메뉴 건너뛰기




Volumn 6, Issue 2, 1999, Pages 174-181

Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROPHENYL PHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 0032910476     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/5861     Document Type: Article
Times cited : (149)

References (15)
  • 1
    • 0032044237 scopus 로고    scopus 로고
    • Protein phosphatase and the regulation of MAP kinase activity
    • Keyse, S.M. Protein phosphatase and the regulation of MAP kinase activity. Semin. Cell. Dev. Biol. 9, 143-152 (1998).
    • (1998) Semin. Cell. Dev. Biol. , vol.9 , pp. 143-152
    • Keyse, S.M.1
  • 2
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb, M & Goldsmith E.J. How MAP kinases are regulated J. Biol. Chem. 270, 14843-14846 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 14843-14846
    • Cobb, M.1    Goldsmith, E.J.2
  • 3
    • 0030296632 scopus 로고    scopus 로고
    • Structure and function of the protein tyrosine phosphatases
    • Fauman, E.B., & Saper, M.A. Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21, 413-417 (1996).
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 413-417
    • Fauman, E.B.1    Saper, M.A.2
  • 4
    • 0027423987 scopus 로고
    • Amino acid sequence similarity between CL100, a dual-specificity MAP kinase phosphatase and cdc25
    • Keyse, S.M. & Ginsburg, M. Amino acid sequence similarity between CL100, a dual-specificity MAP kinase phosphatase and cdc25. Trends Biochem. Sci. 18, 377-378 (1993).
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 377-378
    • Keyse, S.M.1    Ginsburg, M.2
  • 5
    • 18144432725 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the human cell cycle control phosphatase. CDC25A
    • Fauman, E.B. et al. Crystal structure of the catalytic domain of the human cell cycle control phosphatase. CDC25A. Cell. 93, 617-625 (1998).
    • (1998) Cell , vol.93 , pp. 617-625
    • Fauman, E.B.1
  • 6
    • 0026779540 scopus 로고
    • Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase
    • Keyse, S.M. & Emslie, E.A. Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase. Nature 359, 644-647 (1992).
    • (1992) Nature , vol.359 , pp. 644-647
    • Keyse, S.M.1    Emslie, E.A.2
  • 7
    • 0029935418 scopus 로고    scopus 로고
    • Regulation of transcription by MAP kinase cascades
    • Treisman, R. Regulation of transcription by MAP kinase cascades. Curr. Opin. Cell. Biol. 8, 205-215 (1996).
    • (1996) Curr. Opin. Cell. Biol. , vol.8 , pp. 205-215
    • Treisman, R.1
  • 8
    • 0029905354 scopus 로고    scopus 로고
    • Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase
    • Groom, L. A., Sneddon, A. A., Alessi, D. R., Dowd, S. & Keyse, S.M. Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase. EMBO J. 15, 3621-3632 (1996).
    • (1996) EMBO J. , vol.15 , pp. 3621-3632
    • Groom, L.A.1    Sneddon, A.A.2    Alessi, D.R.3    Dowd, S.4    Keyse, S.M.5
  • 9
    • 0032502671 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic domain is responsible for tight substrate binding and enzymatic specificity
    • Muda, M. et al. The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic domain is responsible for tight substrate binding and enzymatic specificity. J. Biol. Chem. 273, 9323-9329 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 9323-9329
    • Muda, M.1
  • 10
    • 0032557632 scopus 로고    scopus 로고
    • Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase
    • Camps, M. et al. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 280, 1262-1265 (1998).
    • (1998) Science , vol.280 , pp. 1262-1265
    • Camps, M.1
  • 11
    • 0029975476 scopus 로고    scopus 로고
    • Crystal structure of the dual-specificity protein phosphatase VHR
    • Yuvaniyama, J., Denu, J.M., Dixon, J.E. & Saper, M.A. Crystal structure of the dual-specificity protein phosphatase VHR. Science 272, 1328-1331 (1996).
    • (1996) Science , vol.272 , pp. 1328-1331
    • Yuvaniyama, J.1    Denu, J.M.2    Dixon, J.E.3    Saper, M.A.4
  • 12
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford, D., Flint, A.J. & Tonks, N.K. Crystal structure of human protein tyrosine phosphatase 1B. Science 263, 1397-1404 (1994).
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 13
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 ̊ and the complex with tungstate
    • Stuckey, J.A., Schubert, H.L., Fauman, E.B., Zhang, Z.Y., Dixon, J.E. & Saper, M.A. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 ̊ and the complex with tungstate. Nature 370, 571-575 (1994).
    • (1994) Nature , vol.370 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.Y.4    Dixon, J.E.5    Saper, M.A.6
  • 14
    • 0027201613 scopus 로고
    • Three-dimensional structure of rat acid phosphatase
    • Schneider, G., Lindqvist, Y. & Vihko, P. Three-dimensional structure of rat acid phosphatase. EMBO J. 12, 2609-2615 (1993).
    • (1993) EMBO J. , vol.12 , pp. 2609-2615
    • Schneider, G.1    Lindqvist, Y.2    Vihko, P.3
  • 15
    • 0030866897 scopus 로고    scopus 로고
    • Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    • Canagarajah, B.J., Khokhlatchev, A., Cobb, M.H. & Goldsmith, E.J. Activation mechanism of the MAP kinase ERK2 by dual phosphorylation. Cell 90, 859-869 (1997).
    • (1997) Cell , vol.90 , pp. 859-869
    • Canagarajah, B.J.1    Khokhlatchev, A.2    Cobb, M.H.3    Goldsmith, E.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.