Open AccessCadmium‐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
Author(s) -
Jiang Linghuo,
Cao Chunlei,
Zhang Lilin,
Lin Wei,
Xia Jing,
Xu Huihui,
Zhang Yan
Publication year - 2014
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/1567-1364.12220
Subject(s) - biology , cadmium , kinase , microbiology and biotechnology , yeast , osmotic concentration , mutant , glycerol kinase , intracellular , cadmium chloride , biochemistry , gene , chemistry , organic chemistry
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 ( HOG 1 , SLT 2 , and KSS 1 ), 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.