The mitogen-activated protein kinase Slt2 modulates arsenite transport through the aquaglyceroporin Fps1.
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.
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
Doryaneh
D
Ahmadpour
Institute of Experimental Biology, University of Wroclaw, Poland.
Ewa
E
Maciaszczyk-Dziubinska
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
Roja
R
Babazadeh
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
Sita
S
Dahal
Institute of Experimental Biology, University of Wroclaw, Poland.
Magdalena
M
Migocka
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden.
Mikael
M
Andersson
Institute of Experimental Biology, University of Wroclaw, Poland.
Robert
R
Wysocki
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden. markus.tamas@cmb.gu.se.
Markus J
MJ
Tamás
Department of Chemistry and Molecular Biology, University of Gothenburg, Sweden. stefan.hohmann@chalmers.se.
Stefan
S
Hohmann
D018053:Arsenites / Q000378:metabolism*; D001665:Binding Sites; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D014443:Tyrosine / Q000378:metabolism
D018053:Arsenites; C093263:FPS1 protein, S cerevisiae; D008565:Membrane Proteins; D029701:Saccharomyces cerevisiae Proteins; D014443:Tyrosine; D012694:Serine; C088589:HOG1 protein, S cerevisiae; D020928:Mitogen-Activated Protein Kinases; C072724:SLT2 protein, S cerevisiae; C015001:arsenite
arsenite; mitogen-activated protein kinase; signal transduction; stress response; transmembrane transport