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Phosphorylations of Sds23/Psp1/Moc1 by stress‐activated kinase and cAMP‐dependent kinase are essential for regulating cell viability in prolonged stationary phase
Author(s) -
Jang YoungJoo,
Won Misun,
Yoo HyangSook
Publication year - 2013
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.2958
Subject(s) - biology , microbiology and biotechnology , protein kinase a , kinase , stationary phase , schizosaccharomyces pombe , map kinase kinase kinase , mutant , biochemistry , gene , chemistry , chromatography
Under nutritional deprivation caused by prolonged culture, actively growing cells prepare to enter stationary phase. We showed here that Sds23/Psp1/Moc1 was phosphorylated by both cAMP‐dependent kinase and stress‐activated MAP kinase Sty1 upon entry into stationary phase. Overexpression of the phosphorylation‐defective mutant Sds23/Psp1/Moc1 induced cell death in prolonged culture and blocked re‐entry into the cell division cycle. These phosphorylations are likely to be required for cell survival during stationary phase and for binding of Ufd2, a Schizosaccharomyces pombe homologue of multi‐ubiquitin chain assembly factor E4. Deletion of the Ufd2 gene and overexpression of Sds23/Psp1/Moc1 increased cell viability in prolonged stationary phase. These results suggested that Ufd2 induces cell death in prolonged nutrient deprivation, that Sds23/Psp1/Moc1 may be a target protein of the ubiquitin‐fusion degradation pathway for regulation of cell viability under this stress condition, and that Sty1 and PKA activity in stationary phase is essential for interaction between Sds23/Psp1/Moc1 and Ufd2. Copyright © 2013 John Wiley & Sons, Ltd.