Novel in vitro and in vivo phosphorylation sites on protein phosphatase 1 inhibitor CPI-17

Biochemical and Biophysical Research Communications

Volumn 302, Issue 2, 2003, Pages 186-192

  Dubois, Thierry ^a,c   Howell, Steven ^b   Zemlickova, Eva ^a   Learmonth, Michele ^a   Cronshaw, Andy ^a   Aitken, Alastair ^a,c  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^c INSTITUT CURIE   (France)

Author keywords

CamKII; CKI; CPI 17; Phosphatase inhibitor; PKA; Protein phosphatase 1

Indexed keywords

CPI 17; CYCLIC AMP DEPENDENT PROTEIN KINASE; ENZYME; ENZYME INHIBITOR; ISOPROTEIN; LIMK 2 KINASE; PHI 1; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN KINASE (CALCIUM,CALMODULIN) II; RECOMBINANT ENZYME; SERINE; THREONINE; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; BRAIN; CONTROLLED STUDY; HUMAN; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; SEQUENCE HOMOLOGY;

EID: 0037428308     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00130-X     Document Type: Article

References (26)

1. Aggen J.B., Nairn A.C., Chamberlin R. Regulation of protein phosphatase-1. Chem. Biol. 7:2000;R13-R23.
2. Rubin E., Tamrakar S., Ludlow J.W. Protein phosphatase type 1, the product of the retinoblastoma susceptibility gene, and cell cycle control. Front. Biosci. 3:1998;D1209-D1219.
3. Somlyo A.P., Somlyo A.V. Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 522:2000;177-185.
4. Hubbard M.J., Cohen P. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci. 18:1993;172-177.
5. Oliver C.J., Shenolikar S. Physiologic importance of protein phosphatase inhibitors. Front. Biosci. 3:1998;D961-D972.
6. Kamm K.E., Stull J.T. Dedicated myosin light chain kinases with diverse cellular functions. J. Biol. Chem. 276:2001;4527-4530.
7. Eto M., Senba S., Morita F., Yazawa M. Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: its specific localization in smooth muscle. FEBS Lett. 410:1997;356-360.
8. Eto M., Karginov A., Brautigan D.L. A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes. Biochemistry. 38:1999;16952-16957.
9. Watanabe Y., Ito M., Kataoka Y., Wada H., Koyama M., Feng J., Shiku H., Nishikawa M. Protein kinase C-catalyzed phosphorylation of an inhibitory phosphoprotein of myosin phosphatase is involved in human platelet secretion. Blood. 97:2001;3798-3805.
10. Eto M., Ohmori T., Suzuki M., Furuya K., Morita F. A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J. Biochem. 118:1995;1104-1107.
11. Koyama M., Ito M., Feng J., Seko T., Shiraki K., Takase K., Hartshorne D.J., Nakano T. Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett. 475:2000;197-200.
12. Hamaguchi T., Ito M., Feng J., Seko T., Koyama M., Machida H., Takase K., Amano M., Kaibuchi K., Hartshorne D.J., Nakano T. Phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by protein kinase N. Biochem. Biophys. Res. Commun. 274:2000;825-830.
13. MacDonald J.A., Eto M., Borman M.A., Brautigan D.L., Haystead T.A. Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase. FEBS Lett. 493:2001;91-94.
14. Deng J.T., Sutherland C., Brautigan D.L., Eto M., Walsh M.P. Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase. Biochem. J. 367:2002;517-524.
15. Takizawa N., Koga Y., Ikebe M. Phosphorylation of CPI17 and myosin binding subunit of type 1 protein phosphatase by p21-activated kinase. Biochem. Biophys. Res. Commun. 297:2002;773-778.
16. Kitazawa T., Eto M., Woodsome T.P., Brautigan D.L. Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J. Biol. Chem. 275:2000;9897-9900.
17. Etter E.F., Eto M., Wardle R.L., Brautigan D.L., Murphy R.A. Activation of myosin light chain phosphatase in intact arterial smooth muscle during nitric oxide-induced relaxation. J. Biol. Chem. 276:2001;34681-34685.
18. Li L., Eto M., Lee M.R., Morita F., Yazawa M., Kitazawa T. Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle. J. Physiol. 508:1998;871-881.
19. 2+ sensitization in Triton X-100-demembranated rabbit arterial smooth muscle. J. Physiol. 520:1999;139-152.
20. Eto M., Kitazawa T., Yazawa M., Mukai H., Ono Y., Brautigan D.L. Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase Cα and δ isoforms. J. Biol. Chem. 276:2001;29072-29078.
21. Takizawa N., Niiro N., Ikebe M. Dephosphorylation of the two regulatory components of myosin phosphatase, MBS and CPI17. FEBS Lett. 515:2002;127-132.
22. Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A. 14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J. Biol. Chem. 272:1997;28882-28888.
23. Dubois T., Kerai P., Zemlickova E., Howell S., Jackson T.R., Venkateswarlu K., Cullen P.J., Theibert A.B., Larose L., Roach P.J., Aitken A. Casein kinase I associates with members of the centaurin-α family of phosphatidylinositol 3,4,5-trisphosphate-binding proteins. J. Biol. Chem. 276:2001;18757-18764.
24. Dubois T., Howell S., Zemlickova E., Aitken A. Identification of casein kinase Iα interacting protein partners. FEBS Lett. 517:2002;167-171.
25. Hayashi Y., Senba S., Yazawa M., Brautigan D.L., Eto M. Defining the structural determinants and a potential mechanism for inhibition of myosin phosphatase by the protein kinase C-potentiated inhibitor protein of 17. kDa J. Biol. Chem. 276:2001;39858-39863.
26. Ohki S.S., Eto M., Kariya E., Hayano T., Hayashi Y., Yazawa M., Brautigan D.L., Kainosho M. Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation. J. Mol. Biol. 314:2001;839-849.