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A role of deubiquitinating enzyme Ubp3 in coping with oxidative stress
Author(s) -
Jin Xin
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.916.1
Subject(s) - deubiquitinating enzyme , ubiquitin , microbiology and biotechnology , oxidative stress , mutant , mapk/erk pathway , phosphorylation , oxidative phosphorylation , intracellular , chemistry , biology , biochemistry , gene
Ubiquitination plays important roles in regulating numerous cellular processes. In response to extracellular and intracellular stimuli, deubiquitinating enzymes (DUBs) cooperate with E3 ubiquitin ligases to control the level and the type of ubiquitination on cellular substrates. Thus, DUBs are emerging as important regulators for cellular processes. Here, we show that Ubp3, a deubiquitinating enzyme in yeast, is required for cell survival under oxidative stress. The ubp3 deletion mutant exhibits increased sensitivity to the treatment of hydrogen peroxide. Notably, the mutant phenotype can be rescued by wild type Ubp3 but not a Ser695Ala mutant form of Ubp3, suggesting a potential role of phosphorylation of Ubp3 by MAPK in this process. Consistent with this model, we find that Mpk1 interacts with Ubp3 and disrupting Mpk1 but not any other MAPK in yeast similarly renders cells more sensitive to hydrogen peroxide treatment. Our results suggest phosphorylation and activation of Ubp3 by Mpk1 as a potential new mechanism for cells to cope with oxidative stress.