Yeast protein phosphatases Ptp2p and Msg5p are involved in G1–S transition, CLN2 transcription, and vacuole morphogenesis
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Abstract
We previously reported that double disruption of protein phosphatase (PPase) genes PTP2 (phosphotyrosine-specific PPase) and MSG5 (phosphotyrosine and phosphothreonine/serine-PPase) causes Ca2+ sensitive growth, whereas the single disruptions do not. This finding suggests that Ptp2p and Msg5p are involved in Ca2+-induced stress response in a redundant manner. To gain insight into the molecular mechanism causing calcium sensitivity of the ∆ptp2 ∆msg5 double disruptant, we performed fluorescence-activated cell sorting analysis and found a delayed G1 phase. This delayed G1 was consistent with the defect in bud emergence, and reduced CLN2 transcription upon addition of CaCl2. We also found that Slt2p is hyper-phosphorylated in the Δptp2 Δmsg5 double disruptant and that the vacuole of the Δptp2 Δmsg5 double disruptant is fragmented even in the absence of Ca2+. These findings suggest that both Ptp2p and Msg5p are involved in the G1 to S transition and vacuole morphogenesis possibly through their regulation of Slt2 pathway.
Keywords
Saccharomyces cerevisiae Protein phosphatase PTP2 MSG5 Calcium sensitivity Delayed G1Abbreviations
- PPase
Protein phosphatase
- MAPK
Mitogen-activated protein kinase
- Cas
Calcium sensitive
- CWI
Cell wall integrity
Notes
Acknowledgment
This work was supported by a Grant-in-Aid for Scientific Research B, 2007 to 2009, to S.H. from the Ministry of Education, Science, Sports and Culture of Japan.
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