Plant PP2C phosphatases: Emerging functions in stress signaling

Trends in Plant Science

Volumn 9, Issue 5, 2004, Pages 236-243

  Schweighofer, Alois ^a   Hirt, Heribert ^a   Meskiene, Irute ^a  

^a UNIVERSITY OF VIENNA   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C;

ANIMAL; ARABIDOPSIS; ENZYMOLOGY; GENETICS; HUMAN; METABOLISM; MULTIGENE FAMILY; PHYSIOLOGY; PLANT; PLANT PHYSIOLOGY; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; ARABIDOPSIS; ARABIDOPSIS PROTEINS; HUMANS; MULTIGENE FAMILY; PHOSPHOPROTEIN PHOSPHATASE; PLANT PHYSIOLOGY; PLANTS; SIGNAL TRANSDUCTION;

ANIMALIA; ARABIDOPSIS; EUKARYOTA; PROKARYOTA;

EID: 2442602365     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2004.03.007     Document Type: Review

References (63)

1. Bogre L., et al. Growth signalling pathways in Arabidopsis and the AGC protein kinases. Trends Plant Sci. 8:2003;424-431
2. Cohen P.T. Novel protein serine/threonine phosphatases: variety is the spice of life. Trends Biochem. Sci. 22:1997;245-251
3. Kerk D., et al. The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol. 129:2002;908-925
4. Zhou B., et al. The specificity of extracellular signal-regulated kinase 2 dephosphorylation by protein phosphatases. J. Biol. Chem. 277:2002;31818-31825
5. Meskiene I., et al. The stress-induced protein phosphatase 2C is a negative regulator of a mitogen-activated protein kinase. J. Biol. Chem. 278:2003;18945-18952
6. Bork P., et al. The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. Protein Sci. 5:1996;1421-1425
7. Ho D.T., et al. A docking site in MKK4 mediates high affinity binding to JNK MAPKs and competes with similar docking sites in JNK substrates. J. Biol. Chem. 278:2003;32662-32672
8. Kiegerl S., et al. SIMKK, a mitogen-activated protein kinase (MAPK) kinase, is a specific activator of the salt stress-induced MAPK, SIMK. Plant Cell. 12:2000;2247-2258
9. Biondi R.M., Nebreda A.R. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372:2003;1-13
10. Takeshima H., et al. Junctophilins: a novel family of junctional membrane complex proteins. Mol. Cell. 6:2000;11-22
11. Das A.K., et al. Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution. EMBO J. 15:1996;6798-6809
12. Cohen P. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58:1989;453-508
13. Leung-Hagesteijn C., et al. Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1. EMBO J. 20:2001;2160-2170
14. Tong Y., et al. Cloning and characterization of a novel mammalian PP2C isozyme. J. Biol. Chem. 273:1998;35282-35290
15. Field C.C., Denu J.M. Kinetic analysis of human serine/threonine protein phosphatase 2C α J. Biol. Chem. 274:1999;20336-20343
16. Leube M.P., et al. ABI1 of Arabidopsis is a protein serine/threonine phosphatase highly regulated by the proton and magnesium ion concentration. FEBS Lett. 424:1998;100-104
17. Baudouin E., et al. Short communication: unsaturated fatty acids inhibit MP2C, a protein phosphatase 2C involved in the wound-induced MAP kinase pathway regulation. Plant J. 20:1999;343-348
18. Takezawa D. Characterization of a novel plant PP2C-like protein Ser/Thr phosphatase as a calmodulin-binding protein. J. Biol. Chem. 278:2003;38076-38083
19. Meinhard M., et al. The sensitivity of ABI2 to hydrogen peroxide links the abscisic acid-response regulator to redox signalling. Planta. 214:2002;775-782
20. 2+: stimulation by unsaturated fatty acids. FEBS Lett. 437:1998;229-232
21. Bertauche N., et al. Protein phosphatase activity of abscisic acid insensitive 1 (ABI1) protein from Arabidopsis thaliana. Eur. J. Biochem. 241:1996;193-200
22. Cheng A.Y., et al. Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev. 13:1999;2946-2957
23. Cheng A., et al. Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C α and β 2 isoforms. J. Biol. Chem. 275:2000;34744-34749
24. De Smedt V., et al. Thr-161 phosphorylation of monomeric Cdc2. Regulation by protein phosphatase 2C in Xenopus oocytes. J. Biol. Chem. 277:2002;28592-28600
25. Ofek P., et al. Cell cycle regulation and p53 activation by protein phosphatase 2Cα J. Biol. Chem. 278:2003;14299-14305
26. Guthridge M.A., et al. FIN13, a novel growth factor-inducible serine-threonine phosphatase which can inhibit cell cycle progression. Mol. Cell. Biol. 17:1997;5485-5498
27. Menges M., et al. Cell cycle-regulated gene expression in Arabidopsis. J. Biol. Chem. 277:2002;41987-42002
28. Leroy C., et al. PP2C phosphatases Ptc2 and Ptc3 are required for DNA checkpoint inactivation after a double-strand break. Mol. Cell. 11:2003;827-835
29. Murray M.V., et al. The type 2C Ser/Thr phosphatase PP2C γ is a pre-mRNA splicing factor. Genes Dev. 13:1999;87-97
30. Warmka J., et al. Ptc1, a type 2C Ser/Thr phosphatase, inactivates the HOG pathway by dephosphorylating the mitogen-activated protein kinase Hog1. Mol. Cell. Biol. 21:2001;51-60
31. Nguyen A.N., Shiozaki K. Heat-shock-induced activation of stress MAP kinase is regulated by threonine- and tyrosine-specific phosphatases. Genes Dev. 13:1999;1653-1663
32. Takekawa M., et al. Protein phosphatase 2Cα inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J. 17:1998;4744-4752
33. Takekawa M., et al. p53-inducible Wip1 phosphatase mediates a negative feedback regulation of p38 MAPK-p53 signaling in response to UV radiation. EMBO J. 19:2000;6517-6526
34. Hanada M., et al. Regulation of the TAK1 signaling pathway by protein phosphatase 2C. J. Biol. Chem. 276:2001;5753-5759
35. Li M.G., et al. Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cε). J. Biol. Chem. 278:2003;12013-12021
36. Koh C.G., et al. The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Curr. Biol. 12:2002;317-321
37. Meskiene I., et al. MP2C, a plant protein phosphatase 2C, functions as a negative regulator of mitogen-activated protein kinase pathways in yeast and plants. Proc. Natl. Acad. Sci. U. S. A. 95:1998;1938-1943
38. Bogre L., et al. Wounding induces the rapid and transient activation of a specific MAP kinase pathway. Plant Cell. 9:1997;75-83
39. Rodriguez P.L. Protein phosphatase 2C (PP2C) function in higher plants. Plant Mol. Biol. 38:1998;919-927
40. Sheen J. Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants. Proc. Natl. Acad. Sci. U. S. A. 95:1998;975-980
41. Merlot S., et al. The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback regulatory loop of the abscisic acid signalling pathway. Plant J. 25:2001;295-303
42. Gosti F., et al. ABI1 protein phosphatase 2C is a negative regulator of abscisic acid signaling. Plant Cell. 11:1999;1897-1909
43. Wu Y., et al. The abi1-1 mutation blocks ABA signaling downstream of cADPR action. Plant J. 34:2003;307-315
44. Allen G.J., et al. Arabidopsis abi1-1 and abi2-1 phosphatase mutations reduce abscisic acid-induced cytoplasmic calcium rises in guard cells. Plant Cell. 11:1999;1785-1798
45. 2+ channels in guard cells requires cytosolic NAD(P)H and is differentially disrupted upstream and downstream of reactive oxygen species production in abi1-1 and abi2-1 protein phosphatase 2C mutants. Plant Cell. 13:2001;2513-2523
46. Guo Y., et al. A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis. Dev. Cell. 3:2002;233-244
47. Himmelbach A., et al. Homeodomain protein ATHB6 is a target of the protein phosphatase ABI1 and regulates hormone responses in Arabidopsis. EMBO J. 21:2002;3029-3038
48. Rodriguez P.L., et al. Molecular cloning in Arabidopsis thaliana of a new protein phosphatase 2C (PP2C) with homology to ABI1 and ABI2. Plant Mol. Biol. 38:1998;879-883
49. Kuromori T., Yamamoto M. Cloning of cDNAs from Arabidopsis thaliana that encode putative protein phosphatase 2C and a human Dr1-like protein by transformation of a fission yeast mutant. Nucleic Acids Res. 22:1994;5296-5301
50. Tahtiharju S., Palva T. Antisense inhibition of protein phosphatase 2C accelerates cold acclimation in Arabidopsis thaliana. Plant J. 26:2001;461-470
51. Vranova E., et al. The AKT3 potassium channel protein interacts with the AtPP2CA protein phosphatase 2C. J. Exp. Bot. 52:2001;181-182
52. + channel AKT2 and phosphatase AtPP2CA. Plant Cell. 14:2002;1133-1146
53. Zhu T., et al. Association of cystic fibrosis transmembrane conductance regulator and protein phosphatase 2C. J. Biol. Chem. 274:1999;29102-29107
54. Stone J.M., et al. Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science. 266:1994;793-795
55. Braun D.M., et al. Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: implications for transmembrane signaling in plants. Plant J. 12:1997;83-95
56. Trotochaud A.E., et al. The CLAVATA1 receptor-like kinase requires CLAVATA3 for its assembly into a signaling complex that includes KAPP and a Rho-related protein. Plant Cell. 11:1999;393-405
57. Torii K.U. Receptor kinase activation and signal transduction in plants: an emerging picture. Curr. Opin. Plant Biol. 3:2000;361-367
58. Stone J.M., et al. Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions. Plant Physiol. 117:1998;1217-1225
59. Li J., et al. Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain. Proc. Natl. Acad. Sci. U. S. A. 96:1999;7821-7826
60. Shah K., et al. The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1. Genes Dev. 16:2002;1707-1720
61. Yu L.P., et al. POLTERGEIST functions to regulate meristem development downstream of the CLAVATA loci. Development. 127:2000;1661-1670
62. Yu L.P., et al. POLTERGEIST encodes a protein phosphatase 2C that regulates CLAVATA pathways controlling stem cell identity at Arabidopsis shoot and flower meristems. Curr. Biol. 13:2003;179-188
63. Notredame C., et al. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302:2000;205-217