The mitogen-activated protein kinase Slt2 modulates arsenite transport through the aquaglyceroporin Fps1.
Journal article, 2016

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.

Author

Doryaneh Ahmadpour

University of Gothenburg

Ewa Maciaszczyk-Dziubinska

University of Wrocław

Roja Babazadeh

University of Gothenburg

Sita Dahal

University of Gothenburg

Magdalena Migocka

University of Wrocław

Mikael Andersson

University of Gothenburg

Robert Wysocki

University of Wrocław

Markus J. Tamás

University of Gothenburg

Stefan Hohmann

University of Gothenburg

FEBS letters

1873-3468 (eISSN)

Vol. 590 20 3649-3659

Subject Categories

Cell Biology

Biochemistry and Molecular Biology

DOI

10.1002/1873-3468.12390

PubMed

27607883

More information

Created

10/10/2017