期刊
MOLECULAR BIOLOGY OF THE CELL
卷 32, 期 8, 页码 703-711出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E20-08-0508
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- Swiss National Science Foundation [31003A_138177, 310030B_176396, CRSII3_160728]
- Swiss National Science Foundation (SNF) [31003A_138177, 310030B_176396, CRSII3_160728] Funding Source: Swiss National Science Foundation (SNF)
The phosphatase 2C Ptc1 is identified as a negative regulator of the kinase Pom1 in fission yeast cells, playing both direct and indirect roles in the cell size control pathway by influencing microtubule stability.
The fission yeast cells Schizosaccharomyces pombe divide at constant cell size regulated by environmental stimuli. An important pathway of cell size control involves the membrane-associated DYRK-family kinase Pom1, which forms decreasing concentration gradients from cell poles and inhibits mitotic inducers at midcell. Here, we identify the phosphatase 2C Ptc1 as negative regulator of Pom1. Ptc1 localizes to cell poles in a manner dependent on polarity and cell-wall integrity factors. We show that Ptc1 directly binds Pom1 and can dephosphorylate it in vitro but modulates Pom1 localization indirectly upon growth in low-glucose conditions by influencing microtubule stability. Thus, Ptc1 phosphatase plays both direct and indirect roles in the Pom1 cell size control pathway.
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