Historical Background
Protein phosphatase 2C (PP2C) was first defined as magnesium (or manganese)-dependent Ser/Thr-specific dephosphorylation activity in mammalian tissue extract (Cohen 1989). This activity was also found to be resistant to okadaic acid, a potent inhibitor of Ser/Thr phosphatases. Because of its cation dependency, PP2C is sometimes referred as PPM (protein phosphatase, magnesium or manganese dependent). Genes encoding PP2C were subsequently isolated from yeast to humans, revealing a conserved protein phosphatase family with no apparent sequence similarity to the other Ser/Thr phosphatases such as PP1, PP2A, and PP2B. It is also notable that eukaryotic species have more genes encoding for PP2C than those for the other Ser/Thr phosphatase families. For example, the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombehave seven and six PP2C or...
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Barford D, Das AK, Egloff MP. The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct. 1998;27:133–64. https://doi.org/10.1146/annurev.biophys.27.1.133.
Brock AK, Willmann R, Kolb D, Grefen L, Lajunen HM, Bethke G, et al. The Arabidopsis mitogen-activated protein kinase phosphatase PP2C5 affects seed germination, stomatal aperture, and abscisic acid-inducible gene expression. Plant Physiol. 2010;153(3):1098–111. https://doi.org/10.1104/pp.110.156109.
Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem. 1989;58:453–508. https://doi.org/10.1146/annurev.bi.58.070189.002321.
Cutler SR, Rodriguez PL, Finkelstein RR, Abrams SR. Abscisic acid: emergence of a core signaling network. Annu Rev Plant Biol. 2010;61:651–79. https://doi.org/10.1146/annurev-arplant-042809-112122.
Fuchs S, Grill E, Meskiene I, Schweighofer A. Type 2C protein phosphatases in plants. FEBS J. 2013;280(2):681–93. https://doi.org/10.1111/j.1742-4658.2012.08670.x.
Goloudina AR, Kochetkova EY, Pospelova TV, Demidov ON. Wip1 phosphatase: between p53 and MAPK kinases pathways. Oncotarget. 2016;7(21):31563–71. https://doi.org/10.18632/oncotarget.7325.
Hecker M, Pané-Farré J, Völker U. SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria. Annu Rev Microbiol. 2007;61:215–36. https://doi.org/10.1146/annurev.micro.61.080706.093445.
Hilbert DW, Piggot PJ. Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol Mol Biol Rev. 2004;68(2):234–62. https://doi.org/10.1128/MMBR.68.2.234-262.2004.
Hohmann S. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol Mol Biol Rev. 2002;66(2):300. https://doi.org/10.1128/MMBR.66.2.300-372.2002.
Hubbard KE, Nishimura N, Hitomi K, Getzoff ED, Schroeder JI. Early abscisic acid signal transduction mechanisms: newly discovered components and newly emerging questions. Genes Dev. 2010;24(16):1695–708. https://doi.org/10.1101/gad.1953910.
Lammers T, Lavi S. Role of type 2C protein phosphatases in growth regulation and in cellular stress signaling. Crit Rev Biochem Mol Biol. 2007;42(6):437–61. https://doi.org/10.1080/10409230701693342.
Lu X, Nguyen TA, Moon SH, Darlington Y, Sommer M, Donehower LA. The type 2C phosphatase wip1: an oncogenic regulator of tumor suppressor and DNA damage response pathways. Cancer Metastasis Rev. 2008;27(2):123–35. https://doi.org/10.1007/s10555-008-9127-x.
Lu G, Wang Y. Functional diversity of mammalian type 2C protein phosphatase isoforms: new tales from an old family. Clin Exp Pharmacol Physiol. 2008;35(2):107–12. https://doi.org/10.1111/j.1440-1681.2007.04843.x.
Martín H, Flández M, Nombela C, Molina M. Protein phosphatases in MAPK signalling: we keep learning from yeast. Mol Microbiol. 2005;58(1):6–16. https://doi.org/10.1111/j.1365-2958.2005.04822.x.
Miyakawa T, Fujita Y, Yamaguchi-Shinozaki K, Tanokura M. Structure and function of abscisic acid receptors. Trends Plant Sci. 2013;18(5):259–66. https://doi.org/10.1016/j.tplants.2012.11.002.
Ng LM, Melcher K, Teh BT, Xu HE. Abscisic acid perception and signaling: structural mechanisms and applications. Acta Pharmacol Sin. 2014;35(5):567–84. https://doi.org/10.1038/aps.2014.5.
Schweighofer A, Kazanaviciute V, Scheikl E, Teige M, Doczi R, Hirt H, et al. The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in Arabidopsis. Plant Cell. 2007;19(7):2213–24. https://doi.org/10.1105/tpc.106.049585.
Shi Y. Serine/threonine phosphatases: mechanism through structure. Cell. 2009;139(3):468–84. https://doi.org/10.1016/j.cell.2009.10.006.
Xue T, Wang D, Zhang S, Ehlting J, Ni F, Jakab S, et al. Genome-wide and expression analysis of protein phosphatase 2C in rice and Arabidopsis. BMC Genomics. 2008;9:550. https://doi.org/10.1186/1471-2164-9-550.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this entry
Cite this entry
Tatebe, H., Shiozaki, K. (2018). PP2C. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_249
Download citation
DOI: https://doi.org/10.1007/978-3-319-67199-4_249
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-67198-7
Online ISBN: 978-3-319-67199-4
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences