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Volumn 1, Issue 8, 1999, Pages 472-478

Ubiquitin-dependent degradation of TGF-β-activated Smad2

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; DNA BINDING PROTEIN; MULTIENZYME COMPLEX; PROTEASOME; SMAD2 PROTEIN; SMAD2 PROTEIN, HUMAN; TRANSACTIVATOR PROTEIN; TRANSFORMING GROWTH FACTOR BETA; UBIQUITIN;

EID: 0033257926     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/70258     Document Type: Article
Times cited : (303)

References (30)
  • 2
    • 0025222517 scopus 로고
    • The transforming growth factor-β family
    • Massagué, J. The transforming growth factor-β family. Annu. Rev. Cell Biol. 6, 597-641 (1990).
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 597-641
    • Massagué, J.1
  • 3
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan, B. L. M. Bone morphogenetic proteins: multifunctional regulators of vertebrate development. Genes Dev. 10, 1580-1594 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 1580-1594
    • Hogan, B.L.M.1
  • 4
    • 0032529159 scopus 로고    scopus 로고
    • Smads and early developmental signaling by the TGFβ superfamily
    • Whitman, M. Smads and early developmental signaling by the TGFβ superfamily. Genes Dev. 12, 2445-2462 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2445-2462
    • Whitman, M.1
  • 5
    • 0031685620 scopus 로고    scopus 로고
    • TGFβ signal transduction
    • Massagué, J. TGFβ signal transduction. Annu. Rev. Biochem. 67, 753-791 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 6
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signalling from cell membrane to nucleus through SMAD proteins
    • Heldin, C.-H., Miyazono, K. & ten Dijke, P. TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature 390, 465-471 (1997).
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.-H.1    Miyazono, K.2    Ten Dijke, P.3
  • 7
    • 0033168915 scopus 로고    scopus 로고
    • Regulation of Smad signaling by protein associations and signaling crosstalk
    • Zhang, Y. & Derynck, R. Regulation of Smad signaling by protein associations and signaling crosstalk. Trends Cell Biol. 9, 274-279 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 274-279
    • Zhang, Y.1    Derynck, R.2
  • 8
    • 0030613249 scopus 로고    scopus 로고
    • TβRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling
    • Abdollah, S. et al. TβRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J. Biol Chem. 272, 27678-27685 (1997).
    • (1997) J. Biol Chem. , vol.272 , pp. 27678-27685
    • Abdollah, S.1
  • 9
    • 0030613262 scopus 로고    scopus 로고
    • Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling
    • Souchelnytskyi, S. et al. Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling. J. Biol. Chem. 272, 28107-28115 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28107-28115
    • Souchelnytskyi, S.1
  • 10
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L. et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771 (1994).
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1
  • 11
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G. et al. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731 (1995).
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1
  • 12
    • 0030961168 scopus 로고    scopus 로고
    • Smad4 and FAST-1 in the assembly of activin-responsive factor
    • Chen, X. et al. Smad4 and FAST-1 in the assembly of activin-responsive factor. Nature 389, 85-89 (1997).
    • (1997) Nature , vol.389 , pp. 85-89
    • Chen, X.1
  • 13
    • 0030690337 scopus 로고    scopus 로고
    • Dual role of the Smad4/DPC4 tumor suppressor in TGFβ-inducible transcriptional responses
    • Liu, F., Pouponnot, C. & Massagué, J. Dual role of the Smad4/DPC4 tumor suppressor in TGFβ-inducible transcriptional responses. Genes Dev. 11, 3157-3167 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 3157-3167
    • Liu, F.1    Pouponnot, C.2    Massagué, J.3
  • 14
    • 0032110463 scopus 로고    scopus 로고
    • Smad2 and Smad3 positively and negatively regulate TGFβ-dependent transcription through the forkhead DNA-binding protein FAST2
    • Labbé, E., Silvestri, C., Hoodless, P. A., Wrana, J. L. & Attisano, L. Smad2 and Smad3 positively and negatively regulate TGFβ-dependent transcription through the forkhead DNA-binding protein FAST2. Mol. Cell 2, 109-120 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 109-120
    • Labbé, E.1    Silvestri, C.2    Hoodless, P.A.3    Wrana, J.L.4    Attisano, L.5
  • 15
    • 0032909167 scopus 로고    scopus 로고
    • Fast2 is a mammalian winged helix protein that mediates TGFβ signals
    • Liu, B., Dou, C., Prabhu, L. & Lai, E. Fast2 is a mammalian winged helix protein that mediates TGFβ signals. Mol. Cell Biol. 19, 424-430 (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 424-430
    • Liu, B.1    Dou, C.2    Prabhu, L.3    Lai, E.4
  • 16
    • 0033515620 scopus 로고    scopus 로고
    • A Smad transcriptional corepressor
    • Wotton, D., Lo, R. S., Lee, S. & Massagué, J. A Smad transcriptional corepressor. Cell 97, 29-39 (1999).
    • (1999) Cell , vol.97 , pp. 29-39
    • Wotton, D.1    Lo, R.S.2    Lee, S.3    Massagué, J.4
  • 17
    • 0029829230 scopus 로고    scopus 로고
    • A novel mesoderm inducer, mMadr-2, functions in the activin signal transduction pathway
    • Baker, J. & Harland, R. M. A novel mesoderm inducer, mMadr-2, functions in the activin signal transduction pathway. Genes Dev. 10, 1880-1889 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 1880-1889
    • Baker, J.1    Harland, R.M.2
  • 18
    • 0029931509 scopus 로고    scopus 로고
    • A human Mad protein acting as a BMP-regulated transcriptional activator
    • Liu, F. et al. A human Mad protein acting as a BMP-regulated transcriptional activator. Nature 381, 620-623 (1996).
    • (1996) Nature , vol.381 , pp. 620-623
    • Liu, F.1
  • 19
    • 0030825516 scopus 로고    scopus 로고
    • Mutations increasing autoinhibition inactivate the tumour suppressors Smad2 and Smad4
    • Hata, A., Lo, R. S., Wotton, D., Lagna, M. & Massagué, J. Mutations increasing autoinhibition inactivate the tumour suppressors Smad2 and Smad4. Nature 388, 82-86 (1997).
    • (1997) Nature , vol.388 , pp. 82-86
    • Hata, A.1    Lo, R.S.2    Wotton, D.3    Lagna, M.4    Massagué, J.5
  • 20
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover, A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17, 7151-7160 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 21
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney, J. D. & Hochstrasser, M. Substrate targeting in the ubiquitin system. Cell 97, 427-430 (1999).
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 22
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V. et al. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583 (1989).
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1
  • 23
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate ot the TGFβ receptor and phosphorylation is required for nuclear accumulation and signaling
    • Macias-Silva, M. et al. MADR2 is a substrate ot the TGFβ receptor and phosphorylation is required for nuclear accumulation and signaling. Cell 87, 1215-1224 (1996).
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macias-Silva, M.1
  • 24
    • 0030911104 scopus 로고    scopus 로고
    • The TGF-β mediator Smad1 is directly phosphorylated and functionally activated by the BMP receptor kinase
    • Kretzschmar, M., Liu, F., Hata, A., Doody, J. & Massagué, J. The TGF-β mediator Smad1 is directly phosphorylated and functionally activated by the BMP receptor kinase. Genes Dev. 11, 984-995 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 984-995
    • Kretzschmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massagué, J.5
  • 25
    • 0033083158 scopus 로고    scopus 로고
    • Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP
    • Spencer, E., Jiang, J. and Chen, Z. J. Signal-induced ubiquitination of IκBα by the F-box protein Slimb/β-TrCP. Genes Dev. 13, 284-294 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 284-294
    • Spencer, E.1    Jiang, J.2    Chen, Z.J.3
  • 26
    • 0033591363 scopus 로고    scopus 로고
    • Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation of subsequent degradation of IκBα
    • Gonen, H. et al. Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation of subsequent degradation of IκBα. J. Biol. Chem. 274, 14823-14830 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 14823-14830
    • Gonen, H.1
  • 27
    • 0033106149 scopus 로고    scopus 로고
    • A ubiquitin ligase complex essential for the NF-κB, Wnt/Wingless, and Hedgehog signaling pathways
    • Maniatis, T. A ubiquitin ligase complex essential for the NF-κB, Wnt/Wingless, and Hedgehog signaling pathways. Genes Dev. 13, 505-510 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 505-510
    • Maniatis, T.1
  • 28
    • 0033549789 scopus 로고    scopus 로고
    • A Smad ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • Zhu, H. et al. A Smad ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400, 687-693 (1999).
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1
  • 29
    • 0033106484 scopus 로고    scopus 로고
    • A mechanism of repression of TGFβ/Smad signaling by ongenic ras
    • Kretzschmar, M., Doody, J., Timokhina, I. & Massagué, J. A mechanism of repression of TGFβ/Smad signaling by ongenic ras. Genes Dev. 13, 804-816 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 804-816
    • Kretzschmar, M.1    Doody, J.2    Timokhina, I.3    Massagué, J.4
  • 30
    • 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. G., Pavletich, N. & Massagué, J. The L3 loop: a structural motif determining specific interactions between SMAD proteins and TGF-β receptors. EMBO J 17, 996-1005 (1998).
    • (1998) EMBO J , vol.17 , pp. 996-1005
    • Lo, R.S.1    Chen, Y.G.2    Shi, Y.G.3    Pavletich, N.4    Massagué, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.