Slt2, is transiently phosphorylated in response to arsenite influx. Our findings indicate that the protein kinase activity of Slt2 is required for its role in arsenite tolerance. While Hog1 prevents arsenite influx via phosphorylation of T231 at the N-terminal domain of Fps1, Slt2 promotes arsenite efflux through phosphorylation of S537 at the C terminus. Our data suggest that Slt2 physically interacts with Fps1 and that this interaction depends on phosphorylation of S537. We hypothesize that Hog1 and Slt2 may affect each other's binding to Fps1, thereby controlling the opening and closing of the channel.

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