Myostatin signaling through Smad2, Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism

As a member of the TGF-β superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the myostatin signal transduction pathway, we used a luciferase reporter assay to elucidate myostatin-induced activity. The myostatin-induced transcripti...

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Published inCytokine (Philadelphia, Pa.) Vol. 26; no. 6; pp. 262 - 272
Main Authors Zhu, Xiangyang, Topouzis, Stavros, Liang, Li-fang, Stotish, Ronald L.
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 21.06.2004
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Abstract As a member of the TGF-β superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the myostatin signal transduction pathway, we used a luciferase reporter assay to elucidate myostatin-induced activity. The myostatin-induced transcription requires the participation of regulatory Smads (Smad2/3) and Co-Smads (Smad4). Conversely, inhibitory Smad7, but not Smad6, dramatically reduces the myostatin-induced transcription. This Smad7 inhibition is enhanced by co-expression of Smurf1. We have also shown that Smad7 expression is stimulated by myostatin via the interaction between Smad2, Smad3, Smad4 and the SBE (Smad binding element) in the Smad7 promoter. These results suggest that the myostatin signal transduction pathway is regulated by Smad7 through a negative feedback mechanism.
AbstractList As a member of the TGF-b superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the myostatin signal transduction pathway, we used a luciferase reporter assay to elucidate myostatin-induced activity. The myostatin-induced transcription requires the participation of regulatory Smads (Smad2/3) and Co-Smads (Smad4). Conversely, inhibitory Smad7, but not Smad6, dramatically reduces the myostatin- induced transcription. This Smad7 inhibition is enhanced by co-expression of Smurf1. We have also shown that Smad7 expression is stimulated by myostatin via the interaction between Smad2, Smad3, Smad4 and the SBE (Smad binding element) in the Smad7 promoter. These results suggest that the myostatin signal transduction pathway is regulated by Smad7 through a negative feedback mechanism.
As a member of the TGF-beta superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the myostatin signal transduction pathway, we used a luciferase reporter assay to elucidate myostatin-induced activity. The myostatin-induced transcription requires the participation of regulatory Smads (Smad2/3) and Co-Smads (Smad4). Conversely, inhibitory Smad7, but not Smad6, dramatically reduces the myostatin-induced transcription. This Smad7 inhibition is enhanced by co-expression of Smurf1. We have also shown that Smad7 expression is stimulated by myostatin via the interaction between Smad2, Smad3, Smad4 and the SBE (Smad binding element) in the Smad7 promoter. These results suggest that the myostatin signal transduction pathway is regulated by Smad7 through a negative feedback mechanism.As a member of the TGF-beta superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the myostatin signal transduction pathway, we used a luciferase reporter assay to elucidate myostatin-induced activity. The myostatin-induced transcription requires the participation of regulatory Smads (Smad2/3) and Co-Smads (Smad4). Conversely, inhibitory Smad7, but not Smad6, dramatically reduces the myostatin-induced transcription. This Smad7 inhibition is enhanced by co-expression of Smurf1. We have also shown that Smad7 expression is stimulated by myostatin via the interaction between Smad2, Smad3, Smad4 and the SBE (Smad binding element) in the Smad7 promoter. These results suggest that the myostatin signal transduction pathway is regulated by Smad7 through a negative feedback mechanism.
As a member of the TGF-β superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the myostatin signal transduction pathway, we used a luciferase reporter assay to elucidate myostatin-induced activity. The myostatin-induced transcription requires the participation of regulatory Smads (Smad2/3) and Co-Smads (Smad4). Conversely, inhibitory Smad7, but not Smad6, dramatically reduces the myostatin-induced transcription. This Smad7 inhibition is enhanced by co-expression of Smurf1. We have also shown that Smad7 expression is stimulated by myostatin via the interaction between Smad2, Smad3, Smad4 and the SBE (Smad binding element) in the Smad7 promoter. These results suggest that the myostatin signal transduction pathway is regulated by Smad7 through a negative feedback mechanism.
Author Zhu, Xiangyang
Topouzis, Stavros
Stotish, Ronald L.
Liang, Li-fang
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  fullname: Stotish, Ronald L.
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Cites_doi 10.1038/316701a0
10.1006/bbrc.2002.6500
10.1016/S0092-8674(00)81250-7
10.3109/08977190109029114
10.1128/MCB.23.20.7230-7242.2003
10.1038/39355
10.1038/ng0997-71
10.1074/jbc.M212663200
10.1126/science.3201241
10.1016/S0962-8924(99)01579-2
10.1016/S1359-6101(01)00027-2
10.1074/jbc.274.47.33412
10.1101/gr.7.9.910
10.1172/JCI0213562
10.1038/39369
10.1016/S0955-0674(99)00081-2
10.1093/emboj/19.8.1745
10.1074/jbc.M003282200
10.1126/science.1069525
10.1074/jbc.275.15.11320
10.1139/o02-161
10.1210/me.2002-0366
10.1038/381620a0
10.1016/0092-8674(93)90489-D
10.1016/S1286-4579(99)00258-0
10.1074/jbc.274.19.13637
10.1074/jbc.273.38.24293
10.1074/jbc.M206379200
10.1101/gad.12.2.186
10.1038/387083a0
10.1093/emboj/17.11.3091
10.1073/pnas.93.23.12992
10.1016/S0092-8674(00)80303-7
10.1093/emboj/16.17.5353
10.1016/S0092-8674(00)81696-7
10.1074/jbc.M002433200
10.1073/pnas.151270098
10.1073/pnas.94.23.12457
10.1165/ajrcmb.25.1.4396
10.1093/emboj/19.19.5178
10.1074/jbc.M002815200
10.1074/jbc.M201901200
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References Nagarajan, Zhang, Li, Chen (BIB38) 1999; 274
Kambadur, Sharma, Smith, Bass (BIB6) 1997; 7
McPherron, Lawler, Lee (BIB1) 1997; 387
Rebbapragada, Benchabane, Wrana, Celeste, Attisano (BIB15) 2003; 2003
Rosendahl, Checchin, Fehniger, ten Dijke, Heldin, Sideras (BIB23) 2001; 25
Hill, Qiu, Hewick, Wolfman (BIB14) 2003; 17
Nakao, Imamura, Souchelnytskyi, Kawabata, Ishisaki, Oeda (BIB22) 1997; 16
von Gersdorff, Susztak, Rezvani, Bitzer, Liang, Bottinger (BIB39) 2000; 275
Zhang, Derynck (BIB17) 1999; 9
Brodin, Ahgren, Dijke, Heldin, Heuchel (BIB41) 2000; 275
Attisano, Wrana (BIB27) 2000; 12
Derynck, Jarrett, Chen, Eaton, Bell, Assoian (BIB9) 1985; 316
Imamura, Takase, Nishihara, Oeda, Hanai, Kawabata (BIB30) 1997; 389
Franzen, ten Dijke, Ichijo, Yamashita, Schulz, Heldin (BIB20) 1993; 75
Sarkar, Sommer (BIB44) 1990; 8
Ishisaki, Yamato, Nakao, Nonaka, Ohguchi, ten Dijke (BIB36) 1998; 273
Hayashi, Abdollah, Qiu, Cai, Xu, Grinnell (BIB37) 1997; 89
Ishisaki, Yamato, Hashimoto, Nakao, Tamaki, Nonaka (BIB33) 1999; 274
Hata, Lagna, Massagué, Hemmati, Hemmati-Brivanlou (BIB34) 1998; 12
Nakao, Afrakhte, Moren, Nakayama, Christian, Heuchel (BIB35) 1997; 389
Wozney, Rosen, Celeste, Mitsock, Whitters, Kriz (BIB10) 1988; 242
Roberts (BIB21) 1999; 1
McPherron, Lee (BIB2) 2002; 109
Massague, Wotton (BIB19) 2000; 19
Zhao, Shi, Chen, Warburton (BIB31) 2000; 275
Hill, Davies, Pearson, Wang, Hewick, Wolfman (BIB13) 2002; 277
Dennler, Itoh, Vivien, ten Dijke, Huet, Gauthier (BIB24) 1998; 17
McPherron, Lee (BIB8) 1997; 94
Derynck, Zhang, Feng (BIB26) 1998; 95
Hoodless, Haerry, Abdollah, Stapleton, O'Connor, Attisano (BIB28) 1996; 85
Stopa, Anhuf, Terstegen, Gatsios, Gressner, Dooley (BIB40) 2000; 275
Zimmers, Davies, Koniaris, Haynes, Esquela, Tomkinson (BIB4) 2002; 296
Thies, Chen, Davies, Tomkinson, Pearson, Shakey (BIB11) 2001; 18
Lee, McPherron (BIB12) 2001; 98
Suzuki, Murakami, Fukuchi, Shimanuki, Shikauchi, Imamura (BIB42) 2002; 277
Arnold, Della-Fera, Baile (BIB3) 2001; 1
Feng, Lin, Derymck (BIB25) 2000; 19
Chen, Lebrun, Vale (BIB32) 1996; 93
Mehra, Wrana (BIB16) 2002; 80
Tajima, Goto, Yoshida, Shinomiya, Sekimoto, Yoneda (BIB43) 2003; 278
Liu, Hata, Baker, Doody, Carcamo, Harland (BIB29) 1996; 381
Grobet, Martin, Poncelet, Pirottin, Brouwers, Riquet (BIB7) 1997; 17
Roberts (BIB18) 2002; 13
Lin, Arnold, Della-Fera, Azain, Hartzell, Baile (BIB5) 2002; 291
Ishisaki (10.1016/j.cyto.2004.03.007_BIB36) 1998; 273
Chen (10.1016/j.cyto.2004.03.007_BIB32) 1996; 93
Tajima (10.1016/j.cyto.2004.03.007_BIB43) 2003; 278
Zimmers (10.1016/j.cyto.2004.03.007_BIB4) 2002; 296
Roberts (10.1016/j.cyto.2004.03.007_BIB21) 1999; 1
Derynck (10.1016/j.cyto.2004.03.007_BIB26) 1998; 95
Hill (10.1016/j.cyto.2004.03.007_BIB13) 2002; 277
Massague (10.1016/j.cyto.2004.03.007_BIB19) 2000; 19
Hayashi (10.1016/j.cyto.2004.03.007_BIB37) 1997; 89
Feng (10.1016/j.cyto.2004.03.007_BIB25) 2000; 19
Mehra (10.1016/j.cyto.2004.03.007_BIB16) 2002; 80
Zhao (10.1016/j.cyto.2004.03.007_BIB31) 2000; 275
Brodin (10.1016/j.cyto.2004.03.007_BIB41) 2000; 275
Hata (10.1016/j.cyto.2004.03.007_BIB34) 1998; 12
von Gersdorff (10.1016/j.cyto.2004.03.007_BIB39) 2000; 275
Imamura (10.1016/j.cyto.2004.03.007_BIB30) 1997; 389
Arnold (10.1016/j.cyto.2004.03.007_BIB3) 2001; 1
McPherron (10.1016/j.cyto.2004.03.007_BIB1) 1997; 387
Derynck (10.1016/j.cyto.2004.03.007_BIB9) 1985; 316
Nakao (10.1016/j.cyto.2004.03.007_BIB22) 1997; 16
Dennler (10.1016/j.cyto.2004.03.007_BIB24) 1998; 17
Nakao (10.1016/j.cyto.2004.03.007_BIB35) 1997; 389
Stopa (10.1016/j.cyto.2004.03.007_BIB40) 2000; 275
Thies (10.1016/j.cyto.2004.03.007_BIB11) 2001; 18
Hoodless (10.1016/j.cyto.2004.03.007_BIB28) 1996; 85
Franzen (10.1016/j.cyto.2004.03.007_BIB20) 1993; 75
McPherron (10.1016/j.cyto.2004.03.007_BIB8) 1997; 94
Rebbapragada (10.1016/j.cyto.2004.03.007_BIB15) 2003; 2003
Liu (10.1016/j.cyto.2004.03.007_BIB29) 1996; 381
Roberts (10.1016/j.cyto.2004.03.007_BIB18) 2002; 13
Hill (10.1016/j.cyto.2004.03.007_BIB14) 2003; 17
Ishisaki (10.1016/j.cyto.2004.03.007_BIB33) 1999; 274
Sarkar (10.1016/j.cyto.2004.03.007_BIB44) 1990; 8
Kambadur (10.1016/j.cyto.2004.03.007_BIB6) 1997; 7
Lin (10.1016/j.cyto.2004.03.007_BIB5) 2002; 291
Attisano (10.1016/j.cyto.2004.03.007_BIB27) 2000; 12
Rosendahl (10.1016/j.cyto.2004.03.007_BIB23) 2001; 25
McPherron (10.1016/j.cyto.2004.03.007_BIB2) 2002; 109
Suzuki (10.1016/j.cyto.2004.03.007_BIB42) 2002; 277
Wozney (10.1016/j.cyto.2004.03.007_BIB10) 1988; 242
Lee (10.1016/j.cyto.2004.03.007_BIB12) 2001; 98
Zhang (10.1016/j.cyto.2004.03.007_BIB17) 1999; 9
Grobet (10.1016/j.cyto.2004.03.007_BIB7) 1997; 17
Nagarajan (10.1016/j.cyto.2004.03.007_BIB38) 1999; 274
References_xml – volume: 75
  start-page: 681
  year: 1993
  end-page: 692
  ident: BIB20
  article-title: Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor
  publication-title: Cell
– volume: 1
  start-page: 1001
  year: 2001
  end-page: 1013
  ident: BIB3
  article-title: Review of myostatin history, physiology and applications
  publication-title: LifeXY
– volume: 19
  start-page: 1745
  year: 2000
  end-page: 1754
  ident: BIB19
  article-title: Transcriptional control by the TGF-beta/Smad signaling system
  publication-title: EMBO J
– volume: 16
  start-page: 5353
  year: 1997
  end-page: 5362
  ident: BIB22
  article-title: TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4
  publication-title: EMBO J
– volume: 93
  start-page: 12992
  year: 1996
  end-page: 12997
  ident: BIB32
  article-title: Regulation of transforming growth factor beta- and activin-induced transcription by mammalian Mad proteins
  publication-title: Proc Natl Acad Sci U S A
– volume: 12
  start-page: 186
  year: 1998
  end-page: 197
  ident: BIB34
  article-title: Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor
  publication-title: Genes Dev
– volume: 291
  start-page: 701
  year: 2002
  end-page: 706
  ident: BIB5
  article-title: Myostatin knockout in mice increases myogenesis and decreases adipogenesis
  publication-title: Biochem Biophys Res Commun
– volume: 275
  start-page: 11320
  year: 2000
  end-page: 11326
  ident: BIB39
  article-title: Smad3 and Smad4 mediate transcriptional activation of the human Smad7 promoter by transforming growth factor beta
  publication-title: J Biol Chem
– volume: 94
  start-page: 12457
  year: 1997
  end-page: 12461
  ident: BIB8
  article-title: Double muscling in cattle due to mutations in the myostatin gene
  publication-title: Proc Natl Acad Sci U S A
– volume: 296
  start-page: 1486
  year: 2002
  end-page: 1488
  ident: BIB4
  article-title: Induction of cachexia in mice by systemically administered myostatin
  publication-title: Science
– volume: 17
  start-page: 71
  year: 1997
  end-page: 74
  ident: BIB7
  article-title: A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle
  publication-title: Nat Genet
– volume: 80
  start-page: 605
  year: 2002
  end-page: 622
  ident: BIB16
  article-title: TGF-beta and the Smad signal transduction pathway
  publication-title: Biochem Cell Biol
– volume: 98
  start-page: 9306
  year: 2001
  end-page: 9311
  ident: BIB12
  article-title: Regulation of myostatin activity and muscle growth
  publication-title: Proc Natl Acad Sci U S A
– volume: 89
  start-page: 1165
  year: 1997
  end-page: 1173
  ident: BIB37
  article-title: The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling
  publication-title: Cell
– volume: 95
  start-page: 737
  year: 1998
  end-page: 740
  ident: BIB26
  article-title: Smads: transcriptional activators of TGF-beta responses
  publication-title: Cell
– volume: 1
  start-page: 1265
  year: 1999
  end-page: 1273
  ident: BIB21
  article-title: TGF-beta signaling from receptors to the nucleus
  publication-title: Microbes Infect
– volume: 278
  start-page: 10716
  year: 2003
  end-page: 10721
  ident: BIB43
  article-title: Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-beta signaling by Smad7
  publication-title: J Biol Chem
– volume: 17
  start-page: 1144
  year: 2003
  end-page: 1154
  ident: BIB14
  article-title: Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: a novel protein with protease inhibitor and follistatin domains
  publication-title: Mol Endocrinol
– volume: 275
  start-page: 29308
  year: 2000
  end-page: 29317
  ident: BIB40
  article-title: Participation of Smad2, Smad3, and Smad4 in transforming growth factor beta (TGF-beta)-induced activation of Smad7. The TGF-beta response element of the promoter requires functional Smad binding element and E-box sequences for transcriptional regulation
  publication-title: J Biol Chem
– volume: 13
  start-page: 3
  year: 2002
  end-page: 5
  ident: BIB18
  article-title: The ever-increasing complexity of TGF-beta signaling
  publication-title: Cytokine Growth Factor Rev
– volume: 389
  start-page: 622
  year: 1997
  end-page: 626
  ident: BIB30
  article-title: Smad6 inhibits signalling by the TGF-beta superfamily
  publication-title: Nature
– volume: 9
  start-page: 274
  year: 1999
  end-page: 279
  ident: BIB17
  article-title: Regulation of Smad signalling by protein associations and signalling crosstalk
  publication-title: Trends Cell Biol
– volume: 2003
  start-page: 7230
  year: 2003
  end-page: 7242
  ident: BIB15
  article-title: Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis
  publication-title: Mol Cell Biol
– volume: 109
  start-page: 595
  year: 2002
  end-page: 601
  ident: BIB2
  article-title: Suppression of body fat accumulation in myostatin-deficient mice
  publication-title: J Clin Invest
– volume: 85
  start-page: 489
  year: 1996
  end-page: 500
  ident: BIB28
  article-title: MADR1, a MAD-related protein that functions in BMP2 signaling pathways
  publication-title: Cell
– volume: 381
  start-page: 620
  year: 1996
  end-page: 623
  ident: BIB29
  article-title: A human Mad protein acting as a BMP-regulated transcriptional activator
  publication-title: Nature
– volume: 12
  start-page: 235
  year: 2000
  end-page: 243
  ident: BIB27
  article-title: Smads as transcriptional co-modulators
  publication-title: Curr Opin Cell Biol
– volume: 17
  start-page: 3091
  year: 1998
  end-page: 3100
  ident: BIB24
  article-title: Direct binding of Smad3 and Smad4 to critical TGF beta-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene
  publication-title: EMBO J
– volume: 19
  start-page: 5178
  year: 2000
  end-page: 5193
  ident: BIB25
  article-title: Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15(Ink4B) transcription in response to TGF-beta
  publication-title: EMBO J
– volume: 277
  start-page: 39919
  year: 2002
  end-page: 39925
  ident: BIB42
  article-title: Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane
  publication-title: J Biol Chem
– volume: 275
  start-page: 23992
  year: 2000
  end-page: 23997
  ident: BIB31
  article-title: Smad7 and Smad6 differentially modulate transforming growth factor beta -induced inhibition of embryonic lung morphogenesis
  publication-title: J Biol Chem
– volume: 389
  start-page: 631
  year: 1997
  end-page: 635
  ident: BIB35
  article-title: Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling
  publication-title: Nature
– volume: 274
  start-page: 33412
  year: 1999
  end-page: 33418
  ident: BIB38
  article-title: Regulation of Smad7 promoter by direct association with Smad3 and Smad4
  publication-title: J Biol Chem
– volume: 8
  start-page: 404
  year: 1990
  end-page: 407
  ident: BIB44
  article-title: The “megaprimer” method of site-directed mutagenesis
  publication-title: Biotechniques
– volume: 242
  start-page: 1528
  year: 1988
  end-page: 1534
  ident: BIB10
  article-title: Novel regulators of bone formation: molecular clones and activities
  publication-title: Science
– volume: 7
  start-page: 910
  year: 1997
  end-page: 916
  ident: BIB6
  article-title: Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle
  publication-title: Genome Res
– volume: 277
  start-page: 40735
  year: 2002
  end-page: 40741
  ident: BIB13
  article-title: The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum
  publication-title: J Biol Chem
– volume: 316
  start-page: 701
  year: 1985
  end-page: 705
  ident: BIB9
  article-title: Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells
  publication-title: Nature
– volume: 273
  start-page: 24293
  year: 1998
  end-page: 24296
  ident: BIB36
  article-title: Smad7 is an activin-inducible inhibitor of activin-induced growth arrest and apoptosis in mouse B cells
  publication-title: J Biol Chem
– volume: 18
  start-page: 251
  year: 2001
  end-page: 259
  ident: BIB11
  article-title: GDF-8 propeptide binds to GDF-8 and antagonizes biological activity by inhibiting GDF-8 receptor binding
  publication-title: Growth Factors
– volume: 274
  start-page: 13637
  year: 1999
  end-page: 13642
  ident: BIB33
  article-title: Differential inhibition of Smad6 and Smad7 on bone morphogenetic protein- and activin-mediated growth arrest and apoptosis in B cells
  publication-title: J Biol Chem
– volume: 275
  start-page: 29023
  year: 2000
  end-page: 29030
  ident: BIB41
  article-title: Efficient TGF-beta induction of the Smad7 gene requires cooperation between AP-1, Sp1, and Smad proteins on the mouse Smad7 promoter
  publication-title: J Biol Chem
– volume: 25
  start-page: 60
  year: 2001
  end-page: 68
  ident: BIB23
  article-title: Activation of the TGF-beta/activin-Smad2 pathway during allergic airway inflammation
  publication-title: Am J Respir Cell Mol Biol
– volume: 387
  start-page: 83
  year: 1997
  end-page: 90
  ident: BIB1
  article-title: Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
  publication-title: Nature
– volume: 316
  start-page: 701
  year: 1985
  ident: 10.1016/j.cyto.2004.03.007_BIB9
  article-title: Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells
  publication-title: Nature
  doi: 10.1038/316701a0
– volume: 291
  start-page: 701
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB5
  article-title: Myostatin knockout in mice increases myogenesis and decreases adipogenesis
  publication-title: Biochem Biophys Res Commun
  doi: 10.1006/bbrc.2002.6500
– volume: 85
  start-page: 489
  year: 1996
  ident: 10.1016/j.cyto.2004.03.007_BIB28
  article-title: MADR1, a MAD-related protein that functions in BMP2 signaling pathways
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81250-7
– volume: 8
  start-page: 404
  year: 1990
  ident: 10.1016/j.cyto.2004.03.007_BIB44
  article-title: The “megaprimer” method of site-directed mutagenesis
  publication-title: Biotechniques
– volume: 18
  start-page: 251
  year: 2001
  ident: 10.1016/j.cyto.2004.03.007_BIB11
  article-title: GDF-8 propeptide binds to GDF-8 and antagonizes biological activity by inhibiting GDF-8 receptor binding
  publication-title: Growth Factors
  doi: 10.3109/08977190109029114
– volume: 2003
  start-page: 7230
  issue: 20
  year: 2003
  ident: 10.1016/j.cyto.2004.03.007_BIB15
  article-title: Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis
  publication-title: Mol Cell Biol
  doi: 10.1128/MCB.23.20.7230-7242.2003
– volume: 389
  start-page: 622
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB30
  article-title: Smad6 inhibits signalling by the TGF-beta superfamily
  publication-title: Nature
  doi: 10.1038/39355
– volume: 17
  start-page: 71
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB7
  article-title: A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle
  publication-title: Nat Genet
  doi: 10.1038/ng0997-71
– volume: 278
  start-page: 10716
  year: 2003
  ident: 10.1016/j.cyto.2004.03.007_BIB43
  article-title: Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-beta signaling by Smad7
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M212663200
– volume: 1
  start-page: 1001
  year: 2001
  ident: 10.1016/j.cyto.2004.03.007_BIB3
  article-title: Review of myostatin history, physiology and applications
  publication-title: LifeXY
– volume: 242
  start-page: 1528
  year: 1988
  ident: 10.1016/j.cyto.2004.03.007_BIB10
  article-title: Novel regulators of bone formation: molecular clones and activities
  publication-title: Science
  doi: 10.1126/science.3201241
– volume: 9
  start-page: 274
  year: 1999
  ident: 10.1016/j.cyto.2004.03.007_BIB17
  article-title: Regulation of Smad signalling by protein associations and signalling crosstalk
  publication-title: Trends Cell Biol
  doi: 10.1016/S0962-8924(99)01579-2
– volume: 13
  start-page: 3
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB18
  article-title: The ever-increasing complexity of TGF-beta signaling
  publication-title: Cytokine Growth Factor Rev
  doi: 10.1016/S1359-6101(01)00027-2
– volume: 274
  start-page: 33412
  year: 1999
  ident: 10.1016/j.cyto.2004.03.007_BIB38
  article-title: Regulation of Smad7 promoter by direct association with Smad3 and Smad4
  publication-title: J Biol Chem
  doi: 10.1074/jbc.274.47.33412
– volume: 7
  start-page: 910
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB6
  article-title: Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle
  publication-title: Genome Res
  doi: 10.1101/gr.7.9.910
– volume: 109
  start-page: 595
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB2
  article-title: Suppression of body fat accumulation in myostatin-deficient mice
  publication-title: J Clin Invest
  doi: 10.1172/JCI0213562
– volume: 389
  start-page: 631
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB35
  article-title: Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling
  publication-title: Nature
  doi: 10.1038/39369
– volume: 12
  start-page: 235
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB27
  article-title: Smads as transcriptional co-modulators
  publication-title: Curr Opin Cell Biol
  doi: 10.1016/S0955-0674(99)00081-2
– volume: 19
  start-page: 1745
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB19
  article-title: Transcriptional control by the TGF-beta/Smad signaling system
  publication-title: EMBO J
  doi: 10.1093/emboj/19.8.1745
– volume: 275
  start-page: 29308
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB40
  article-title: Participation of Smad2, Smad3, and Smad4 in transforming growth factor beta (TGF-beta)-induced activation of Smad7. The TGF-beta response element of the promoter requires functional Smad binding element and E-box sequences for transcriptional regulation
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M003282200
– volume: 296
  start-page: 1486
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB4
  article-title: Induction of cachexia in mice by systemically administered myostatin
  publication-title: Science
  doi: 10.1126/science.1069525
– volume: 275
  start-page: 11320
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB39
  article-title: Smad3 and Smad4 mediate transcriptional activation of the human Smad7 promoter by transforming growth factor beta
  publication-title: J Biol Chem
  doi: 10.1074/jbc.275.15.11320
– volume: 80
  start-page: 605
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB16
  article-title: TGF-beta and the Smad signal transduction pathway
  publication-title: Biochem Cell Biol
  doi: 10.1139/o02-161
– volume: 17
  start-page: 1144
  year: 2003
  ident: 10.1016/j.cyto.2004.03.007_BIB14
  article-title: Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: a novel protein with protease inhibitor and follistatin domains
  publication-title: Mol Endocrinol
  doi: 10.1210/me.2002-0366
– volume: 381
  start-page: 620
  year: 1996
  ident: 10.1016/j.cyto.2004.03.007_BIB29
  article-title: A human Mad protein acting as a BMP-regulated transcriptional activator
  publication-title: Nature
  doi: 10.1038/381620a0
– volume: 75
  start-page: 681
  year: 1993
  ident: 10.1016/j.cyto.2004.03.007_BIB20
  article-title: Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor
  publication-title: Cell
  doi: 10.1016/0092-8674(93)90489-D
– volume: 1
  start-page: 1265
  year: 1999
  ident: 10.1016/j.cyto.2004.03.007_BIB21
  article-title: TGF-beta signaling from receptors to the nucleus
  publication-title: Microbes Infect
  doi: 10.1016/S1286-4579(99)00258-0
– volume: 274
  start-page: 13637
  year: 1999
  ident: 10.1016/j.cyto.2004.03.007_BIB33
  article-title: Differential inhibition of Smad6 and Smad7 on bone morphogenetic protein- and activin-mediated growth arrest and apoptosis in B cells
  publication-title: J Biol Chem
  doi: 10.1074/jbc.274.19.13637
– volume: 273
  start-page: 24293
  year: 1998
  ident: 10.1016/j.cyto.2004.03.007_BIB36
  article-title: Smad7 is an activin-inducible inhibitor of activin-induced growth arrest and apoptosis in mouse B cells
  publication-title: J Biol Chem
  doi: 10.1074/jbc.273.38.24293
– volume: 277
  start-page: 40735
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB13
  article-title: The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M206379200
– volume: 12
  start-page: 186
  year: 1998
  ident: 10.1016/j.cyto.2004.03.007_BIB34
  article-title: Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor
  publication-title: Genes Dev
  doi: 10.1101/gad.12.2.186
– volume: 387
  start-page: 83
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB1
  article-title: Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
  publication-title: Nature
  doi: 10.1038/387083a0
– volume: 17
  start-page: 3091
  year: 1998
  ident: 10.1016/j.cyto.2004.03.007_BIB24
  article-title: Direct binding of Smad3 and Smad4 to critical TGF beta-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene
  publication-title: EMBO J
  doi: 10.1093/emboj/17.11.3091
– volume: 93
  start-page: 12992
  year: 1996
  ident: 10.1016/j.cyto.2004.03.007_BIB32
  article-title: Regulation of transforming growth factor beta- and activin-induced transcription by mammalian Mad proteins
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.93.23.12992
– volume: 89
  start-page: 1165
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB37
  article-title: The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80303-7
– volume: 16
  start-page: 5353
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB22
  article-title: TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4
  publication-title: EMBO J
  doi: 10.1093/emboj/16.17.5353
– volume: 95
  start-page: 737
  year: 1998
  ident: 10.1016/j.cyto.2004.03.007_BIB26
  article-title: Smads: transcriptional activators of TGF-beta responses
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81696-7
– volume: 275
  start-page: 23992
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB31
  article-title: Smad7 and Smad6 differentially modulate transforming growth factor beta -induced inhibition of embryonic lung morphogenesis
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M002433200
– volume: 98
  start-page: 9306
  year: 2001
  ident: 10.1016/j.cyto.2004.03.007_BIB12
  article-title: Regulation of myostatin activity and muscle growth
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.151270098
– volume: 94
  start-page: 12457
  year: 1997
  ident: 10.1016/j.cyto.2004.03.007_BIB8
  article-title: Double muscling in cattle due to mutations in the myostatin gene
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.94.23.12457
– volume: 25
  start-page: 60
  year: 2001
  ident: 10.1016/j.cyto.2004.03.007_BIB23
  article-title: Activation of the TGF-beta/activin-Smad2 pathway during allergic airway inflammation
  publication-title: Am J Respir Cell Mol Biol
  doi: 10.1165/ajrcmb.25.1.4396
– volume: 19
  start-page: 5178
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB25
  article-title: Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15(Ink4B) transcription in response to TGF-beta
  publication-title: EMBO J
  doi: 10.1093/emboj/19.19.5178
– volume: 275
  start-page: 29023
  year: 2000
  ident: 10.1016/j.cyto.2004.03.007_BIB41
  article-title: Efficient TGF-beta induction of the Smad7 gene requires cooperation between AP-1, Sp1, and Smad proteins on the mouse Smad7 promoter
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M002815200
– volume: 277
  start-page: 39919
  year: 2002
  ident: 10.1016/j.cyto.2004.03.007_BIB42
  article-title: Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M201901200
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Snippet As a member of the TGF-β superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the...
As a member of the TGF-b superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the...
As a member of the TGF-beta superfamily, myostatin is a specific negative regulator of skeletal muscle mass. To identify the downstream components in the...
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SubjectTerms Myostatin
Smad proteins
TGF-β
Title Myostatin signaling through Smad2, Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism
URI https://dx.doi.org/10.1016/j.cyto.2004.03.007
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