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Volumn 12, Issue 14, 1998, Pages 2153-2163

The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for Smad3 in TGF-β-induced transcriptional activation

Author keywords

CBP p300; PAI 1 promoter; Smad; TGF signaling; Transcription

Indexed keywords

ADAPTOR PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; DNA BINDING PROTEIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; NUCLEOPROTEIN; PLASMINOGEN ACTIVATOR INHIBITOR 1; TRANSCRIPTION FACTOR; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; VIRUS PROTEIN;

EID: 0032528236     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.14.2153     Document Type: Article
Times cited : (464)

References (41)
  • 3
    • 0030663881 scopus 로고    scopus 로고
    • Cellular interpretation of multiple TGF-β signals: Intracellular antagonism between activin/BVg1 and BMP-2/4 signaling mediated by Smads
    • Candia, A., T. Watabe, S. Hawley, D. Onichtchouk, Y. Zhang, R. Derynck, C. Niehrs, and K.W.Y. Cho. 1997. Cellular interpretation of multiple TGF-β signals: Intracellular antagonism between activin/BVg1 and BMP-2/4 signaling mediated by Smads. Development 124: 4467-4480.
    • (1997) Development , vol.124 , pp. 4467-4480
    • Candia, A.1    Watabe, T.2    Hawley, S.3    Onichtchouk, D.4    Zhang, Y.5    Derynck, R.6    Niehrs, C.7    Cho, K.W.Y.8
  • 4
    • 0028937160 scopus 로고
    • Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor β receptor kinases
    • Chen, F. and R.A. Weinberg. 1995. Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor β receptor kinases. Proc. Natl. Acad. Sci. 92: 1565-1569.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 1565-1569
    • Chen, F.1    Weinberg, R.A.2
  • 6
    • 0029073142 scopus 로고
    • Transforming growth factor β induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism
    • Datto, M., Y. Li, J. Panus, D. Howe, Y. Xiong, and X.-F. Wang. 1995. Transforming growth factor β induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism. Proc. Natl. Acad. Sci. 92: 5545-5549.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 5545-5549
    • Datto, M.1    Li, Y.2    Panus, J.3    Howe, D.4    Xiong, Y.5    Wang, X.-F.6
  • 7
    • 0030265714 scopus 로고    scopus 로고
    • Intracellular signaling: The Mad way to do it
    • Derynck, R. and Y. Zhang. 1996. Intracellular signaling: The Mad way to do it. Curr. Biol. 6: 1226-1229.
    • (1996) Curr. Biol. , vol.6 , pp. 1226-1229
    • Derynck, R.1    Zhang, Y.2
  • 9
    • 17544376741 scopus 로고    scopus 로고
    • Ligand-independent activation of TGF-β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors
    • Feng, X.-H. and R. Derynck. 1996. Ligand-independent activation of 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
  • 10
    • 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 R. Derynck. 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
  • 11
    • 0028972072 scopus 로고
    • TGF-β-induced downregulation of cyclin A expression requires a functional TGF-β receptor complex. Characterization of chimeric and truncated type I and type II receptors
    • Feng, X.-H., E.H. Filvaroff, and R. Derynck. 1995. TGF-β-induced downregulation of cyclin A expression requires a functional TGF-β 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
  • 12
    • 0030625679 scopus 로고    scopus 로고
    • The multifunctional role of the co-activator CBP in transcriptional regulation
    • Goldman, P., V. Tran, and R.H. Goodman. 1997. The multifunctional role of the co-activator CBP in transcriptional regulation. Recent Prog. Hormone Res. 52: 103-119.
    • (1997) Recent Prog. Hormone Res. , vol.52 , pp. 103-119
    • Goldman, P.1    Tran, V.2    Goodman, R.H.3
  • 13
    • 0026515183 scopus 로고
    • Progression of colorectal cancer is associated with multiple tumor suppressor gene defects but inhibition of tumorigenicity is accomplished by correction of any single defect via chromosome transfer
    • Goyette, M.C., K. Cho, C.L. Fasching, D.B. Levy, K.W. Kinzler, C. Paraskeva, B. Vogelstein, and E. Stanbridge. 1992. Progression of colorectal cancer is associated with multiple tumor suppressor gene defects but inhibition of tumorigenicity is accomplished by correction of any single defect via chromosome transfer. Mol. Cell. Biol. 12: 1387-1395.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1387-1395
    • Goyette, M.C.1    Cho, K.2    Fasching, C.L.3    Levy, D.B.4    Kinzler, K.W.5    Paraskeva, C.6    Vogelstein, B.7    Stanbridge, E.8
  • 14
    • 0024816337 scopus 로고
    • Human transforming growth factor-β 3: Recombinant expression, purification, and biological activities in comparison with transforming growth factors-β1 and -β2
    • Graycar, J.L., D.A. Miller, B.A. Arrick, R.M. Lyons, H.L. Moses, and R. Derynck. 1989. Human transforming growth factor-β 3: Recombinant expression, purification, and biological activities in comparison with transforming growth factors-β1 and -β2. Mol. Endocrinol. 3: 1977-1986.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1977-1986
    • Graycar, J.L.1    Miller, D.A.2    Arrick, B.A.3    Lyons, R.M.4    Moses, H.L.5    Derynck, R.6
  • 15
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris, J., E. Golemis, H. Chertkov, and R. Brent. 1993. Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75: 791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 16
    • 0030825516 scopus 로고    scopus 로고
    • Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4
    • Hata, A., R. Lo, D. Wotton, G. Lagna, and J. Massagué. 1997. Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4. Nature 88: 82-87.
    • (1997) Nature , vol.88 , pp. 82-87
    • Hata, A.1    Lo, R.2    Wotton, D.3    Lagna, G.4    Massagué, J.5
  • 17
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signalling from cell membrane to nucleus through SMAD proteins
    • Heldin, C.-H., K. Miyazono, and P. ten Dijke. 1997. TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature 390: 465-471.
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.-H.1    Miyazono, K.2    Ten Dijke, P.3
  • 21
    • 0026334362 scopus 로고
    • Identification of regulatory sequences in the type 1 plasminogen activator inhibitor gene responsive to transforming growth factor β
    • Keeton, M., S. Curriden, A.-J. van Zonneveld, and D.J. Loskutoff. 1991. Identification of regulatory sequences in the type 1 plasminogen activator inhibitor gene responsive to transforming growth factor β. J. Biol. Chem. 266: 23048-23052.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23048-23052
    • Keeton, M.1    Curriden, S.2    Van Zonneveld, A.-J.3    Loskutoff, D.J.4
  • 22
    • 0030872367 scopus 로고    scopus 로고
    • Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decapentaplegic
    • Kim, J., K. Johnson, H. Chen, S. Carroll, and A. Laughon. 1997. Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decapentaplegic. Nature 388: 304-308.
    • (1997) Nature , vol.388 , pp. 304-308
    • Kim, J.1    Johnson, K.2    Chen, H.3    Carroll, S.4    Laughon, A.5
  • 24
    • 0030911104 scopus 로고    scopus 로고
    • The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase
    • Kretzschmar, M., F. Liu, A. Hata, J. Doody, and J. Massagué. 1997. The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally 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
  • 26
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • Lagna, G., A. Hata, A. Hemmati-Brivanlou, and J. Massagué. 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
  • 29
    • 0030300115 scopus 로고    scopus 로고
    • MADR-2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signaling
    • Macías-Silva, M., S. Abdollah, P. Hoodless, R. Pirone, L. Attisano, and J.L. Wrana. 1996. MADR-2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87: 1215-1224.
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macías-Silva, M.1    Abdollah, S.2    Hoodless, P.3    Pirone, R.4    Attisano, L.5    Wrana, J.L.6
  • 30
    • 0030816043 scopus 로고    scopus 로고
    • TGF-β signalling through the Smad pathway
    • Massagué, J., A. Hata, and F. Liu. 1997. TGF-β signalling through the Smad pathway. Trends Cell Biol. 7: 187-192.
    • (1997) Trends Cell Biol. , vol.7 , pp. 187-192
    • Massagué, J.1    Hata, A.2    Liu, F.3
  • 32
    • 0030837455 scopus 로고    scopus 로고
    • A structural basis for mutational inactivation of the tumour suppressor Smad4
    • Shi, Y., A. Hata, R. Lo, J. Massagué, and N. Pavletich. 1997. A structural basis for mutational inactivation of the tumour suppressor Smad4. Nature 388: 87-93.
    • (1997) Nature , vol.388 , pp. 87-93
    • Shi, Y.1    Hata, A.2    Lo, R.3    Massagué, J.4    Pavletich, N.5
  • 33
    • 0343417089 scopus 로고    scopus 로고
    • The p300/CBP family: Integrating signals with transcription factors and chromatin
    • Shikama, N., J. Lyon, and N. La Thangue. 1997. The p300/CBP family: Integrating signals with transcription factors and chromatin. Trends Cell Biol. 7: 230-236.
    • (1997) Trends Cell Biol. , vol.7 , pp. 230-236
    • Shikama, N.1    Lyon, J.2    La Thangue, N.3
  • 34
    • 0000976047 scopus 로고
    • Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization
    • Silver, P., L. Keegan, and M. Ptashne. 1984. Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization. Proc. Natl. Acad. Sci. 81: 5951-5955.
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 5951-5955
    • Silver, P.1    Keegan, L.2    Ptashne, M.3
  • 36
    • 0029842713 scopus 로고    scopus 로고
    • MAD-related proteins in TGF-β signalling
    • Wrana, J.L. and L. Attisano. 1996. MAD-related proteins in TGF-β signalling. Trends Genet. 12: 493-496.
    • (1996) Trends Genet. , vol.12 , pp. 493-496
    • Wrana, J.L.1    Attisano, L.2
  • 38
    • 0030974042 scopus 로고    scopus 로고
    • Homomeric and heteromeric interactions are required for signaling activity and functional cooperativity of Smad-3 and -4
    • Wu, R.-Y., Y. Zhang, X.-H. Feng, and R. Derynck. 1997. Homomeric and heteromeric interactions are required for signaling activity and functional cooperativity of Smad-3 and -4. Mol. Cell. Biol. 17: 2521-2528.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2521-2528
    • Wu, R.-Y.1    Zhang, Y.2    Feng, X.-H.3    Derynck, R.4
  • 39
    • 0030697971 scopus 로고    scopus 로고
    • Tumor suppressor Smad4 is a transforming growth factor β-inducible DNA binding protein
    • Yingling, J., M. Datto, C. Wong, J. Frederick, N. Liberati, and X.-F. Wang. 1997. Tumor suppressor Smad4 is a transforming growth factor β-inducible DNA binding protein. Mol. Cell. Biol. 17: 7019-7028.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7019-7028
    • Yingling, J.1    Datto, M.2    Wong, C.3    Frederick, J.4    Liberati, N.5    Wang, X.-F.6
  • 40
    • 0029786212 scopus 로고    scopus 로고
    • Receptor-associated Mad homologues synergize as effectors of the TGF-β response
    • Zhang, Y., X.-H. Feng, R.-Y. Wu, and R. Derynck. 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
  • 41
    • 0031128153 scopus 로고    scopus 로고
    • The tumor suppressor Smad4/DPC4 as a central mediator of Smad function: Cooperativity with other Smads and interference of a Smad4/DPC4 mutant with nuclear translocation of Smads. Curr
    • Zhang, Y., T. Musci, and R. Derynck. 1997. The tumor suppressor Smad4/DPC4 as a central mediator of Smad function: Cooperativity with other Smads and interference of a Smad4/DPC4 mutant with nuclear translocation of Smads. Curr. Biol. 7: 270-276.
    • (1997) Biol. , vol.7 , pp. 270-276
    • Zhang, Y.1    Musci, T.2    Derynck, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.