Cadmium-induced activation of high osmolarity glycerol pathway through its Sln1 branch is dependent on the MAP kinase kinase kinase Ssk2, but not its paralog Ssk22, in budding yeast. Issue 8 (1st December 2014)

• Record Type: Journal Article
• Authors: Jiang, Linghuo; Cao, Chunlei; Zhang, Lilin; Lin, Wei; Xia, Jing; Xu, Huihui; Zhang, Yan
• Is Part Of: FEMS yeast research. Volume 14:Issue 8(2014)
• Page Start: 1263
• Page End: 1272
• Publication Date: 2014-12-01
• Subjects: Saccharomyces cerevisiae -- cadmium -- vacuolar protein sorting -- MAP kinase -- high osmolarity glycerol -- Ssk2; Yeast -- Periodicals; Yeasts -- Periodicals; 579.562
• DOI: 10.1111/1567-1364.12220
• Languages: English
• ISSNs: 1567-1356

Abstract

Abstract: Cadmium ions disrupt reactive oxygen species/Ca 2+ homeostasis and subsequently elicit cell death and adaptive signaling cascades in eukaryotic cells. Through a functional genomics approach, we have identified deletion mutants of 106 yeast genes, including three MAP kinase genes ( HOG1, SLT2, and KSS1 ), are sensitive to a sublethal concentration of cadmium, and 64 mutants show elevated intracellular cadmium concentrations upon exposure to cadmium. Hog1 is phosphorylated, reaching a peak 30 min after the cadmium treatment. Both Sln1 and Sho1 upstream branches are involved in the cadmium-induced activation of high osmolarity glycerol (HOG) pathway. Cadmium-induced HOG activation is dependent on the MAP kinase kinase kinase Ssk2, but not its paralog Ssk22, in the Sln1 branch. The environmental pollutant cadmium induces phosphorylation of the Hog1 MAP kinase through its two upstream Sln1 and Sho1 branches in budding yeast cells. The environmental pollutant cadmium induces phosphorylation of the Hog1 MAP kinase through its two upstream Sln1 and Sho1 branches in budding yeast cells.