메뉴 건너뛰기




Volumn 429, Issue 6993, 2004, Pages 780-784

Structural basis of protein phosphatase 1 regulation

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ENZYMES; GENES; METABOLISM; MUSCLE;

EID: 3042547846     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02582     Document Type: Article
Times cited : (319)

References (30)
  • 1
    • 0035399464 scopus 로고    scopus 로고
    • Combinatorial control of protein phosphatase-1
    • Bollen M. Combinatorial control of protein phosphatase-1. Trends Biochem. Sci. 26, 426-431 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 426-431
    • Bollen, M.1
  • 2
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase-1-targeted in many directions
    • Cohen, P. T. Protein phosphatase-1-targeted in many directions. J. Cell Sci. 115, 241-256 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 241-256
    • Cohen, P.T.1
  • 3
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne, D. J., Ito, M. & Erdodi, F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19, 325-341 (1998).
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 4
    • 0030036564 scopus 로고    scopus 로고
    • Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targeting subunits
    • Johnson, D. F. et al. Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targeting subunits. Eur. J. Biochem. 239, 317-325 (1996).
    • (1996) Eur. J. Biochem. , vol.239 , pp. 317-325
    • Johnson, D.F.1
  • 5
    • 0031034680 scopus 로고    scopus 로고
    • Interactions of the subunits of smooth muscle myosin phosphatase
    • Hirano, K., Phan, B. C. & Hartshorne, D. J. Interactions of the subunits of smooth muscle myosin phosphatase. J. Biol. Chem. 272, 3683-3688 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 3683-3688
    • Hirano, K.1    Phan, B.C.2    Hartshorne, D.J.3
  • 6
    • 0032564320 scopus 로고    scopus 로고
    • Interaction of myosin phosphatase target subunit 1 with the catalytic subunit of type 1 protein phosphatase
    • Tanaka, J. et al. Interaction of myosin phosphatase target subunit 1 with the catalytic subunit of type 1 protein phosphatase. Biochemistry 37, 16697-16703 (1998).
    • (1998) Biochemistry , vol.37 , pp. 16697-16703
    • Tanaka, J.1
  • 7
    • 0000606386 scopus 로고    scopus 로고
    • Study of the subunit interactions in myosin phosphatase by surface plasmon resonance
    • Toth, A. et al. Study of the subunit interactions in myosin phosphatase by surface plasmon resonance. Eur. J. Biochem. 267, 1687-1697 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1687-1697
    • Toth, A.1
  • 8
    • 0030037103 scopus 로고    scopus 로고
    • Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle
    • Gailly, P. et al. Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle. Eur. J. Biochem. 239, 326-332 (1996).
    • (1996) Eur. J. Biochem. , vol.239 , pp. 326-332
    • Gailly, P.1
  • 9
    • 0037063362 scopus 로고    scopus 로고
    • Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1 M at Thr 850 induces its dissociation from myosin
    • Velasco, G., Armstrong, C., Morrice, N., Frame, S. & Cohen, P. Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1 M at Thr 850 induces its dissociation from myosin. FEBS Lett. 527, 101-104 (2002).
    • (2002) FEBS Lett. , vol.527 , pp. 101-104
    • Velasco, G.1    Armstrong, C.2    Morrice, N.3    Frame, S.4    Cohen, P.5
  • 10
    • 0029885778 scopus 로고    scopus 로고
    • Interactions and properties of smooth muscle myosin phosphatase
    • Ichikawa, K. et al. Interactions and properties of smooth muscle myosin phosphatase. Biochemistry 35, 6313-6320 (1996).
    • (1996) Biochemistry , vol.35 , pp. 6313-6320
    • Ichikawa, K.1
  • 11
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J. et al. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 745-753 (1995).
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1
  • 12
    • 0035941284 scopus 로고    scopus 로고
    • Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1
    • Maynes, J. T. et al. Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1. J. Biol. Chem. 276, 44078-44082 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44078-44082
    • Maynes, J.T.1
  • 13
    • 0036111253 scopus 로고    scopus 로고
    • Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1
    • Kita, A. et al. Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1. Structure 10, 715-724 (2002).
    • (2002) Structure , vol.10 , pp. 715-724
    • Kita, A.1
  • 14
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff, M. P., Cohen, P. T., Reinemer, P. & Barford, D. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. 254, 942-959 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.P.1    Cohen, P.T.2    Reinemer, P.3    Barford, D.4
  • 15
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff, M. P. et al. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16, 1876-1887 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1876-1887
    • Egloff, M.P.1
  • 16
    • 0033529415 scopus 로고    scopus 로고
    • Importance of the beta12-beta13 loop in protein phosphatase-1 catalytic subunit for inhibition by toxins and mammalian protein inhibitors
    • Connor, J. H., Kleeman, T., Barik, S., Honkanen, R. E. & Shenolikar, S. Importance of the beta12-beta13 loop in protein phosphatase-1 catalytic subunit for inhibition by toxins and mammalian protein inhibitors. J. Biol. Chem. 274, 22366-22372 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22366-22372
    • Connor, J.H.1    Kleeman, T.2    Barik, S.3    Honkanen, R.E.4    Shenolikar, S.5
  • 17
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: A diversity of interactions on a common structural framework
    • Sedgwick, S. G. & Smerdon, S. J. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24, 311-316 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 311-316
    • Sedgwick, S.G.1    Smerdon, S.J.2
  • 18
    • 0028848524 scopus 로고
    • Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex
    • Kissinger, C. R. et al. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 378, 641-644 (1995).
    • (1995) Nature , vol.378 , pp. 641-644
    • Kissinger, C.R.1
  • 19
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng, J. et al. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274, 37385-37390 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37385-37390
    • Feng, J.1
  • 20
    • 0029617851 scopus 로고
    • Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53
    • Helps, N. R., Barker, H. M., Elledge, S. J. & Cohen, P. T. Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53. FEBS Lett. 377, 295-300 (1995).
    • (1995) FEBS Lett. , vol.377 , pp. 295-300
    • Helps, N.R.1    Barker, H.M.2    Elledge, S.J.3    Cohen, P.T.4
  • 21
    • 0036170228 scopus 로고    scopus 로고
    • Inhibition of protein phosphatase-1 is linked to phosphorylation of p53 and apoptosis
    • Long, X., Wu, G., Gaa, S. T. & Rogers, T. B. Inhibition of protein phosphatase-1 is linked to phosphorylation of p53 and apoptosis. Apoptosis 7, 31-39 (2002).
    • (2002) Apoptosis , vol.7 , pp. 31-39
    • Long, X.1    Wu, G.2    Gaa, S.T.3    Rogers, T.B.4
  • 22
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p 53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina, S. & Pavletich, N. P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 274, 1001-1005 (1996).
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 23
    • 0033553546 scopus 로고    scopus 로고
    • Molecular determinants of nuclear protein phosphatase-1 regulation by NIPP-1
    • Beullens, M. et al. Molecular determinants of nuclear protein phosphatase-1 regulation by NIPP-1. J. Biol. Chem. 274, 14053-14061 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14053-14061
    • Beullens, M.1
  • 24
    • 0037008779 scopus 로고    scopus 로고
    • The neuronal actin-binding proteins, neurabin I and neurabin II, recruit specific isoforms of protein phosphatase-1 catalytic subunits
    • Terry-Lorenzo, R. T. et al. The neuronal actin-binding proteins, neurabin I and neurabin II, recruit specific isoforms of protein phosphatase-1 catalytic subunits. J. Biol. Chem. 277, 27716-27724 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 27716-27724
    • Terry-Lorenzo, R.T.1
  • 25
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • Barford, D., Das, A. K. & Egloff, M. P. The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu. Rev. Biophys. Biomol. Struct. 27, 133-164 (1998).
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 28
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.