메뉴 건너뛰기




Volumn 429, Issue 6988, 2004, Pages 197-201

The GTPase-activating protein Rap1GAP uses a catalytic asparagine

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; ASSAYS; CATALYSIS; CELLS; CRYSTAL STRUCTURE; FLUORESCENCE; HYDROLYSIS;

EID: 2442669194     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02505     Document Type: Article
Times cited : (120)

References (30)
  • 2
    • 0142024483 scopus 로고    scopus 로고
    • Rap1 GTPase: Functions, regulation, and malignancy
    • Hattori, M. & Minato, N. Rap1 GTPase: functions, regulation, and malignancy. J. Biochem. (Tokyo) 134, 479-484 (2003).
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 479-484
    • Hattori, M.1    Minato, N.2
  • 3
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001).
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 4
    • 0037066723 scopus 로고    scopus 로고
    • Rap-specific GTPase activating protein follows an alternative mechanism
    • Brinkmann, T. et al. Rap-specific GTPase activating protein follows an alternative mechanism. J Biol. Chem. 277, 12525-12531 (2002).
    • (2002) J Biol. Chem. , vol.277 , pp. 12525-12531
    • Brinkmann, T.1
  • 5
    • 0025897167 scopus 로고
    • Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1
    • Rubinfeld, B. et al. Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1. Cell 65, 1033-1042 (1991).
    • (1991) Cell , vol.65 , pp. 1033-1042
    • Rubinfeld, B.1
  • 6
    • 0026667452 scopus 로고
    • Localisation of the rap 1GAP catalytic domain and sites of phosphorylation by mutational analysis
    • Rubinfeld, B. et al. Localisation of the rap1GAP catalytic domain and sites of phosphorylation by mutational analysis. Mol. Cell. Biol. 12, 4634-4642 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4634-4642
    • Rubinfeld, B.1
  • 7
    • 0028947758 scopus 로고
    • Molecular cloning of a novel mitogen-inducible nuclear protein with a Ran GTPase-activating domain that affects cell cycle progression
    • Hattori, M. et al. Molecular cloning of a novel mitogen-inducible nuclear protein with a Ran GTPase-activating domain that affects cell cycle progression. Mol. Cell. Biol. 15, 552-560 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 552-560
    • Hattori, M.1
  • 8
    • 0032952586 scopus 로고    scopus 로고
    • The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative GAP protein, E6TP1, and target it for degradation
    • Gao, Q., Srinivasan, S., Boyer, S. N., Wazer, D. E. & Band, V. The E6 oncoproteins of high-risk papillomaviruses bind to a novel putative GAP protein, E6TP1, and target it for degradation. Mol. Cell. Biol. 19, 733-744 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 733-744
    • Gao, Q.1    Srinivasan, S.2    Boyer, S.N.3    Wazer, D.E.4    Band, V.5
  • 9
    • 0347716759 scopus 로고    scopus 로고
    • Rheb fills a GAP between TSC and TOR
    • Manning, B. D. & Cantley, L. C. Rheb fills a GAP between TSC and TOR. Trends Biochem. Sci. 28, 573-576 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 573-576
    • Manning, B.D.1    Cantley, L.C.2
  • 10
    • 0035051806 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6-induced degradation of E6TP1 correlates with its ability to immortalise human mammary epithelial cells
    • Gao, Q. et al. Human papillomavirus type 16 E6-induced degradation of E6TP1 correlates with its ability to immortalise human mammary epithelial cells. J. Virol. 75, 4459-4466 (2001).
    • (2001) J. Virol. , vol.75 , pp. 4459-4466
    • Gao, Q.1
  • 11
    • 10744228326 scopus 로고    scopus 로고
    • Myeloproliferative stem cell disorders by deregulated Rap1 activation in SPA-1-deficient mice
    • Ishida, D. et al. Myeloproliferative stem cell disorders by deregulated Rap1 activation in SPA-1-deficient mice. Cancer Cell 4, 55-65 (2003).
    • (2003) Cancer Cell , vol.4 , pp. 55-65
    • Ishida, D.1
  • 12
    • 0036928818 scopus 로고    scopus 로고
    • Fluorescently labelled guanine nucleotide binding proteins to analyse elementary steps of GAP-catalysed reactions
    • Kraemer, A., Brinkmann, T., Plettner, I., Goody, R. & Wittinghofer, A. Fluorescently labelled guanine nucleotide binding proteins to analyse elementary steps of GAP-catalysed reactions. J. Mol. Biol. 324, 763-774 (2002).
    • (2002) J. Mol. Biol. , vol.324 , pp. 763-774
    • Kraemer, A.1    Brinkmann, T.2    Plettner, I.3    Goody, R.4    Wittinghofer, A.5
  • 13
    • 0025191377 scopus 로고
    • Aluminofluoride and beryllofluoride complexes: A new phosphate analogs in enzymology
    • Chabre, M. Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology. Trends Biochem. Sci. 15, 6-10 (1990).
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 6-10
    • Chabre, M.1
  • 14
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: Helping hands to complement an active site
    • Scheffzek, K., Ahmadian, M. R. & Wittinghofer, A. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23, 257-262 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 15
    • 0030828764 scopus 로고    scopus 로고
    • The GAP-related domain of tuberin, the product of the TSC2 gene, is a target for missense mutations in tuberous sclerosis
    • Maheshwar, M. M. et al. The GAP-related domain of tuberin, the product of the TSC2 gene, is a target for missense mutations in tuberous sclerosis. Hum. Mol. Genet. 6, 1991-1996 (1997).
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1991-1996
    • Maheshwar, M.M.1
  • 16
    • 0033365408 scopus 로고    scopus 로고
    • Comprehensive mutation analysis of TSC1 and TSC2 and phenotypic: Correlations in 150 families with tuberous sclerosis
    • Jones, A. C. et al. Comprehensive mutation analysis of TSC1 and TSC2 and phenotypic: correlations in 150 families with tuberous sclerosis. Am. J. Hum. Genet. 64, 1305-1315 (1999).
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1305-1315
    • Jones, A.C.1
  • 17
    • 0031888424 scopus 로고    scopus 로고
    • Germ-line mutational analysis of the TSC2 gene in 90 tuberous-sclerosis patients
    • Au, K. S. et al. Germ-line mutational analysis of the TSC2 gene in 90 tuberous-sclerosis patients. Am. J. Hum. Genet. 62, 286-294 (1998).
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 286-294
    • Au, K.S.1
  • 18
    • 7344222073 scopus 로고    scopus 로고
    • Selective disactivation of neurofibromin GAP activity in neurofibromatosis type 1
    • Klose, A. et al. Selective disactivation of neurofibromin GAP activity in neurofibromatosis type 1. Hum. Mol. Genet. 7, 1261-1268 (1998).
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1261-1268
    • Klose, A.1
  • 19
    • 0031037028 scopus 로고    scopus 로고
    • Guanine nucleotide binding properties of Rac 2 mutant proteins and analysis of the responsiveness to guanine nucleotide dissociation stimulator
    • Xu, X., Wang, Y., Barry, D. C., Chanock, S. J. & Bokoch, G. M. Guanine nucleotide binding properties of Rac2 mutant proteins and analysis of the responsiveness to guanine nucleotide dissociation stimulator. Biochemistry 36, 626-632 (1997).
    • (1997) Biochemistry , vol.36 , pp. 626-632
    • Xu, X.1    Wang, Y.2    Barry, D.C.3    Chanock, S.J.4    Bokoch, G.M.5
  • 20
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • Seewald, M. J., Körner, C., Wittinghofer, A. & Vetter, I. R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 415, 662-666 (2002).
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1    Körner, C.2    Wittinghofer, A.3    Vetter, I.R.4
  • 21
    • 0037175026 scopus 로고    scopus 로고
    • Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs
    • De Antoni, A., Schmitzova, J., Trepte, H. H., Gallwitz, D. & Albert, S. Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs. J. Biol. Chem. 277, 41023-41031 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 41023-41031
    • De Antoni, A.1    Schmitzova, J.2    Trepte, H.H.3    Gallwitz, D.4    Albert, S.5
  • 22
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian, M. R., Stege, P., Scheffzek, K. & Wittinghofer, A. Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nature Struct. Biol. 4, 686-689 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 23
    • 0033214775 scopus 로고    scopus 로고
    • Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases
    • Albert, S., Will, E. & Gallwitz, D. Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases. EMBO J. 18, 5216-5225 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5216-5225
    • Albert, S.1    Will, E.2    Gallwitz, D.3
  • 24
    • 0031762533 scopus 로고    scopus 로고
    • Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP
    • Nassar, N., Hoffman, G. R., Manor, D., Clardy, J. C. & Cerione, R. A. Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nature Struct. Biol. 5, 1047-1052 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1047-1052
    • Nassar, N.1    Hoffman, G.R.2    Manor, D.3    Clardy, J.C.4    Cerione, R.A.5
  • 25
    • 0033539492 scopus 로고    scopus 로고
    • Magnesium fluoride-dependent binding of small G proteins to their GTPase-activating proteins
    • Graham, D. L., Eccleston, J. F., Chung, C. W. & Lowe, P. N. Magnesium fluoride-dependent binding of small G proteins to their GTPase-activating proteins. Biochemistry 38, 14981-14987 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14981-14987
    • Graham, D.L.1    Eccleston, J.F.2    Chung, C.W.3    Lowe, P.N.4
  • 26
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg, J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96, 893-902 (1999).
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 27
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: Structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • Scheffzek, K. et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338 (1997).
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1
  • 28
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J. & Gamblin, S. J. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762 (1997).
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 29
    • 2442678744 scopus 로고    scopus 로고
    • Purification, crystallisation and preliminary structural characterisation of human Rap1GAP
    • Daumke, O., Wittinghofer, A. & Weyand, M. Purification, crystallisation and preliminary structural characterisation of human Rap1GAP. Acta Crystallogr. D 60, 752-754 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 752-754
    • Daumke, O.1    Wittinghofer, A.2    Weyand, M.3
  • 30
    • 0029112918 scopus 로고
    • Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements
    • Lenzen, C., Cool, R. H. & Wittinghofer, A. Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements. Methods Enzymol. 255, 95-109 (1995).
    • (1995) Methods Enzymol. , vol.255 , pp. 95-109
    • Lenzen, C.1    Cool, R.H.2    Wittinghofer, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.