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Volumn 43, Issue 19, 2004, Pages 5698-5706

Semisynthesis of Phosphovariants of Smad2 Reveals a Substrate Preference of the Activated TβRI Kinase

Author keywords

[No Author keywords available]

Indexed keywords

DISEASES; ENZYME INHIBITION; ENZYMES; GENES; OLIGOMERS; SYNTHESIS (CHEMICAL);

EID: 2442457100     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0498407     Document Type: Article
Times cited : (31)

References (34)
  • 1
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué, J. (1998) TGF-β signal transduction, Annu. Rev. Biochem. 67, 753-91.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 2
    • 0242499448 scopus 로고    scopus 로고
    • Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer
    • Siegel, P. M., and Massagué, J. (2003) Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer, Nat. Rev. Cancer 3, 807-820.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 807-820
    • Siegel, P.M.1    Massagué, J.2
  • 3
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi, Y., and Massagué, J. (2003) Mechanisms of TGF-β signaling from cell membrane to the nucleus, Cell 113, 685-700.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massagué, J.2
  • 4
    • 0032481351 scopus 로고    scopus 로고
    • The L3 loop: A structural motif determining specific interactions between SMAD proteins and TGF-β receptors
    • Lo, R. S., Chen, Y.-G., Shi, Y., Pavletich, N. P., and Massagué, J. (1998) The L3 loop: a structural motif determining specific interactions between SMAD proteins and TGF-β receptors, EMBO J. 17, 996-1005.
    • (1998) EMBO J. , vol.17 , pp. 996-1005
    • Lo, R.S.1    Chen, Y.-G.2    Shi, Y.3    Pavletich, N.P.4    Massagué, J.5
  • 5
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity
    • Feng, X.-H., and Derynck, R. (1997) A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity, EMBO J. 16, 3912-3923.
    • (1997) EMBO J. , vol.16 , pp. 3912-3923
    • Feng, X.-H.1    Derynck, R.2
  • 7
    • 0034796457 scopus 로고    scopus 로고
    • The TGFβ receptor activation process: An inhibitor- to substrate-binding switch
    • Huse, M., Muir, T. W., Xu, L., Chen, Y.-G., Kuriyan, J., and Massagué, J. (2001) The TGFβ receptor activation process: an inhibitor- to substrate-binding switch, Mol. Cell 8, 671-682.
    • (2001) Mol. Cell , vol.8 , pp. 671-682
    • Huse, M.1    Muir, T.W.2    Xu, L.3    Chen, Y.-G.4    Kuriyan, J.5    Massagué, J.6
  • 8
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor
    • Tsukazaki, T., Chiang, T. A., Davison, A. F., Attisano, L., and Wrana, J. L. (1998) SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor, Cell 95, 779-791.
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5
  • 9
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-β signals
    • Massagué, J. (2000) How cells read TGF-β signals, Nat. Rev. Mol. Cell Bio. 1, 169-178.
    • (2000) Nat. Rev. Mol. Cell Bio. , vol.1 , pp. 169-178
    • Massagué, J.1
  • 10
    • 18244362844 scopus 로고    scopus 로고
    • Crystal structure of a phosphorylated Smad2: Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-β signaling
    • Wu, J.-W., Hu, M., Chai, J., Seoane, J., Huse, M., Li, C., Rigotti, D. J., Kyin, S., Muir, T. W., Fairman, R., Massagué, J., and Shi, Y. (2001) Crystal structure of a phosphorylated Smad2: recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-β signaling, Mol. Cell 8, 1277-1289.
    • (2001) Mol. Cell. , vol.8 , pp. 1277-1289
    • Wu, J.-W.1    Hu, M.2    Chai, J.3    Seoane, J.4    Huse, M.5    Li, C.6    Rigotti, D.J.7    Kyin, S.8    Muir, T.W.9    Fairman, R.10    Massagué, J.11    Shi, Y.12
  • 11
    • 0035695116 scopus 로고    scopus 로고
    • Structural basis of Smad1 activation by receptor kinase phosphorylation
    • Qin, B. Y., Chacko, B. M., Lam, S. S., de Caestecker, M. P., Correia, J. J., and Lin, K. (2001) Structural basis of Smad1 activation by receptor kinase phosphorylation, Mol. Cell 8, 1303-1312.
    • (2001) Mol. Cell , vol.8 , pp. 1303-1312
    • Qin, B.Y.1    Chacko, B.M.2    Lam, S.S.3    De Caestecker, M.P.4    Correia, J.J.5    Lin, K.6
  • 12
    • 0037185010 scopus 로고    scopus 로고
    • Stoichiometry of active Smad-transcription factor complexes on DNA
    • Inman, G. J., and Hill, C. S. (2002) Stoichiometry of active Smad-transcription factor complexes on DNA, J. Biol. Chem. 277, 51008-51016.
    • (2002) J. Biol. Chem. , vol.277 , pp. 51008-51016
    • Inman, G.J.1    Hill, C.S.2
  • 13
    • 0035814804 scopus 로고    scopus 로고
    • Sedimentation studies reveal a direct role of phosphorylation in Smad3:Smad4 homo- and hetero-trimerization
    • Correia, J. J., Chacko, B. M., Lam, S. S., and Lin, K. (2001) Sedimentation studies reveal a direct role of phosphorylation in Smad3:Smad4 homo- and hetero-trimerization, Biochemistry 40, 1473-1482.
    • (2001) Biochemistry , vol.40 , pp. 1473-1482
    • Correia, J.J.1    Chacko, B.M.2    Lam, S.S.3    Lin, K.4
  • 14
    • 0035827668 scopus 로고    scopus 로고
    • Formation of a stable heterodimer between Smad2 and Smad4
    • Wu, J.-W., Fairman, R., Penry, J., and Shi, Y. (2001) Formation of a stable heterodimer between Smad2 and Smad4, J. Biol. Chem. 276, 20688-20694.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20688-20694
    • Wu, J.-W.1    Fairman, R.2    Penry, J.3    Shi, Y.4
  • 15
    • 0034731334 scopus 로고    scopus 로고
    • Distinct oligomeric states of SMAD proteins in the transforming growth factor-β pathway
    • Jayaraman, L., and Massagué, J. (2000) Distinct oligomeric states of SMAD proteins in the transforming growth factor-β pathway, J. Biol. Chem. 275, 40710-40717.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40710-40717
    • Jayaraman, L.1    Massagué, J.2
  • 16
    • 0035123060 scopus 로고    scopus 로고
    • The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization
    • Chacko, B. M., Qin, B., Correia, J. J., Lam, S. S., de Caestecker, M. P., and Lin, K. (2001) The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization, Nat. Struct. Biol. 8, 248-253.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 248-253
    • Chacko, B.M.1    Qin, B.2    Correia, J.J.3    Lam, S.S.4    De Caestecker, M.P.5    Lin, K.6
  • 19
    • 0030698182 scopus 로고    scopus 로고
    • Coupling reagents and activation
    • Albericio, F., and Caprino, L. A. (1997) Coupling reagents and activation, Methods Enzymol. 289, 104-126.
    • (1997) Methods Enzymol. , vol.289 , pp. 104-126
    • Albericio, F.1    Caprino, L.A.2
  • 20
    • 0000277428 scopus 로고    scopus 로고
    • Occurrence and minimization of cysteine racemization during stepwise solid-phase peptide synthesis
    • Han, Y., Albericio, F., and Barany, G. (1997) Occurrence and minimization of cysteine racemization during stepwise solid-phase peptide synthesis, J. Org. Chem. 62, 4307-4312.
    • (1997) J. Org. Chem. , vol.62 , pp. 4307-4312
    • Han, Y.1    Albericio, F.2    Barany, G.3
  • 21
    • 0037140789 scopus 로고    scopus 로고
    • Solid-phase synthesis of lipidated peptides
    • Ludolph, B., Eisele, F., and Waldmann, H. (2002) Solid-phase synthesis of lipidated peptides, J. Am. Chem. Soc. 124, 5954-5955.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5954-5955
    • Ludolph, B.1    Eisele, F.2    Waldmann, H.3
  • 22
    • 0030711494 scopus 로고    scopus 로고
    • Cleavage and deprotection of resin-bound peptides following synthesis by Fmoc chemistry
    • Guy, C. A., and Fields, G. B. (1997) Cleavage and deprotection of resin-bound peptides following synthesis by Fmoc chemistry, Methods Enzymol. 289, 67-83.
    • (1997) Methods Enzymol. , vol.289 , pp. 67-83
    • Guy, C.A.1    Fields, G.B.2
  • 23
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12
    • Huse, M., Chen, Y.-G., Massagué, J., and Kuriyan, J. (1999) Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12, Cell 96, 425-436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.-G.2    Massagué, J.3    Kuriyan, J.4
  • 24
    • 0034734354 scopus 로고    scopus 로고
    • Semisynthesis of hyperphosphorylated type I TGFβ receptor: Addressing the mechanism of kinase activation
    • Huse, M., Holford, M. N., Kuriyan, J., and Muir, T. W. (2000) Semisynthesis of hyperphosphorylated type I TGFβ receptor: addressing the mechanism of kinase activation, J. Am. Chem. Soc. 122, 8337-8338.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8337-8338
    • Huse, M.1    Holford, M.N.2    Kuriyan, J.3    Muir, T.W.4
  • 25
    • 0037165313 scopus 로고    scopus 로고
    • Efficient semisynthesis of a tetraphosphorylated analogue of the type I TGFβ receptor
    • Flavell, R. R., Huse, M., Goger, M., Trester-Zedlitz, M., Kuriyan, J., and Muir, T. W. (2002) Efficient semisynthesis of a tetraphosphorylated analogue of the type I TGFβ receptor, Org. Lett. 4, 165-168.
    • (2002) Org. Lett. , vol.4 , pp. 165-168
    • Flavell, R.R.1    Huse, M.2    Goger, M.3    Trester-Zedlitz, M.4    Kuriyan, J.5    Muir, T.W.6
  • 26
    • 0002498995 scopus 로고
    • Computer-Aided Interpretation of Analytical Sedimentation Data for Proteins
    • (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.), Royal Society of Chemistry, Cambridge, U.K.
    • Laue, T., Shaw, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) Computer-Aided Interpretation of Analytical Sedimentation Data for Proteins, in Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.) pp 90-125, Royal Society of Chemistry, Cambridge, U.K.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.1    Shaw, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 28
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir, T. W. (2003) Semisynthesis of proteins by expressed protein ligation, Annu. Rev. Biochem. 72, 249-289.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 29
    • 0036682952 scopus 로고    scopus 로고
    • Smad3 allostery links TGF-β receptor kinase activation to transcriptional control
    • Qin, B. Y., Lam, S. S., Correia, J. J., and Lin, K. (2002) Smad3 allostery links TGF-β receptor kinase activation to transcriptional control, Genes Dev. 16, 1950-1963.
    • (2002) Genes Dev , vol.16 , pp. 1950-1963
    • Qin, B.Y.1    Lam, S.S.2    Correia, J.J.3    Lin, K.4
  • 30
    • 0030932129 scopus 로고    scopus 로고
    • Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine
    • Narayana, N., Cox, S., Shaltiel, S., Taylor, S. S., and Xuong, N.-h. (1997) Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine, Biochemistry 36, 4438-4448.
    • (1997) Biochemistry , vol.36 , pp. 4438-4448
    • Narayana, N.1    Cox, S.2    Shaltiel, S.3    Taylor, S.S.4    Xuong, N.-H.5
  • 31
    • 0002308879 scopus 로고
    • The eukaryotic protein kinase superfamily
    • (Hardie, G., and Hanks, S., Eds.), Academic Press Inc., San Diego, CA
    • Hanks, S. K., and Hunter, T. (1995) The eukaryotic protein kinase superfamily, in The Protein Kinase Fact Book: Protein-Serine Kinases (Hardie, G., and Hanks, S., Eds.) pp 7-47, Academic Press Inc., San Diego, CA.
    • (1995) The Protein Kinase Fact Book: Protein-Serine Kinases , pp. 7-47
    • Hanks, S.K.1    Hunter, T.2
  • 32
    • 0036714017 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor-β signaling by low molecular weight compounds interfering with ATP- or substrate-binding sites of the TGFβ type I receptor kinase
    • Yakymovych, I., Engström, U., Grimsby, S., Heldin, C.-H., and Souchelnytskyi, S. (2002) Inhibition of transforming growth factor-β signaling by low molecular weight compounds interfering with ATP- or substrate-binding sites of the TGFβ type I receptor kinase, Biochemistry 41, 11000-11007.
    • (2002) Biochemistry , vol.41 , pp. 11000-11007
    • Yakymovych, I.1    Engström, U.2    Grimsby, S.3    Heldin, C.-H.4    Souchelnytskyi, S.5
  • 34
    • 0029559786 scopus 로고
    • The specificity of the transforming growth factor β receptor kinases determined by a spatially addressable peptide library
    • Luo, K., Zhou, P., and Lodish, H. F. (1995) The specificity of the transforming growth factor β receptor kinases determined by a spatially addressable peptide library, Proc. Natl. Acad. Sci. U.S.A. 92, 11761-11765.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11761-11765
    • Luo, K.1    Zhou, P.2    Lodish, H.F.3


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