[21] Activity of PP2Cβ is Increased by Divalent Cations and Lipophilic Compounds Depending on the Substrate

Methods in Enzymology

Volumn 366, Issue , 2003, Pages 282-289

  Krieglstein, Josef ^a   Selke, Dagmar ^b   Maaben, Alexander ^a   Klumpp, Susanne ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN; CATION; ISOENZYME; MAGNESIUM; MANGANESE; OKADAIC ACID; PHOSPHOPEPTIDE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN BAD; SERINE THREONINE PROTEIN PHOSPHATASE 2C; UNCLASSIFIED DRUG;

ARTICLE; DEPHOSPHORYLATION; DIMERIZATION; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; ENZYME SUBSTRATE; LIPOPHILICITY; PRIORITY JOURNAL;

EID: 0344234367     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(03)66021-0     Document Type: Review

References (17)

1. T. S. Ingebritsen and P. Cohen, Protein Phosphatases: Properties and Role in Cellular Regulation, Science 221, 331-338 (1983).
2. 2+-dependent enzyme, Methods Enzymol. 159, 416-426 (1988).
3. P. T. W. Cohen, Nomenclature and Chromosomal Localization of Human Protein Serine/Threonine Phosphatase, Adv. Prot. Phosphatases 8, 371-376 (1994).
4. G. Mieskes and H.-D. Söling, On the 6-phosphofructo-1-kinase phosphatase activity of protein phosphatase 2C and its dimeric nature, FEBS Lett. 181(1), 7-11 (1985).
5. 2+-dependent protein phosphatase α (Type 2Cα) by casein kinase II, Biochem. Biophys. Res. Commun. 195(1), 484-489 (1993).
6. M. Meinhard and E. Grill, Hydrogen peroxide is a regulator of ABIl, protein phosphatase 2C from Arabidopsis, FEBS Lett. 508, 443-446 (2001).
7. M. D. Pato and E. Kerc, Regulation of smooth muscle phosphatase-II by divalent cations, Mol. Cell. Biochem. 101, 31-41 (1991).
8. 2+-inhibitable Serine/Threonine Protein Phosphatase from Bovine Brain, J. Biol. Chem. 270(43), 25607-25612 (1995).
9. S. Klumpp et al., Protein phosphatase type-2C isozyme present in vertebrate retinae: purification, characterization, and localisation in photoreceptors, J. Neurosci. Res. 51, 328-338 (1998).
10. 2+: stimulation by unsaturated fatty acids, FEBS Lett. 437, 229-232 (1998).
11. S. Klumpp and D. Selke, Purification and Characterization of Protein Phosphatase Type 2C in Photoreceptors, Methods Enzymol. 315, 570-578 (2000).
12. S. Klumpp, D. Selke, and J. Kriegstein, Protein phosphatase type 2C dephosphorylates BAD, Neurochem. Inter. 42(7), 555-560 (2003).
13. E. B. Cogan, G. B. Birrel, and O. H. Griffith, A robotics-based automated assay for inorganic and organic phosphates, Anal. Biochem. 271(1), 29-35 (1999).
14. J. D. Mahuren et al., Microassay of phosphate provides a general method for measuring the activity of phosphatases using physiological, nonchromogenic substrates such as lysophosphatidic acid, Anal. Biochem. 298(2), 241-245 (2001).
15. C. C. Fjeld and J. M. Denu, Kinetic analysis of human serine/threonine protein phosphatase 2Calpha, J. Biol. Chem. 274(29), 20336-20343 (1999).
16. L. A. Pinna and A. Donella-Deana, Phosphorylated synthetic peptides as tools for studying protein phosphatases, Biochim. Biophys. Acta 1222, 415-431 (1994).
17. E. Baudouin, I. Meskiene, and H. Hirt, Unsaturated fatty acids inhibit MP2C, a protein phosphatase 2C involved in the wound-induced MAP kinase pathway regulation, Plant J. 20(3), 343-348 (1999).