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Volumn 400, Issue 6745, 1999, Pages 687-693

A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN; PROTEIN SERINE THREONINE KINASE; TRANSFORMING GROWTH FACTOR BETA; UBIQUITIN PROTEIN LIGASE;

EID: 0033549789     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/23293     Document Type: Article
Times cited : (726)

References (30)
  • 1
    • 0028180315 scopus 로고
    • The TGF-β superfamily: New members, new receptors, and new genetic tests of function in different organisms
    • Kingsley, D. M. The TGF-β superfamily: new members, new receptors, and new genetic tests of function in different organisms. Genes Dev. 8, 133-146 (1994).
    • (1994) Genes Dev. , vol.8 , pp. 133-146
    • Kingsley, D.M.1
  • 2
    • 0030271736 scopus 로고    scopus 로고
    • Regulation of differentiation by TGF-beta
    • Moses, H. L. & Serra, R. Regulation of differentiation by TGF-beta. Curr. Opin. Genet. Dev. 6, 581-586 (1996).
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 581-586
    • Moses, H.L.1    Serra, R.2
  • 3
    • 0031469373 scopus 로고    scopus 로고
    • Formation and Function of Spemann's organizer
    • Harland, R. & Gerhart, J. Formation and Function of Spemann's organizer. Annu. Rev. Cell Biol. 13, 611-667 (1997).
    • (1997) Annu. Rev. Cell Biol. , vol.13 , pp. 611-667
    • Harland, R.1    Gerhart, J.2
  • 4
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague, J. TGF-beta signal transduction. Annu. Rev. Biochem. 67, 753-791 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 5
    • 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
  • 6
    • 0029126514 scopus 로고
    • Analyzing protein-protein interactions using two-hybrid system
    • Bartel, P. & Fields, S. Analyzing protein-protein interactions using two-hybrid system. Methods Enzymol. 254, 241-263 (1995).
    • (1995) Methods Enzymol. , vol.254 , pp. 241-263
    • Bartel, P.1    Fields, S.2
  • 7
    • 0028907874 scopus 로고
    • Family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Published erratum appears in Proc. Natl Acad. Sci. USA 92, 5249 (1995)
    • Huibregtse, J. M., Scheffner, M., Beaudenon, S. & Howley, P. M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA 92, 2563-2567 (1995). [Published erratum appears in Proc. Natl Acad. Sci. USA 92, 5249 (1995). ]
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.A.4
  • 9
    • 0030006130 scopus 로고    scopus 로고
    • Publ acts as an E6-AP-like protein ubiquitin ligase in the degradation of cdc25
    • Nefsky, B. & Beach, D. Publ acts as an E6-AP-like protein ubiquitin ligase in the degradation of cdc25. EMBO J. 15, 1301-1312 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1301-1312
    • Nefsky, B.1    Beach, D.2
  • 10
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, B. D. & Howley, P. M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505 (1993).
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, B.D.3    Howley, P.M.4
  • 11
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein, C., Springael, J., Volland, C., Haguenauer-Tsapis, R. & Andre, B. NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol. 18, 77-87 (1995).
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.2    Volland, C.3    Haguenauer-Tsapis, R.4    Andre, B.5
  • 12
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski, E. A. & Falke, J. J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5, 2375-2390 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 14
    • 0030781598 scopus 로고    scopus 로고
    • WW (WWP) domains: From structure to function
    • Rotin, D. WW (WWP) domains: from structure to function. Curr. Top. Microbiol. Immunol. 228, 115-133 (1998).
    • (1998) Curr. Top. Microbiol. Immunol. , vol.228 , pp. 115-133
    • Rotin, D.1
  • 15
    • 0028110497 scopus 로고
    • On the function of BMP-4 in patterning the marginal zone of the Xenopus embryo
    • Fainsod, A., Steinbeisser, H. & De Robertis, E. M. On the function of BMP-4 in patterning the marginal zone of the Xenopus embryo. EMBO J. 13, 5015-5025 (1994).
    • (1994) EMBO J. , vol.13 , pp. 5015-5025
    • Fainsod, A.1    Steinbeisser, H.2    De Robertis, E.M.3
  • 16
    • 0029148342 scopus 로고
    • Ventral mesodermal patterning in Xenopus embryos: Expression patterns and activities of BMP-2 and BMP-4
    • Hemmati-Brivanlou, A. & Thomsen, G. H. Ventral mesodermal patterning in Xenopus embryos: expression patterns and activities of BMP-2 and BMP-4. Dev. Genet. 17, 78-89 (1995).
    • (1995) Dev. Genet. , vol.17 , pp. 78-89
    • Hemmati-Brivanlou, A.1    Thomsen, G.H.2
  • 17
    • 0032102668 scopus 로고    scopus 로고
    • Ventral mesoderm induction and patterning by BMP heterodimers in Xenopus embryos
    • Nishimatsu, S. & Thomsen, G. H. Ventral mesoderm induction and patterning by BMP heterodimers in Xenopus embryos. Mech. Dev. 74, 75-88 (1997).
    • (1997) Mech. Dev. , vol.74 , pp. 75-88
    • Nishimatsu, S.1    Thomsen, G.H.2
  • 18
    • 0029834231 scopus 로고    scopus 로고
    • Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor
    • Thomsen, G. H. Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor. Development 122, 2359-2366 (1996).
    • (1996) Development , vol.122 , pp. 2359-2366
    • Thomsen, G.H.1
  • 19
    • 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
  • 20
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier, M., Staszewski, L. M. & Bohmann, D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78, 787-798 (1994).
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 21
    • 0032475884 scopus 로고    scopus 로고
    • Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2
    • Macias-Silva, M., Hoodless, P. A., Tang, S. J., Buchwald, M. & Wrana, J. L. Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2, J. Biol. Chem. 273, 25628-25636 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 25628-25636
    • Macias-Silva, M.1    Hoodless, P.A.2    Tang, S.J.3    Buchwald, M.4    Wrana, J.L.5
  • 22
    • 0033559209 scopus 로고    scopus 로고
    • Dominant-negative Smad2 mutants inhibit activin/Vg1 signaling and disrupt axis formation in Xenopus
    • Hoodless, P. A. et al. Dominant-negative Smad2 mutants inhibit activin/Vg1 signaling and disrupt axis formation in Xenopus. Dev. Biol. 207, 364-379 (1999).
    • (1999) Dev. Biol. , vol.207 , pp. 364-379
    • Hoodless, P.A.1
  • 23
    • 0030937808 scopus 로고    scopus 로고
    • Vertebrate embryonic cells will become nerve cells unless told otherwise
    • Hemmati-Brivanlou, A. & Melton, D. Vertebrate embryonic cells will become nerve cells unless told otherwise. Cell 88, 13-17 (1997).
    • (1997) Cell , vol.88 , pp. 13-17
    • Hemmati-Brivanlou, A.1    Melton, D.2
  • 24
    • 0030886059 scopus 로고    scopus 로고
    • Concentration-dependent patterning of the Xenopus ectoderm by BMP4 and its signal transducer Smad1
    • Wilson, P. A., Lagna, G., Suzuki, A. & Hemmati-Brivanlou, A. Concentration-dependent patterning of the Xenopus ectoderm by BMP4 and its signal transducer Smad1. Development 124, 3177-3184 (1997).
    • (1997) Development , vol.124 , pp. 3177-3184
    • Wilson, P.A.1    Lagna, G.2    Suzuki, A.3    Hemmati-Brivanlou, A.4
  • 26
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • Lagna, G., Hata, A., Hemmati-Brivanlou, A. & Massague, J. Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. Nature 383, 832-836 (1996).
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    Hemmati-Brivanlou, A.3    Massague, J.4
  • 27
    • 0030663881 scopus 로고    scopus 로고
    • Cellular interpretation of multiple TGF-beta signals: Intracellular antagonism between activin/BVg1 and BMP-2/4 signaling mediated by Smads
    • Candia, A. F. et al. Cellular interpretation of multiple TGF-beta signals: intracellular antagonism between activin/BVg1 and BMP-2/4 signaling mediated by Smads. Development 124, 4467-4480 (1997).
    • (1997) Development , vol.124 , pp. 4467-4480
    • Candia, A.F.1
  • 28
    • 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. MADR2 maps to 18q21 and encodes a TGFβ regulated MAD-related protein that is functionally mutated in colorectal carcinoma. Cell 86, 543-552 (1996).
    • (1996) Cell , vol.86 , pp. 543-552
    • Eppert, K.1
  • 29
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S. & Kopito, R. R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127 (1995).
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.