This chapter deals with protein serine/threonine-phosphatase 2C (PP2C). Eukaryotic organisms appear to have multiple PP2C genes; even the simplest eukaryotes, the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe, have seven and five PP2C genes in their genomes, respectively. In humans there are at least 16 PP2C genes, which express at least 22 isoforms by alternative splicing. PP2Cs and related protein phosphatases are implicated in numerous biological processes, often in stress signaling. This chapter reviews various signal transduction mechanisms where the molecular functions of PP2C enzymes have been relatively well elucidated. It also briefly touches upon PHLPP, PP2C-like phosphatases implicated in the regulation of protein kinase B (PKB). The functions of PP2C in both lower and higher eukaryotes include regulation of the stress-activated MAP kinase cascades, dephosphorylation of the cyclin-dependent kinase (Cdk), and regulation in DNA checkpoint through checkpoint kinases. Specifically in higher eukaryotes, the PP2C functions take into consideration PP2Cγ, a smad phosphatase in TGFβ signaling, Wip1 (PP2Cγ), an Oncogenic PP2C, calmodulin-dependent protein kinase phosphatase (CaMKP), abscisic acid signaling in Arabidopsis thaliana, and bacterial PP2Cs: key regulators of β factors. © 2010 Elsevier Inc. All rights reserved.
Tatebe, H., & Shiozaki, K. (2010). Protein serine/threonine-phosphatase 2C (PP2C). In Handbook of Cell Signaling, 2/e (Vol. 2, pp. 711–716). Elsevier Inc. https://doi.org/10.1016/B978-0-12-374145-5.00091-7