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Volumn 16, Issue 13, 1997, Pages 3866-3876

Mechanism of TGFβ receptor inhibition by FKBP12

Author keywords

FKBP12; Receptor signaling; Transforming growth factor

Indexed keywords

IMMUNOPHILIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; ACTIVIN RECEPTOR 1; CARRIER PROTEIN; DNA BINDING PROTEIN; ENZYME INHIBITOR; FK 506 BINDING PROTEIN; HEAT SHOCK PROTEIN; HYBRID PROTEIN; POLYENE; PROTEIN SERINE THREONINE KINASE; RAPAMYCIN; TGF BETA TYPE I RECEPTOR; TGF-BETA TYPE I RECEPTOR; TRANSFORMING GROWTH FACTOR BETA TYPE II RECEPTOR; TRANSFORMING GROWTH FACTOR-BETA TYPE II RECEPTOR;

EID: 0030926004     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.13.3866     Document Type: Article
Times cited : (305)

References (71)
  • 1
    • 0025035782 scopus 로고
    • Substrate specificity for the human rotamase FKBP: A view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics
    • Albers, M.W., Walsh, C.T. and Schreiber, S.L. (1990) Substrate specificity for the human rotamase FKBP: a view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics. J. Org. Chem., 55, 4984-4986.
    • (1990) J. Org. Chem. , vol.55 , pp. 4984-4986
    • Albers, M.W.1    Walsh, C.T.2    Schreiber, S.L.3
  • 2
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson, S., Davis, D.L., Dahlback, H., Jornvall, H. and Russell, D.W. (1989) Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem., 264, 8222-8229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4    Russell, D.W.5
  • 3
    • 0030060831 scopus 로고    scopus 로고
    • Activation of signalling by the activin receptor complex
    • Attisano, L., Wrana, J.L., Montalvo, E. and Massagué, J. (1996) Activation of signalling by the activin receptor complex. Mol. Cell. Biol., 16, 1066-1073.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1066-1073
    • Attisano, L.1    Wrana, J.L.2    Montalvo, E.3    Massagué, J.4
  • 4
    • 0029829230 scopus 로고    scopus 로고
    • A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway
    • Baker, J.C. and Harland, R.M. (1996) A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway. Genes Dev., 10, 1880-1889.
    • (1996) Genes Dev. , vol.10 , pp. 1880-1889
    • Baker, J.C.1    Harland, R.M.2
  • 5
    • 0024538265 scopus 로고
    • Transforming growth factor-β inhibition of epithelial cell proliferation linked to the expression of a 53-kDa membrane receptor
    • Boyd, F.T. and Massagué, J. (1989) Transforming growth factor-β inhibition of epithelial cell proliferation linked to the expression of a 53-kDa membrane receptor. J. Biol. Chem., 264, 2272-2278.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2272-2278
    • Boyd, F.T.1    Massagué, J.2
  • 9
    • 0028918776 scopus 로고
    • Immunophilin FK506 binding protein associated with inositol 1,4,5-trisphosphate receptor modulates calcium flux
    • Cameron, A.M., Steiner, J.P., Sabatini, D.M., Kaplin, A.I., Walensky, L.D. and Snyder, S.H. (1995) Immunophilin FK506 binding protein associated with inositol 1,4,5-trisphosphate receptor modulates calcium flux. Proc. Natl Acad. Sci. USA, 92, 1784-1788.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1784-1788
    • Cameron, A.M.1    Steiner, J.P.2    Sabatini, D.M.3    Kaplin, A.I.4    Walensky, L.D.5    Snyder, S.H.6
  • 10
    • 0028359376 scopus 로고
    • Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin
    • Cárcamo, J., Weis, F.M., Ventura, F., Wieser, R., Wrana, J.L., Attisano, L. and Massagué, J. (1994) Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin. Mol. Cell. Biol., 14, 3810-3821.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3810-3821
    • Cárcamo, J.1    Weis, F.M.2    Ventura, F.3    Wieser, R.4    Wrana, J.L.5    Attisano, L.6    Massagué, J.7
  • 11
    • 0029836237 scopus 로고    scopus 로고
    • FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor-β receptors
    • Charng, M.-J., Kinnunen, P., Hawker, J., Brand, T. and Schneider, M.D. (1996) FKBP-12 recognition is dispensable for signal generation by type I transforming growth factor-β receptors. J. Biol. Chem., 271, 22941-22944.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22941-22944
    • Charng, M.-J.1    Kinnunen, P.2    Hawker, J.3    Brand, T.4    Schneider, M.D.5
  • 12
    • 0028937160 scopus 로고
    • Biochemical evidence for the autophosphorylation and transphosphoryiation of transforming growth factor beta receptor kinases
    • Chen, F. and Weinberg, R.A. (1995) Biochemical evidence for the autophosphorylation and transphosphoryiation of transforming growth factor beta receptor kinases. Proc. Natl Acad. Sci. USA, 92, 1565-1569.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1565-1569
    • Chen, F.1    Weinberg, R.A.2
  • 13
    • 0029010192 scopus 로고
    • Phosphorylation-dependent interaction of the cytoplasmic domains of the type I and type II transforming growth factor-beta receptors
    • Chen, R.H., Moses, H.L., Maruoka, E.M., Derynck, R. and Kawabata, M. (1995) Phosphorylation-dependent interaction of the cytoplasmic domains of the type I and type II transforming growth factor-beta receptors. J. Biol. Chem., 270, 12235-12241.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12235-12241
    • Chen, R.H.1    Moses, H.L.2    Maruoka, E.M.3    Derynck, R.4    Kawabata, M.5
  • 14
    • 0029802485 scopus 로고    scopus 로고
    • A transcriptional partner for MAD proteins in TGF-β signalling
    • Chen, X., Rubock, M.J. and Whitman, M. (1996) A transcriptional partner for MAD proteins in TGF-β signalling. Nature, 383, 691-696.
    • (1996) Nature , vol.383 , pp. 691-696
    • Chen, X.1    Rubock, M.J.2    Whitman, M.3
  • 15
    • 16044369574 scopus 로고    scopus 로고
    • MADR2 maps to 18q21 and encodes a TGFβ-regulated MAD-related protein that is functionally mutated in colorectal carcinoma
    • Eppert, K. et al. (1996) MADR2 maps to 18q21 and encodes a TGFβ-regulated MAD-related protein that is functionally mutated in colorectal carcinoma. Cell, 86, 543-552.
    • (1996) Cell , vol.86 , pp. 543-552
    • Eppert, K.1
  • 16
    • 17544376741 scopus 로고    scopus 로고
    • Ligand-independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors
    • Feng, X.H. and Derynck, R. (1996) Ligand-independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors. J. Biol. Chem., 271, 13123-13129.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13123-13129
    • Feng, X.H.1    Derynck, R.2
  • 17
    • 0028972072 scopus 로고
    • Transforming growth factor-beta (TGF-beta)-induced down-regulation of cyclin A expression requires a functional TGF-beta receptor complex. Characterization of chimeric and truncated type I and type II receptors
    • Feng, X.H., Filvaroff, E.H. and Derynck, R. (1995) Transforming growth factor-beta (TGF-beta)-induced down-regulation of cyclin A expression requires a functional TGF-beta receptor complex. Characterization of chimeric and truncated type I and type II receptors. J. Biol. Chem., 270, 24237-24245.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24237-24245
    • Feng, X.H.1    Filvaroff, E.H.2    Derynck, R.3
  • 18
    • 0028985296 scopus 로고
    • The GS domain of the transforming growth factor-beta type I receptor is important in signal transduction
    • Franzén, P., Heldin, C.H. and Miyazono, K. (1995) The GS domain of the transforming growth factor-beta type I receptor is important in signal transduction. Biochem. Biophys. Res. Commun., 207, 682-689.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 682-689
    • Franzén, P.1    Heldin, C.H.2    Miyazono, K.3
  • 19
    • 0029079643 scopus 로고
    • FK506 binding protein mutational analysis. Defining the surface residue contributions to stability of the calcineurin co-complex
    • Futer, O., DeCenzo, M.T., Aldape, R.A. and Livingston, D.J. (1995) FK506 binding protein mutational analysis. Defining the surface residue contributions to stability of the calcineurin co-complex. J. Biol. Chem., 270, 18935-18940.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18935-18940
    • Futer, O.1    Decenzo, M.T.2    Aldape, R.A.3    Livingston, D.J.4
  • 20
    • 0029940972 scopus 로고    scopus 로고
    • Xenopus Mad proteins transduce distinct subsets of signals for the TGFβ superfamily
    • Graff, J.M., Bansal, A. and Metton, D.A. (1996) Xenopus Mad proteins transduce distinct subsets of signals for the TGFβ superfamily. Cell, 85, 479-487.
    • (1996) Cell , vol.85 , pp. 479-487
    • Graff, J.M.1    Bansal, A.2    Metton, D.A.3
  • 21
    • 0025166072 scopus 로고
    • Graded changes in dose of a Xenopus activin A homologue elicit stepwise transitions in embryonic cell fate
    • Green, J.B.A. and Smith, J.C. (1990) Graded changes in dose of a Xenopus activin A homologue elicit stepwise transitions in embryonic cell fate. Nature, 347, 391-394.
    • (1990) Nature , vol.347 , pp. 391-394
    • Green, J.B.A.1    Smith, J.C.2
  • 22
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding, M.W., Galat, A., Uehling, D.E. and Schreiber, S.L. (1989) A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature, 341, 758-760.
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 23
    • 0025373627 scopus 로고
    • Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: Evidence for the existence of a family of distinct enzymes
    • Harrison, R.K. and Stein, R.L. (1990) Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry, 29, 3813-3816.
    • (1990) Biochemistry , vol.29 , pp. 3813-3816
    • Harrison, R.K.1    Stein, R.L.2
  • 24
    • 0028270311 scopus 로고
    • Follistatin, an antagonist of activin, is expressed in the Spemann Organizer and displays direct neuralizing activity
    • Hemmati-Brivanlou, A., Kelly, O.G. and Melton, D.A. (1994) Follistatin, an antagonist of activin, is expressed in the Spemann Organizer and displays direct neuralizing activity. Cell, 77, 283-295.
    • (1994) Cell , vol.77 , pp. 283-295
    • Hemmati-Brivanlou, A.1    Kelly, O.G.2    Melton, D.A.3
  • 25
    • 0030598871 scopus 로고    scopus 로고
    • The Xenopus dorsalizing factor noggin ventralizes Drosophila embryos by preventing DPP from activating its receptor
    • Holly, S.A., Neul, J.L., Attisano, L., Wrana, J.L., Sasai, Y., O'Connor, M.B., De Robertis, E.M. and Ferguson, E.L. (1996) The Xenopus dorsalizing factor noggin ventralizes Drosophila embryos by preventing DPP from activating its receptor. Cell, 86, 607-617.
    • (1996) Cell , vol.86 , pp. 607-617
    • Holly, S.A.1    Neul, J.L.2    Attisano, L.3    Wrana, J.L.4    Sasai, Y.5    O'Connor, M.B.6    De Robertis, E.M.7    Ferguson, E.L.8
  • 29
    • 0028931238 scopus 로고
    • Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor
    • Kawabata, M., Chytil, A. and Moses, H.L. (1995a) Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor. J. Biol. Chem., 270, 5625-5630.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5625-5630
    • Kawabata, M.1    Chytil, A.2    Moses, H.L.3
  • 30
    • 0029610361 scopus 로고
    • Interaction of the transforming growth facotr-β type I receptor with farnesyl-protein transferase
    • Kawabata, M., Imamura, T., Miyazono, K., Engel, M.E. and Moses, H.L. (1995b) Interaction of the transforming growth facotr-β type I receptor with farnesyl-protein transferase. J. Biol. Chem., 270, 29628-29631.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29628-29631
    • Kawabata, M.1    Imamura, T.2    Miyazono, K.3    Engel, M.E.4    Moses, H.L.5
  • 31
    • 0030911104 scopus 로고    scopus 로고
    • The TGF-β family mediator Smadl is directly phosphorylated and functionally activated by the BMP receptor kinase
    • Kretzschmar, M., Liu, F., Hata, A., Doody, J. and Massagué, J. (1997) The TGF-β family mediator Smadl is directly phosphorylated and functionally activated by the BMP receptor kinase. Genes Dev., 11, 984-995.
    • (1997) Genes Dev. , vol.11 , pp. 984-995
    • Kretzschmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massagué, J.5
  • 32
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • Lagna, G., Hata, A., Hemmati-Brivanlou, A. and Massagué, J. (1996) Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. Nature, 383, 832-836.
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    Hemmati-Brivanlou, A.3    Massagué, J.4
  • 33
    • 0025129867 scopus 로고
    • Concomitant loss of transforming growth factor (TGF)-β receptor type I and II in TGF-β-resistant cell mutants implicates both receptor types in signal transduction
    • Laiho, M., Weis, F.M.B. and Massagué, J. (1990) Concomitant loss of transforming growth factor (TGF)-β receptor type I and II in TGF-β-resistant cell mutants implicates both receptor types in signal transduction. J. Biol. Chew., 265, 18518-18524.
    • (1990) J. Biol. Chew. , vol.265 , pp. 18518-18524
    • Laiho, M.1    Weis, F.M.B.2    Massagué, J.3
  • 34
    • 0026537831 scopus 로고
    • Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase
    • Lin, H.Y., Wang, X.F., Ng-Eaton, E., Weinberg, R.A. and Lodish, H.F. (1992) Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase. Cell, 68, 775-785.
    • (1992) Cell , vol.68 , pp. 775-785
    • Lin, H.Y.1    Wang, X.F.2    Ng-Eaton, E.3    Weinberg, R.A.4    Lodish, H.F.5
  • 35
    • 0029008597 scopus 로고
    • Human type II receptor for bone morphogenic proteins (BMPs): Extension of the two-kinase receptor model to the BMPs
    • Liu, F., Ventura, F., Doody, J. and Massagué, J. (1995) Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. Mol. Cell. Biol., 15, 3479-3486.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3479-3486
    • Liu, F.1    Ventura, F.2    Doody, J.3    Massagué, J.4
  • 37
    • 0027276765 scopus 로고
    • Betaglycan presents ligand to the TGF beta signaling receptor
    • López-Casillas, F., Wrana, J.L. and Massagué, J. (1993) Betaglycan presents ligand to the TGF beta signaling receptor. Cell, 73, 1435-1444.
    • (1993) Cell , vol.73 , pp. 1435-1444
    • López-Casillas, F.1    Wrana, J.L.2    Massagué, J.3
  • 38
    • 0029792338 scopus 로고    scopus 로고
    • Signaling by chimeric erythropoietin-TGF-β receptors: Homodimerization of the cytoplasmic domain of the type I TGFβ receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction
    • Luo, K. and Lodish, H.F. (1996) Signaling by chimeric erythropoietin-TGF-β receptors: homodimerization of the cytoplasmic domain of the type I TGFβ receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction. EMBO J., 15, 4485-4496.
    • (1996) EMBO J. , vol.15 , pp. 4485-4496
    • Luo, K.1    Lodish, H.F.2
  • 39
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling
    • Macias-Silva, M., Abdollah, S., Hoodless, P.A., Pirone, R., Attisano, L. and Wrana, J.L. (1996) MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell, 87, 1215-1224.
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macias-Silva, M.1    Abdollah, S.2    Hoodless, P.A.3    Pirone, R.4    Attisano, L.5    Wrana, J.L.6
  • 40
    • 0023575875 scopus 로고
    • Identification of receptors of type β transforming growth factor
    • Massagué, J. (1987) Identification of receptors of type β transforming growth factor. Methods Enzymol., 146, 174-195.
    • (1987) Methods Enzymol. , vol.146 , pp. 174-195
    • Massagué, J.1
  • 41
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massagué, J. (1990) The transforming growth factor-β family. Annu. Rev. Cell Biol. 6, 597-641.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massagué, J.1
  • 42
    • 0030604542 scopus 로고    scopus 로고
    • TGFβ signaling: Receptors, transducers, and Mad proteins
    • Massagué, J. (1996) TGFβ signaling: receptors, transducers, and Mad proteins. Cell, 85, 947-950.
    • (1996) Cell , vol.85 , pp. 947-950
    • Massagué, J.1
  • 43
    • 0027339327 scopus 로고
    • NF-ATp, a T lymphocyte DNA-binding protein that is a target for calcineurin and immunosuppressive drugs
    • McCaffrey, P.G., Perrino, B.A., Soderling, T.R. and Rao, A. (1993) NF-ATp, a T lymphocyte DNA-binding protein that is a target for calcineurin and immunosuppressive drugs. J. Biol. Chem., 268, 3747-3752.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3747-3752
    • McCaffrey, P.G.1    Perrino, B.A.2    Soderling, T.R.3    Rao, A.4
  • 44
    • 0027490673 scopus 로고
    • The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
    • Moustakas, A., Lin, H.Y., Henis, Y.I., Plamondon, J., O'Connor-McCourt, M.D. and Lodish, H.F. (1993) The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand. J. Biol. Chem., 268, 22215-22218.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22215-22218
    • Moustakas, A.1    Lin, H.Y.2    Henis, Y.I.3    Plamondon, J.4    O'Connor-McCourt, M.D.5    Lodish, H.F.6
  • 45
  • 46
    • 0029786480 scopus 로고    scopus 로고
    • Characterization of the interaction of FKBP12 with the transforming growth factor-β type I receptor in vivo
    • Okadome, T., Oeda, E., Saitoh, M., Ichijo, H., Moses, H.L., Miyazono, K. and Kawabata, M. (1996) Characterization of the interaction of FKBP12 with the transforming growth factor-β type I receptor in vivo. J. Biol. Chem., 271, 21687-21690.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21687-21690
    • Okadome, T.1    Oeda, E.2    Saitoh, M.3    Ichijo, H.4    Moses, H.L.5    Miyazono, K.6    Kawabata, M.7
  • 47
    • 0030598867 scopus 로고    scopus 로고
    • Dorsoventral patterning in Xenopus: Inhibition of ventral signals by direct binding of chordin to BMP-4
    • Piccolo, S., Sasai, Y., Lu, B. and De Robertis, E.M. (1996) Dorsoventral patterning in Xenopus: inhibition of ventral signals by direct binding of chordin to BMP-4. Cell, 86, 589-598.
    • (1996) Cell , vol.86 , pp. 589-598
    • Piccolo, S.1    Sasai, Y.2    Lu, B.3    De Robertis, E.M.4
  • 48
    • 0000116653 scopus 로고
    • The transforming growth factor-betas
    • Sporn, M.B. and Roberts, A.B. (eds). Springer-Verlag, Heidelberg
    • Roberts, A.B. and Sporn, M.B. (1990) The transforming growth factor-betas. In Sporn, M.B. and Roberts, A.B. (eds), Peptitle Growth Factors and Their Receptors. Springer-Verlag, Heidelberg, pp. 419-472.
    • (1990) Peptitle Growth Factors and Their Receptors , pp. 419-472
    • Roberts, A.B.1    Sporn, M.B.2
  • 49
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • Sabatini, D.M., Erdjument-Bromage, H., Lui, M., Tempst, P. and Snyder, S.H. (1994) RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. Cell. 78, 35-43.
    • (1994) Cell. , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 50
    • 0030058914 scopus 로고    scopus 로고
    • Caenorhabditis elegans genes sma-2, sma-3, and sma-4 define a conserved family of transforming growth factor beta pathway components
    • Savage, C., Das, P., Finelli, A.L., Townsend, S.R., Sun, C.Y., Baird, S.E. and Padgett, R.W. (1996) Caenorhabditis elegans genes sma-2, sma-3, and sma-4 define a conserved family of transforming growth factor beta pathway components. Proc. Natl Acad. Sci. USA, 93, 790-794.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 790-794
    • Savage, C.1    Das, P.2    Finelli, A.L.3    Townsend, S.R.4    Sun, C.Y.5    Baird, S.E.6    Padgett, R.W.7
  • 51
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber, S.L. (1991) Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science, 251, 283-287.
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 52
    • 0026625939 scopus 로고
    • Immunophilin-sensitive protein phosphatase action in cell signaling pathways
    • Schreiber, S.L. (1992) Immunophilin-sensitive protein phosphatase action in cell signaling pathways. Cell, 70, 365-368.
    • (1992) Cell , vol.70 , pp. 365-368
    • Schreiber, S.L.1
  • 53
    • 0028940853 scopus 로고
    • Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster
    • Sekelsky, J.J., Newfeld, S.J., Raftery, L.A., Chartoff, E.H. and Gelbart, W.M. (1995) Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster. Genetics, 139, 1347-1358.
    • (1995) Genetics , vol.139 , pp. 1347-1358
    • Sekelsky, J.J.1    Newfeld, S.J.2    Raftery, L.A.3    Chartoff, E.H.4    Gelbart, W.M.5
  • 54
    • 0025635897 scopus 로고
    • The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptipyl-prolyl cis-trans isomerase
    • Siekierka, J.J., Wiederrecht, G., Greulich, H., Boulton, D., Hung, S.H.Y., Cryan, J., Hodges, P.J. and Sigal, N.H. (1990) The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptipyl-prolyl cis-trans isomerase. J. Biol. Chem., 265, 21011-21015.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21011-21015
    • Siekierka, J.J.1    Wiederrecht, G.2    Greulich, H.3    Boulton, D.4    Hung, S.H.Y.5    Cryan, J.6    Hodges, P.J.7    Sigal, N.H.8
  • 55
    • 0029944441 scopus 로고    scopus 로고
    • Signaling via hetero- Oligomeric complexes of type I and type II serine/threonine kinase receptors
    • ten Dijke, P., Miyazono, K. and Heldin, C.H. (1996) Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors. Curr. Opin. Cell Biol., 8, 139-145.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 139-145
    • Dijke, P.1    Miyazono, K.2    Heldin, C.H.3
  • 56
    • 0028171082 scopus 로고
    • Reconstitution and transphosphorylation of TGF-beta receptor complexes
    • Ventura, F., Doody, J., Liu, F., Wrana, J.L. and Massagué, J. (1994) Reconstitution and transphosphorylation of TGF-beta receptor complexes. EMBO J., 13, 5581-5589.
    • (1994) EMBO J. , vol.13 , pp. 5581-5589
    • Ventura, F.1    Doody, J.2    Liu, F.3    Wrana, J.L.4    Massagué, J.5
  • 57
    • 0029941824 scopus 로고    scopus 로고
    • Interaction of transforming growth factor-β receptor I with farnesyl-protein transferase-α in yeast and mammalian cells
    • Ventura, F., Liu, F., Doody, J. and Massagué, J. (1996) Interaction of transforming growth factor-β receptor I with farnesyl-protein transferase-α in yeast and mammalian cells. J. Biol. Chem., 271, 13931-13934.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13931-13934
    • Ventura, F.1    Liu, F.2    Doody, J.3    Massagué, J.4
  • 58
    • 0028931686 scopus 로고
    • Signaling activity of homologous and heterologous transforming growth factor-beta receptor kinase complexes
    • Vivien, D., Attisano, L., Wrana, J.L. and Massagué, J. (1995) Signaling activity of homologous and heterologous transforming growth factor-beta receptor kinase complexes. J. Biol. Chem., 270, 7134-7141.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7134-7141
    • Vivien, D.1    Attisano, L.2    Wrana, J.L.3    Massagué, J.4
  • 59
    • 0028108801 scopus 로고
    • Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12
    • Wang, T., Donahoe, P.K. and Zervos, A.S. (1994) Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12. Science, 265, 674-676.
    • (1994) Science , vol.265 , pp. 674-676
    • Wang, T.1    Donahoe, P.K.2    Zervos, A.S.3
  • 60
    • 0029670049 scopus 로고    scopus 로고
    • The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling
    • Wang, T., Danielson, P.D., Li, B.Y., Shah, P.C., Kim, S.D. and Donahoe, P.K. (1996a) The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling. Science, 271, 1120-1122.
    • (1996) Science , vol.271 , pp. 1120-1122
    • Wang, T.1    Danielson, P.D.2    Li, B.Y.3    Shah, P.C.4    Kim, S.D.5    Donahoe, P.K.6
  • 62
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling
    • Weis-Garcia, F. and Massagué, J. (1996) Complementation between kinase-defective and activation-defective TGF-β receptors reveals a novel form of receptor cooperativity essential for signaling. EMBO J., 15, 276-289.
    • (1996) EMBO J. , vol.15 , pp. 276-289
    • Weis-Garcia, F.1    Massagué, J.2
  • 63
    • 0026799412 scopus 로고
    • Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex
    • Wiederrecht, G., Hung, S., Chan, H.K., Marcy, A., Martin, M., Calaycay, J., Sigal, N., Kincaid, R.L. and Siekierka, J.J. (1992) Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex. J. Biol. Chem., 267, 21753-21760.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21753-21760
    • Wiederrecht, G.1    Hung, S.2    Chan, H.K.3    Marcy, A.4    Martin, M.5    Calaycay, J.6    Sigal, N.7    Kincaid, R.L.8    Siekierka, J.J.9
  • 64
    • 0030037438 scopus 로고    scopus 로고
    • Mad acts downstream of Dpp receptors, revealing a differential requirement for dpp signaling in initiation and propagation of morphogenesis in the Drosophila eye
    • Wiersdorff, V., Lecuit, T., Cohen, S.M. and Mlodzik, M. (1996) Mad acts downstream of Dpp receptors, revealing a differential requirement for dpp signaling in initiation and propagation of morphogenesis in the Drosophila eye. Development, 122, 2153-2162.
    • (1996) Development , vol.122 , pp. 2153-2162
    • Wiersdorff, V.1    Lecuit, T.2    Cohen, S.M.3    Mlodzik, M.4
  • 65
    • 0027367937 scopus 로고
    • Signaling activity of transforming growth factor beta type II receptors lacking specific domains in the cytoplasmic region
    • Wieser, R., Attisano, L., Wrana, J.L. and Massagué, J. (1993) Signaling activity of transforming growth factor beta type II receptors lacking specific domains in the cytoplasmic region. Mol. Cell. Biol., 13, 7239-7247.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7239-7247
    • Wieser, R.1    Attisano, L.2    Wrana, J.L.3    Massagué, J.4
  • 66
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex
    • Wieser, R., Wrana, J.L. and Massagué, J. (1995) GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex. EMBO J., 14, 2199-2208.
    • (1995) EMBO J. , vol.14 , pp. 2199-2208
    • Wieser, R.1    Wrana, J.L.2    Massagué, J.3
  • 69
    • 0027463577 scopus 로고
    • A composite FKBP12-FK506 surface that contacts calcineurin
    • Yang, D., Rosen, M.K. and Schreiber, S.L. (1993) A composite FKBP12-FK506 surface that contacts calcineurin. J. Am. Chem. Soc., 115, 819-820.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 819-820
    • Yang, D.1    Rosen, M.K.2    Schreiber, S.L.3
  • 70
    • 0029786212 scopus 로고    scopus 로고
    • Receptor-associated Mad homologues synergize as effectors of the TGF-β response
    • Zhang, Y., Feng, X.H., Wu, R.Y. and Derynck, R. (1996) Receptor-associated Mad homologues synergize as effectors of the TGF-β response. Nature, 383, 168-172.
    • (1996) Nature , vol.383 , pp. 168-172
    • Zhang, Y.1    Feng, X.H.2    Wu, R.Y.3    Derynck, R.4
  • 71
    • 0030598829 scopus 로고    scopus 로고
    • The Spemann Organizer signal noggin binds and inactivates bone morphorgenetic protein 4
    • Zimmerman, L.B., De Jesus-Escobar, J.M. and Harland, R.M. (1996) The Spemann Organizer signal noggin binds and inactivates bone morphorgenetic protein 4. Cell, 86, 599-606.
    • (1996) Cell , vol.86 , pp. 599-606
    • Zimmerman, L.B.1    De Jesus-Escobar, J.M.2    Harland, R.M.3


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