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Title 

Phosphorylations of Sds23/Psp1/Moc1 by stress-activated kinase and cAMP-dependent kinase are essential for regulating cell viability in prolonged stationary phase

Authors 

Y J JangMi Sun WonHyang Sook Yoo

Publisher 

Wiley-Blackwell

Issue Date 

2013

Citation 

Yeast, vol. 30, no. 10, pp. 379-394

Keywords 

SchizosaccharomycesSds23/Psp1/Moc1Stationary phaseSty1

Abstract 

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.

ISSN 

0749-503X

Link 

http://dx.doi.org/10.1002/yea.2958

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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