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Volumn 586, Issue 14, 2012, Pages 1871-1884

Post-translational regulation of TGF-β receptor and Smad signaling

Author keywords

Acetylation; ADP ribosylation; Ectodomain shedding; miRNA; Nucleocytoplasmic shuttling; Phosphorylation; Post translational modification; Receptor kinase; Signal transduction; Signaling crosstalk; Smad; Sumoylation; Transforming growth factor ; Ubiquitylation

Indexed keywords

CELL SURFACE RECEPTOR; MESSENGER RNA; MICRORNA; RECEPTOR REGULATED SMAD PROTEIN; SMAD PROTEIN; SMAD7 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 1; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 2; TRANSFORMING GROWTH FACTOR BETA1; TRANSFORMING GROWTH FACTOR BETA2; TRANSFORMING GROWTH FACTOR BETA3;

EID: 84862765059     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.05.010     Document Type: Review
Times cited : (176)

References (201)
  • 1
    • 44449085619 scopus 로고    scopus 로고
    • TGF-β and the TGF-β Family
    • R. Derynck, K. Miyazono, Cold Spring Harbor Laboratory Press
    • R. Derynck, and K. Miyazono TGF-β and the TGF-β Family R. Derynck, K. Miyazono, The TGF-β Family 2008 Cold Spring Harbor Laboratory Press 29 44
    • (2008) The TGF-β Family , pp. 29-44
    • Derynck, R.1    Miyazono, K.2
  • 3
    • 0029959774 scopus 로고    scopus 로고
    • Phosphorylation of Ser165 in TGF-β type i receptor modulates TGF-β1-induced cellular responses
    • S. Souchelnytskyi, P. ten Dijke, K. Miyazono, and C.H. Heldin Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses EMBO J. 15 1996 6231 6240
    • (1996) EMBO J. , vol.15 , pp. 6231-6240
    • Souchelnytskyi, S.1    Ten Dijke, P.2    Miyazono, K.3    Heldin, C.H.4
  • 4
    • 0034796457 scopus 로고    scopus 로고
    • The TGF β receptor activation process: An inhibitor- to substrate-binding switch
    • M. Huse, T.W. Muir, L. Xu, Y.G. Chen, J. Kuriyan, and J. Massague The TGF β receptor activation process: an inhibitor- to substrate-binding switch Mol. Cell 8 2001 671 682
    • (2001) Mol. Cell , vol.8 , pp. 671-682
    • Huse, M.1    Muir, T.W.2    Xu, L.3    Chen, Y.G.4    Kuriyan, J.5    Massague, J.6
  • 5
    • 0030926004 scopus 로고    scopus 로고
    • Mechanism of TGFβ receptor inhibition by FKBP12
    • Y.G. Chen, F. Liu, and J. Massague Mechanism of TGFβ receptor inhibition by FKBP12 EMBO J. 16 1997 3866 3876
    • (1997) EMBO J. , vol.16 , pp. 3866-3876
    • Chen, Y.G.1    Liu, F.2    Massague, J.3
  • 6
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Y. Shi, and J. Massague Mechanisms of TGF-β signaling from cell membrane to the nucleus Cell 113 2003 685 700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 8
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-β family signalling
    • R. Derynck, and Y.E. Zhang Smad-dependent and Smad-independent pathways in TGF-β family signalling Nature 425 2003 577 584
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 10
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in TGF-β signaling through Smads
    • X.H. Feng, and R. Derynck Specificity and versatility in TGF-β signaling through Smads Annu. Rev. Cell Dev. Biol. 21 2005 659 693
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 659-693
    • Feng, X.H.1    Derynck, R.2
  • 11
    • 61849099472 scopus 로고    scopus 로고
    • TGF-β Bioavailability: Latency, Targeting, and Activation
    • Derynck R. and Miyazono K. eds. Cold Spring Harbor Laboratory Press
    • Dabovic, B., and Rifkin, D. B. (2008) TGF-β Bioavailability: Latency, Targeting, and Activation. The TGF-β Family. Derynck R. and Miyazono K. eds. Cold Spring Harbor Laboratory Press, 179-202.
    • (2008) The TGF-β Family , pp. 179-202
    • Dabovic, B.1    Rifkin, D.B.2
  • 12
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFβ activation
    • J.P. Annes, J.S. Munger, and D.B. Rifkin Making sense of latent TGFβ activation J. Cell Sci. 116 2003 217 224
    • (2003) J. Cell Sci. , vol.116 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 13
    • 49049110677 scopus 로고    scopus 로고
    • Integrins and the activation of latent transforming growth factor β1 - An intimate relationship
    • P.J. Wipff, and B. Hinz Integrins and the activation of latent transforming growth factor β1 - an intimate relationship Eur. J. Cell Biol. 87 2008 601 615
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 601-615
    • Wipff, P.J.1    Hinz, B.2
  • 14
    • 33947265169 scopus 로고    scopus 로고
    • Absence of integrin-mediated TGFβ1 activation in vivo recapitulates the phenotype of TGFβ1-null mice
    • Z. Yang, Z. Mu, B. Dabovic, V. Jurukovski, D. Yu, J. Sung, X. Xiong, and J.S. Munger Absence of integrin-mediated TGFβ1 activation in vivo recapitulates the phenotype of TGFβ1-null mice J. Cell. Biol. 176 2007 787 793
    • (2007) J. Cell. Biol. , vol.176 , pp. 787-793
    • Yang, Z.1    Mu, Z.2    Dabovic, B.3    Jurukovski, V.4    Yu, D.5    Sung, J.6    Xiong, X.7    Munger, J.S.8
  • 16
    • 78649807601 scopus 로고    scopus 로고
    • Expression of αvβ8 integrin on dendritic cells regulates Th17 cell development and experimental autoimmune encephalomyelitis in mice
    • A.C. Melton, S.L. Bailey-Bucktrout, M.A. Travis, B.T. Fife, J.A. Bluestone, and D. Sheppard Expression of αvβ8 integrin on dendritic cells regulates Th17 cell development and experimental autoimmune encephalomyelitis in mice J. Clin. Invest. 120 2010 4436 4444
    • (2010) J. Clin. Invest. , vol.120 , pp. 4436-4444
    • Melton, A.C.1    Bailey-Bucktrout, S.L.2    Travis, M.A.3    Fife, B.T.4    Bluestone, J.A.5    Sheppard, D.6
  • 18
    • 2942653435 scopus 로고    scopus 로고
    • Integrin αvβ6-mediated activation of latent TGF-β requires the latent TGF-β binding protein-1
    • J.P. Annes, Y. Chen, J.S. Munger, and D.B. Rifkin Integrin αVβ6-mediated activation of latent TGF-β requires the latent TGF-β binding protein-1 J. Cell. Biol. 165 2004 723 734
    • (2004) J. Cell. Biol. , vol.165 , pp. 723-734
    • Annes, J.P.1    Chen, Y.2    Munger, J.S.3    Rifkin, D.B.4
  • 19
    • 37249044357 scopus 로고    scopus 로고
    • Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix
    • P.J. Wipff, D.B. Rifkin, J.J. Meister, and B. Hinz Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix J. Cell. Biol. 179 2007 1311 1323
    • (2007) J. Cell. Biol. , vol.179 , pp. 1311-1323
    • Wipff, P.J.1    Rifkin, D.B.2    Meister, J.J.3    Hinz, B.4
  • 20
    • 55749109860 scopus 로고    scopus 로고
    • In vitro and in vivo evidence for shear-induced activation of latent transforming growth factor-β1
    • J. Ahamed, N. Burg, K. Yoshinaga, C.A. Janczak, D.B. Rifkin, and B.S. Coller In vitro and in vivo evidence for shear-induced activation of latent transforming growth factor-β1 Blood 112 2008 3650 3660
    • (2008) Blood , vol.112 , pp. 3650-3660
    • Ahamed, J.1    Burg, N.2    Yoshinaga, K.3    Janczak, C.A.4    Rifkin, D.B.5    Coller, B.S.6
  • 21
    • 0347444723 scopus 로고    scopus 로고
    • MicroRNAs: Genomics, biogenesis, mechanism, and function
    • D.P. Bartel MicroRNAs: genomics, biogenesis, mechanism, and function Cell 116 2004 281 297
    • (2004) Cell , vol.116 , pp. 281-297
    • Bartel, D.P.1
  • 25
    • 79955780736 scopus 로고    scopus 로고
    • Multiple targets of miR-302 and miR-372 promote reprogramming of human fibroblasts to induced pluripotent stem cells
    • D. Subramanyam, S. Lamouille, R.L. Judson, J.Y. Liu, N. Bucay, R. Derynck, and R. Blelloch Multiple targets of miR-302 and miR-372 promote reprogramming of human fibroblasts to induced pluripotent stem cells Nat. Biotechnol. 29 2011 443 448
    • (2011) Nat. Biotechnol. , vol.29 , pp. 443-448
    • Subramanyam, D.1    Lamouille, S.2    Judson, R.L.3    Liu, J.Y.4    Bucay, N.5    Derynck, R.6    Blelloch, R.7
  • 26
  • 28
    • 67650225263 scopus 로고    scopus 로고
    • Essential role of TGF-β signaling in glucose-induced cell hypertrophy
    • L. Wu, and R. Derynck Essential role of TGF-β signaling in glucose-induced cell hypertrophy Dev. Cell 17 2009 35 48
    • (2009) Dev. Cell , vol.17 , pp. 35-48
    • Wu, L.1    Derynck, R.2
  • 29
    • 67649664111 scopus 로고    scopus 로고
    • TACE-mediated ectodomain shedding of the type i TGF-β receptor downregulates TGF-β signaling
    • C. Liu, P. Xu, S. Lamouille, J. Xu, and R. Derynck TACE-mediated ectodomain shedding of the type I TGF-β receptor downregulates TGF-β signaling Mol. Cell 35 2009 26 36
    • (2009) Mol. Cell , vol.35 , pp. 26-36
    • Liu, C.1    Xu, P.2    Lamouille, S.3    Xu, J.4    Derynck, R.5
  • 31
    • 76849107016 scopus 로고    scopus 로고
    • Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation
    • P. Xu, and R. Derynck Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation Mol. Cell 37 2010 551 566
    • (2010) Mol. Cell , vol.37 , pp. 551-566
    • Xu, P.1    Derynck, R.2
  • 33
    • 68549123472 scopus 로고    scopus 로고
    • New regulatory mechanisms of TGF-β receptor function
    • J.S. Kang, C. Liu, and R. Derynck New regulatory mechanisms of TGF-β receptor function Trends Cell Biol. 19 2009 385 394
    • (2009) Trends Cell Biol. , vol.19 , pp. 385-394
    • Kang, J.S.1    Liu, C.2    Derynck, R.3
  • 34
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • S.K. Hanks, and T. Hunter Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification Faseb J. 9 1995 576 596
    • (1995) Faseb J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 36
    • 0030978105 scopus 로고    scopus 로고
    • The type II transforming growth factor-β receptor autophosphorylates not only on serine and threonine but also on tyrosine residues
    • S. Lawler, X.H. Feng, R.H. Chen, E.M. Maruoka, C.W. Turck, I. Griswold-Prenner, and R. Derynck The type II transforming growth factor-β receptor autophosphorylates not only on serine and threonine but also on tyrosine residues J. Biol. Chem. 272 1997 14850 14859
    • (1997) J. Biol. Chem. , vol.272 , pp. 14850-14859
    • Lawler, S.1    Feng, X.H.2    Chen, R.H.3    Maruoka, E.M.4    Turck, C.W.5    Griswold-Prenner, I.6    Derynck, R.7
  • 37
    • 34248584887 scopus 로고    scopus 로고
    • Src phosphorylates Tyr284 in TGF-β type II receptor and regulates TGF-β stimulation of p38 MAPK during breast cancer cell proliferation and invasion
    • A.J. Galliher, and W.P. Schiemann Src phosphorylates Tyr284 in TGF-β type II receptor and regulates TGF-β stimulation of p38 MAPK during breast cancer cell proliferation and invasion Cancer Res. 67 2007 3752 3758
    • (2007) Cancer Res. , vol.67 , pp. 3752-3758
    • Galliher, A.J.1    Schiemann, W.P.2
  • 39
    • 58149239730 scopus 로고    scopus 로고
    • Phospho-control of TGF-β superfamily signaling
    • K.H. Wrighton, X. Lin, and X.H. Feng Phospho-control of TGF-β superfamily signaling Cell Res. 19 2009 8 20
    • (2009) Cell Res. , vol.19 , pp. 8-20
    • Wrighton, K.H.1    Lin, X.2    Feng, X.H.3
  • 40
    • 1642539976 scopus 로고    scopus 로고
    • GADD34-PP1c recruited by Smad7 dephosphorylates TGFβ type i receptor
    • W. Shi, C. Sun, B. He, W. Xiong, X. Shi, D. Yao, and X. Cao GADD34-PP1c recruited by Smad7 dephosphorylates TGFβ type I receptor J. Cell. Biol. 164 2004 291 300
    • (2004) J. Cell. Biol. , vol.164 , pp. 291-300
    • Shi, W.1    Sun, C.2    He, B.3    Xiong, W.4    Shi, X.5    Yao, D.6    Cao, X.7
  • 41
    • 0036699073 scopus 로고    scopus 로고
    • PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster
    • D. Bennett, and L. Alphey PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster Nat. Genet. 31 2002 419 423
    • (2002) Nat. Genet. , vol.31 , pp. 419-423
    • Bennett, D.1    Alphey, L.2
  • 42
    • 53349156578 scopus 로고    scopus 로고
    • Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling
    • J. Batut, B. Schmierer, J. Cao, L.A. Raftery, C.S. Hill, and M. Howell Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling Development 135 2008 2927 2937
    • (2008) Development , vol.135 , pp. 2927-2937
    • Batut, J.1    Schmierer, B.2    Cao, J.3    Raftery, L.A.4    Hill, C.S.5    Howell, M.6
  • 43
    • 0031741865 scopus 로고    scopus 로고
    • Physical and functional interactions between type i transforming growth factor β receptors and Bα, a WD-40 repeat subunit of phosphatase 2A
    • I. Griswold-Prenner, C. Kamibayashi, E.M. Maruoka, M.C. Mumby, and R. Derynck Physical and functional interactions between type I transforming growth factor β receptors and Bα, a WD-40 repeat subunit of phosphatase 2A Mol. Cell Biol. 18 1998 6595 6604
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6595-6604
    • Griswold-Prenner, I.1    Kamibayashi, C.2    Maruoka, E.M.3    Mumby, M.C.4    Derynck, R.5
  • 45
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF β receptor for degradation
    • P. Kavsak, R.K. Rasmussen, C.G. Causing, S. Bonni, H. Zhu, G.H. Thomsen, and J.L. Wrana Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF β receptor for degradation Mol. Cell 6 2000 1365 1375
    • (2000) Mol. Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6    Wrana, J.L.7
  • 47
    • 15944370597 scopus 로고    scopus 로고
    • NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-β (transforming growth factor-β) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-β type i receptor
    • G. Kuratomi, A. Komuro, K. Goto, M. Shinozaki, K. Miyazawa, K. Miyazono, and T. Imamura NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-β (transforming growth factor-β) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-β type I receptor Biochem. J. 386 2005 461 470
    • (2005) Biochem. J. , vol.386 , pp. 461-470
    • Kuratomi, G.1    Komuro, A.2    Goto, K.3    Shinozaki, M.4    Miyazawa, K.5    Miyazono, K.6    Imamura, T.7
  • 48
    • 4644312604 scopus 로고    scopus 로고
    • Negative regulation of transforming growth factor-β (TGF-β) signaling by WW domain-containing protein 1 (WWP1)
    • A. Komuro, T. Imamura, M. Saitoh, Y. Yoshida, T. Yamori, K. Miyazono, and K. Miyazawa Negative regulation of transforming growth factor-β (TGF-β) signaling by WW domain-containing protein 1 (WWP1) Oncogene 23 2004 6914 6923
    • (2004) Oncogene , vol.23 , pp. 6914-6923
    • Komuro, A.1    Imamura, T.2    Saitoh, M.3    Yoshida, Y.4    Yamori, T.5    Miyazono, K.6    Miyazawa, K.7
  • 50
    • 27944498719 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signalling
    • S.J. Wicks, K. Haros, M. Maillard, L. Song, R.E. Cohen, P.T. Dijke, and A. Chantry The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signalling Oncogene 24 2005 8080 8084
    • (2005) Oncogene , vol.24 , pp. 8080-8084
    • Wicks, S.J.1    Haros, K.2    Maillard, M.3    Song, L.4    Cohen, R.E.5    Dijke, P.T.6    Chantry, A.7
  • 52
    • 44649163272 scopus 로고    scopus 로고
    • The type i TGF-β receptor is covalently modified and regulated by sumoylation
    • J.S. Kang, E.F. Saunier, R.J. Akhurst, and R. Derynck The type I TGF-β receptor is covalently modified and regulated by sumoylation Nat. Cell Biol. 10 2008 654 664
    • (2008) Nat. Cell Biol. , vol.10 , pp. 654-664
    • Kang, J.S.1    Saunier, E.F.2    Akhurst, R.J.3    Derynck, R.4
  • 53
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • C. Le Roy, and J.L. Wrana Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling Nat. Rev. Mol. Cell Biol. 6 2005 112 126
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 54
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
    • G.M. Di Guglielmo, C. Le Roy, A.F. Goodfellow, and J.L. Wrana Distinct endocytic pathways regulate TGF-β receptor signalling and turnover Nat. Cell Biol. 5 2003 410 421
    • (2003) Nat. Cell Biol. , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 55
    • 58149269185 scopus 로고    scopus 로고
    • Endocytic regulation of TGF-β signaling
    • Y.G. Chen Endocytic regulation of TGF-β signaling Cell Res. 19 2009 58 70
    • (2009) Cell Res. , vol.19 , pp. 58-70
    • Chen, Y.G.1
  • 56
    • 4344606636 scopus 로고    scopus 로고
    • Ligand-dependent and -independent transforming growth factor-β receptor recycling regulated by clathrin-mediated endocytosis and Rab11
    • H. Mitchell, A. Choudhury, R.E. Pagano, and E.B. Leof Ligand-dependent and -independent transforming growth factor-β receptor recycling regulated by clathrin-mediated endocytosis and Rab11 Mol. Biol. Cell. 15 2004 4166 4178
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 4166-4178
    • Mitchell, H.1    Choudhury, A.2    Pagano, R.E.3    Leof, E.B.4
  • 57
    • 1842832338 scopus 로고    scopus 로고
    • Transforming growth factor-β receptors interact with AP2 by direct binding to β2 subunit
    • D. Yao, M. Ehrlich, Y.I. Henis, and E.B. Leof Transforming growth factor-β receptors interact with AP2 by direct binding to β2 subunit Mol. Biol. Cell. 13 2002 4001 4012
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 4001-4012
    • Yao, D.1    Ehrlich, M.2    Henis, Y.I.3    Leof, E.B.4
  • 58
    • 0037144841 scopus 로고    scopus 로고
    • TGF β receptor internalization into EEA1-enriched early endosomes: Role in signaling to Smad2
    • S. Hayes, A. Chawla, and S. Corvera TGF β receptor internalization into EEA1-enriched early endosomes: role in signaling to Smad2 J. Cell. Biol. 158 2002 1239 1249
    • (2002) J. Cell. Biol. , vol.158 , pp. 1239-1249
    • Hayes, S.1    Chawla, A.2    Corvera, S.3
  • 59
    • 40749126837 scopus 로고    scopus 로고
    • Integration of transforming growth factor β and RAS signaling silences a RAB5 guanine nucleotide exchange factor and enhances growth factor-directed cell migration
    • H. Hu, M. Milstein, J.M. Bliss, M. Thai, G. Malhotra, L.C. Huynh, and J. Colicelli Integration of transforming growth factor β and RAS signaling silences a RAB5 guanine nucleotide exchange factor and enhances growth factor-directed cell migration Mol. Cell Biol. 28 2008 1573 1583
    • (2008) Mol. Cell Biol. , vol.28 , pp. 1573-1583
    • Hu, H.1    Milstein, M.2    Bliss, J.M.3    Thai, M.4    Malhotra, G.5    Huynh, L.C.6    Colicelli, J.7
  • 60
    • 0035794218 scopus 로고    scopus 로고
    • Caveolin-1 regulates transforming growth factor (TGF)-β/SMAD signaling through an interaction with the TGF-β type i receptor
    • B. Razani, X.L. Zhang, M. Bitzer, G. von Gersdorff, E.P. Bottinger, and M.P. Lisanti Caveolin-1 regulates transforming growth factor (TGF)-β/SMAD signaling through an interaction with the TGF-β type I receptor J. Biol. Chem. 276 2001 6727 6738
    • (2001) J. Biol. Chem. , vol.276 , pp. 6727-6738
    • Razani, B.1    Zhang, X.L.2    Bitzer, M.3    Von Gersdorff, G.4    Bottinger, E.P.5    Lisanti, M.P.6
  • 62
    • 64049102327 scopus 로고    scopus 로고
    • Specific activation of mitogen-activated protein kinase by transforming growth factor-β receptors in lipid rafts is required for epithelial cell plasticity
    • W. Zuo, and Y.G. Chen Specific activation of mitogen-activated protein kinase by transforming growth factor-β receptors in lipid rafts is required for epithelial cell plasticity Mol. Biol. Cell 20 2009 1020 1029
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1020-1029
    • Zuo, W.1    Chen, Y.G.2
  • 63
    • 65549146320 scopus 로고    scopus 로고
    • Control of transforming growth factor β signal transduction by small GTPases
    • D. Kardassis, C. Murphy, T. Fotsis, A. Moustakas, and C. Stournaras Control of transforming growth factor β signal transduction by small GTPases FEBS J. 276 2009 2947 2965
    • (2009) FEBS J. , vol.276 , pp. 2947-2965
    • Kardassis, D.1    Murphy, C.2    Fotsis, T.3    Moustakas, A.4    Stournaras, C.5
  • 64
    • 46249083539 scopus 로고    scopus 로고
    • Regulation of activin/nodal signaling by Rap2-directed receptor trafficking
    • S.C. Choi, G.H. Kim, S.J. Lee, E. Park, C.Y. Yeo, and J.K. Han Regulation of activin/nodal signaling by Rap2-directed receptor trafficking Dev. Cell 15 2008 49 61
    • (2008) Dev. Cell , vol.15 , pp. 49-61
    • Choi, S.C.1    Kim, G.H.2    Lee, S.J.3    Park, E.4    Yeo, C.Y.5    Han, J.K.6
  • 65
    • 84859437880 scopus 로고    scopus 로고
    • Role of Smads in TGFβ signaling
    • C.H. Heldin, and A. Moustakas Role of Smads in TGFβ signaling Cell Tissue Res. 347 2012 21 36
    • (2012) Cell Tissue Res. , vol.347 , pp. 21-36
    • Heldin, C.H.1    Moustakas, A.2
  • 66
    • 65649084845 scopus 로고    scopus 로고
    • Transforming growth factor-{β}-inducible phosphorylation of Smad3
    • G. Wang, I. Matsuura, D. He, and F. Liu Transforming growth factor-{β}-inducible phosphorylation of Smad3 J. Biol. Chem. 284 2009 9663 9673
    • (2009) J. Biol. Chem. , vol.284 , pp. 9663-9673
    • Wang, G.1    Matsuura, I.2    He, D.3    Liu, F.4
  • 67
    • 67749106488 scopus 로고    scopus 로고
    • A negative feedback control of transforming growth factor-β signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204
    • C. Millet, M. Yamashita, M. Heller, L.R. Yu, T.D. Veenstra, and Y.E. Zhang A negative feedback control of transforming growth factor-β signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204 J. Biol. Chem. 284 2009 19808 19816
    • (2009) J. Biol. Chem. , vol.284 , pp. 19808-19816
    • Millet, C.1    Yamashita, M.2    Heller, M.3    Yu, L.R.4    Veenstra, T.D.5    Zhang, Y.E.6
  • 73
    • 25144432973 scopus 로고    scopus 로고
    • The G protein-coupled receptor kinase-2 is a TGFβ-inducible antagonist of TGFβ signal transduction
    • J. Ho, E. Cocolakis, V.M. Dumas, B.I. Posner, S.A. Laporte, and J.J. Lebrun The G protein-coupled receptor kinase-2 is a TGFβ-inducible antagonist of TGFβ signal transduction EMBO J. 24 2005 3247 3258
    • (2005) EMBO J. , vol.24 , pp. 3247-3258
    • Ho, J.1    Cocolakis, E.2    Dumas, V.M.3    Posner, B.I.4    Laporte, S.A.5    Lebrun, J.J.6
  • 74
    • 38149054804 scopus 로고    scopus 로고
    • Axin and GSK3-control Smad3 protein stability and modulate TGF-signaling
    • X. Guo, A. Ramirez, D.S. Waddell, Z. Li, X. Liu, and X.F. Wang Axin and GSK3-control Smad3 protein stability and modulate TGF-signaling Genes Dev. 22 2008 106 120
    • (2008) Genes Dev. , vol.22 , pp. 106-120
    • Guo, X.1    Ramirez, A.2    Waddell, D.S.3    Li, Z.4    Liu, X.5    Wang, X.F.6
  • 75
    • 34547108860 scopus 로고    scopus 로고
    • Activation of Mps1 promotes transforming growth factor-β-independent Smad signaling
    • S. Zhu, W. Wang, D.C. Clarke, and X. Liu Activation of Mps1 promotes transforming growth factor-β-independent Smad signaling J. Biol. Chem. 282 2007 18327 18338
    • (2007) J. Biol. Chem. , vol.282 , pp. 18327-18338
    • Zhu, S.1    Wang, W.2    Clarke, D.C.3    Liu, X.4
  • 76
    • 34547099850 scopus 로고    scopus 로고
    • Biological cross-talk between WNK1 and the transforming growth factor β-Smad signaling pathway
    • B.H. Lee, W. Chen, S. Stippec, and M.H. Cobb Biological cross-talk between WNK1 and the transforming growth factor β-Smad signaling pathway J. Biol. Chem. 282 2007 17985 17996
    • (2007) J. Biol. Chem. , vol.282 , pp. 17985-17996
    • Lee, B.H.1    Chen, W.2    Stippec, S.3    Cobb, M.H.4
  • 77
    • 77957280982 scopus 로고    scopus 로고
    • Murine protein serine/threonine kinase 38 stimulates TGF-β signaling in a kinase-dependent manner via direct phosphorylation of Smad proteins
    • H.A. Seong, H. Jung, and H. Ha Murine protein serine/threonine kinase 38 stimulates TGF-β signaling in a kinase-dependent manner via direct phosphorylation of Smad proteins J. Biol. Chem. 285 2010 30959 30970
    • (2010) J. Biol. Chem. , vol.285 , pp. 30959-30970
    • Seong, H.A.1    Jung, H.2    Ha, H.3
  • 79
    • 50349102144 scopus 로고    scopus 로고
    • Opposite effects of dihydrosphingosine 1-phosphate and sphingosine 1-phosphate on transforming growth factor-β/Smad signaling are mediated through the PTEN/PPM1A-dependent pathway
    • S. Bu, B. Kapanadze, T. Hsu, and M. Trojanowska Opposite effects of dihydrosphingosine 1-phosphate and sphingosine 1-phosphate on transforming growth factor-β/Smad signaling are mediated through the PTEN/PPM1A-dependent pathway J. Biol. Chem. 283 2008 19593 19602
    • (2008) J. Biol. Chem. , vol.283 , pp. 19593-19602
    • Bu, S.1    Kapanadze, B.2    Hsu, T.3    Trojanowska, M.4
  • 80
    • 77950874802 scopus 로고    scopus 로고
    • MTMR4 attenuates transforming growth factor β (TGFβ) signaling by dephosphorylating R-Smads in endosomes
    • J. Yu, L. Pan, X. Qin, H. Chen, Y. Xu, Y. Chen, and H. Tang MTMR4 attenuates transforming growth factor β (TGFβ) signaling by dephosphorylating R-Smads in endosomes J. Biol. Chem. 285 2010 8454 8462
    • (2010) J. Biol. Chem. , vol.285 , pp. 8454-8462
    • Yu, J.1    Pan, L.2    Qin, X.3    Chen, H.4    Xu, Y.5    Chen, Y.6    Tang, H.7
  • 81
    • 33747044916 scopus 로고    scopus 로고
    • Unique players in the BMP pathway: Small C-terminal domain phosphatases dephosphorylate Smad1 to attenuate BMP signaling
    • M. Knockaert, G. Sapkota, C. Alarcon, J. Massague, and A.H. Brivanlou Unique players in the BMP pathway: small C-terminal domain phosphatases dephosphorylate Smad1 to attenuate BMP signaling Proc. Natl. Acad. Sci. U S A 103 2006 11940 11945
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 11940-11945
    • Knockaert, M.1    Sapkota, G.2    Alarcon, C.3    Massague, J.4    Brivanlou, A.H.5
  • 83
    • 67349250497 scopus 로고    scopus 로고
    • TGF-β signalling is regulated by Schnurri-2-dependent nuclear translocation of CLIC4 and consequent stabilization of phospho-Smad2 and 3
    • A. Shukla, M. Malik, C. Cataisson, Y. Ho, T. Friesen, K.S. Suh, and S.H. Yuspa TGF-β signalling is regulated by Schnurri-2-dependent nuclear translocation of CLIC4 and consequent stabilization of phospho-Smad2 and 3 Nat. Cell. Biol. 11 2009 777 784
    • (2009) Nat. Cell. Biol. , vol.11 , pp. 777-784
    • Shukla, A.1    Malik, M.2    Cataisson, C.3    Ho, Y.4    Friesen, T.5    Suh, K.S.6    Yuspa, S.H.7
  • 84
    • 33846028557 scopus 로고    scopus 로고
    • Small C-terminal domain phosphatases dephosphorylate the regulatory linker regions of Smad2 and Smad3 to enhance transforming growth factor-β signaling
    • K.H. Wrighton, D. Willis, J. Long, F. Liu, X. Lin, and X.H. Feng Small C-terminal domain phosphatases dephosphorylate the regulatory linker regions of Smad2 and Smad3 to enhance transforming growth factor-β signaling J. Biol. Chem. 281 2006 38365 38375
    • (2006) J. Biol. Chem. , vol.281 , pp. 38365-38375
    • Wrighton, K.H.1    Willis, D.2    Long, J.3    Liu, F.4    Lin, X.5    Feng, X.H.6
  • 85
    • 33845970267 scopus 로고    scopus 로고
    • Dephosphorylation of the linker regions of Smad1 and Smad2/3 by small C-terminal domain phosphatases has distinct outcomes for bone morphogenetic protein and transforming growth factor-β pathways
    • G. Sapkota, M. Knockaert, C. Alarcon, E. Montalvo, A.H. Brivanlou, and J. Massague Dephosphorylation of the linker regions of Smad1 and Smad2/3 by small C-terminal domain phosphatases has distinct outcomes for bone morphogenetic protein and transforming growth factor-β pathways J. Biol. Chem. 281 2006 40412 40419
    • (2006) J. Biol. Chem. , vol.281 , pp. 40412-40419
    • Sapkota, G.1    Knockaert, M.2    Alarcon, C.3    Montalvo, E.4    Brivanlou, A.H.5    Massague, J.6
  • 86
    • 0033257926 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of TGF-β-activated smad2
    • R.S. Lo, and J. Massague Ubiquitin-dependent degradation of TGF-β-activated smad2 Nat. Cell Biol. 1 1999 472 478
    • (1999) Nat. Cell Biol. , vol.1 , pp. 472-478
    • Lo, R.S.1    Massague, J.2
  • 87
    • 55449107515 scopus 로고    scopus 로고
    • Regulation of TGF-β family signaling by E3 ubiquitin ligases
    • Y. Inoue, and T. Imamura Regulation of TGF-β family signaling by E3 ubiquitin ligases Cancer Sci. 99 2008 2107 2112
    • (2008) Cancer Sci. , vol.99 , pp. 2107-2112
    • Inoue, Y.1    Imamura, T.2
  • 88
    • 34548238145 scopus 로고    scopus 로고
    • Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation
    • L. Levy, M. Howell, D. Das, S. Harkin, V. Episkopou, and C.S. Hill Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation Mol. Cell Biol. 27 2007 6068 6083
    • (2007) Mol. Cell Biol. , vol.27 , pp. 6068-6083
    • Levy, L.1    Howell, M.2    Das, D.3    Harkin, S.4    Episkopou, V.5    Hill, C.S.6
  • 91
    • 4444223733 scopus 로고    scopus 로고
    • Itch E3 ligase-mediated regulation of TGF-β signaling by modulating smad2 phosphorylation
    • Y. Bai, C. Yang, K. Hu, C. Elly, and Y.C. Liu Itch E3 ligase-mediated regulation of TGF-β signaling by modulating smad2 phosphorylation Mol. Cell 15 2004 825 831
    • (2004) Mol. Cell , vol.15 , pp. 825-831
    • Bai, Y.1    Yang, C.2    Hu, K.3    Elly, C.4    Liu, Y.C.5
  • 93
    • 82455210962 scopus 로고    scopus 로고
    • Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3
    • L.Y. Tang, M. Yamashita, N.P. Coussens, Y. Tang, X. Wang, C. Li, C.X. Deng, S.Y. Cheng, and Y.E. Zhang Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3 EMBO J. 30 2011 4777 4789
    • (2011) EMBO J. , vol.30 , pp. 4777-4789
    • Tang, L.Y.1    Yamashita, M.2    Coussens, N.P.3    Tang, Y.4    Wang, X.5    Li, C.6    Deng, C.X.7    Cheng, S.Y.8    Zhang, Y.E.9
  • 96
    • 33845970937 scopus 로고    scopus 로고
    • The DNA binding activities of Smad2 and Smad3 are regulated by coactivator-mediated acetylation
    • M. Simonsson, M. Kanduri, E. Gronroos, C.H. Heldin, and J. Ericsson The DNA binding activities of Smad2 and Smad3 are regulated by coactivator-mediated acetylation J. Biol. Chem. 281 2006 39870 39880
    • (2006) J. Biol. Chem. , vol.281 , pp. 39870-39880
    • Simonsson, M.1    Kanduri, M.2    Gronroos, E.3    Heldin, C.H.4    Ericsson, J.5
  • 97
    • 34547132592 scopus 로고    scopus 로고
    • Acetylation of Smad2 by the co-activator p300 regulates activin and transforming growth factor β response
    • A.W. Tu, and K. Luo Acetylation of Smad2 by the co-activator p300 regulates activin and transforming growth factor β response J. Biol. Chem. 282 2007 21187 21196
    • (2007) J. Biol. Chem. , vol.282 , pp. 21187-21196
    • Tu, A.W.1    Luo, K.2
  • 99
    • 44349125602 scopus 로고    scopus 로고
    • Mathematical modeling identifies Smad nucleocytoplasmic shuttling as a dynamic signal-interpreting system
    • B. Schmierer, A.L. Tournier, P.A. Bates, and C.S. Hill Mathematical modeling identifies Smad nucleocytoplasmic shuttling as a dynamic signal-interpreting system Proc. Natl. Acad. Sci. U S A 105 2008 6608 6613
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 6608-6613
    • Schmierer, B.1    Tournier, A.L.2    Bates, P.A.3    Hill, C.S.4
  • 100
    • 58149264873 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of Smad proteins
    • C.S. Hill Nucleocytoplasmic shuttling of Smad proteins Cell Res. 19 2009 36 46
    • (2009) Cell Res. , vol.19 , pp. 36-46
    • Hill, C.S.1
  • 101
    • 34548842261 scopus 로고    scopus 로고
    • Msk is required for nuclear import of TGF-{β}/BMP-activated Smads
    • L. Xu, X. Yao, X. Chen, P. Lu, B. Zhang, and Y.T. Ip Msk is required for nuclear import of TGF-{β}/BMP-activated Smads J. Cell. Biol. 178 2007 981 994
    • (2007) J. Cell. Biol. , vol.178 , pp. 981-994
    • Xu, L.1    Yao, X.2    Chen, X.3    Lu, P.4    Zhang, B.5    Ip, Y.T.6
  • 103
    • 61749096309 scopus 로고    scopus 로고
    • Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-β signaling
    • F. Dai, X. Lin, C. Chang, and X.H. Feng Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-β signaling Dev. Cell 16 2009 345 357
    • (2009) Dev. Cell , vol.16 , pp. 345-357
    • Dai, F.1    Lin, X.2    Chang, C.3    Feng, X.H.4
  • 104
    • 33644996932 scopus 로고    scopus 로고
    • Identification of phosphatases for Smad in the BMP/DPP pathway
    • H.B. Chen, J. Shen, Y.T. Ip, and L. Xu Identification of phosphatases for Smad in the BMP/DPP pathway Genes Dev. 20 2006 648 653
    • (2006) Genes Dev. , vol.20 , pp. 648-653
    • Chen, H.B.1    Shen, J.2    Ip, Y.T.3    Xu, L.4
  • 105
    • 2342647439 scopus 로고    scopus 로고
    • PKB/Akt modulates TGF-β signalling through a direct interaction with Smad3
    • I. Remy, A. Montmarquette, and S.W. Michnick PKB/Akt modulates TGF-β signalling through a direct interaction with Smad3 Nat. Cell Biol. 6 2004 358 365
    • (2004) Nat. Cell Biol. , vol.6 , pp. 358-365
    • Remy, I.1    Montmarquette, A.2    Michnick, S.W.3
  • 106
    • 2342471301 scopus 로고    scopus 로고
    • Akt interacts directly with Smad3 to regulate the sensitivity to TGF-β induced apoptosis
    • A.R. Conery, Y. Cao, E.A. Thompson, C.M. Townsend Jr., T.C. Ko, and K. Luo Akt interacts directly with Smad3 to regulate the sensitivity to TGF-β induced apoptosis Nat. Cell Biol. 6 2004 366 372
    • (2004) Nat. Cell Biol. , vol.6 , pp. 366-372
    • Conery, A.R.1    Cao, Y.2    Thompson, E.A.3    Townsend, Jr.C.M.4    Ko, T.C.5    Luo, K.6
  • 107
    • 30444434212 scopus 로고    scopus 로고
    • Novel roles of Akt and mTOR in suppressing TGF-β/ALK5-mediated Smad3 activation
    • K. Song, H. Wang, T.L. Krebs, and D. Danielpour Novel roles of Akt and mTOR in suppressing TGF-β/ALK5-mediated Smad3 activation EMBO J. 25 2006 58 69
    • (2006) EMBO J. , vol.25 , pp. 58-69
    • Song, K.1    Wang, H.2    Krebs, T.L.3    Danielpour, D.4
  • 108
    • 24644513885 scopus 로고    scopus 로고
    • Cytoplasmic SnoN in normal tissues and nonmalignant cells antagonizes TGF-β signaling by sequestration of the Smad proteins
    • A.R. Krakowski, J. Laboureau, A. Mauviel, M.J. Bissell, and K. Luo Cytoplasmic SnoN in normal tissues and nonmalignant cells antagonizes TGF-β signaling by sequestration of the Smad proteins Proc. Natl. Acad. Sci. U S A 102 2005 12437 12442
    • (2005) Proc. Natl. Acad. Sci. U S A , vol.102 , pp. 12437-12442
    • Krakowski, A.R.1    Laboureau, J.2    Mauviel, A.3    Bissell, M.J.4    Luo, K.5
  • 112
    • 0037422181 scopus 로고    scopus 로고
    • TGF-β-induced nuclear localization of Smad2 and Smad3 in Smad4 null cancer cell lines
    • S.P. Fink, D. Mikkola, J.K. Willson, and S. Markowitz TGF-β-induced nuclear localization of Smad2 and Smad3 in Smad4 null cancer cell lines Oncogene 22 2003 1317 1323
    • (2003) Oncogene , vol.22 , pp. 1317-1323
    • Fink, S.P.1    Mikkola, D.2    Willson, J.K.3    Markowitz, S.4
  • 113
    • 0032528236 scopus 로고    scopus 로고
    • The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for smad3 in TGF-β-induced transcriptional activation
    • X.H. Feng, Y. Zhang, R.Y. Wu, and R. Derynck The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for smad3 in TGF-β-induced transcriptional activation Genes Dev. 12 1998 2153 2163
    • (1998) Genes Dev. , vol.12 , pp. 2153-2163
    • Feng, X.H.1    Zhang, Y.2    Wu, R.Y.3    Derynck, R.4
  • 114
    • 0034460336 scopus 로고    scopus 로고
    • Transforming growth factor β-independent shuttling of Smad4 between the cytoplasm and nucleus
    • C.E. Pierreux, F.J. Nicolas, and C.S. Hill Transforming growth factor β-independent shuttling of Smad4 between the cytoplasm and nucleus Mol. Cell Biol. 20 2000 9041 9054
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9041-9054
    • Pierreux, C.E.1    Nicolas, F.J.2    Hill, C.S.3
  • 115
    • 0034252221 scopus 로고    scopus 로고
    • Regulation of intracellular dynamics of Smad4 by its leucine-rich nuclear export signal
    • M. Watanabe, N. Masuyama, M. Fukuda, and E. Nishida Regulation of intracellular dynamics of Smad4 by its leucine-rich nuclear export signal EMBO Rep. 1 2000 176 182
    • (2000) EMBO Rep. , vol.1 , pp. 176-182
    • Watanabe, M.1    Masuyama, N.2    Fukuda, M.3    Nishida, E.4
  • 116
    • 65249118863 scopus 로고    scopus 로고
    • Association of v-ErbA with Smad4 disrupts TGF-β signaling
    • R.A. Erickson, and X. Liu Association of v-ErbA with Smad4 disrupts TGF-β signaling Mol. Biol. Cell. 20 2009 1509 1519
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 1509-1519
    • Erickson, R.A.1    Liu, X.2
  • 117
    • 78650938892 scopus 로고    scopus 로고
    • Negative regulation of TGFβ signaling by the kinase LKB1 and the scaffolding protein LIP1
    • A. Moren, E. Raja, C.H. Heldin, and A. Moustakas Negative regulation of TGFβ signaling by the kinase LKB1 and the scaffolding protein LIP1 J. Biol. Chem. 286 2011 341 353
    • (2011) J. Biol. Chem. , vol.286 , pp. 341-353
    • Moren, A.1    Raja, E.2    Heldin, C.H.3    Moustakas, A.4
  • 119
    • 0347065367 scopus 로고    scopus 로고
    • Transforming growth factor-β-mediated signaling via the p38 MAP kinase pathway activates Smad-dependent transcription through SUMO-1 modification of Smad4
    • T. Ohshima, and K. Shimotohno Transforming growth factor-β-mediated signaling via the p38 MAP kinase pathway activates Smad-dependent transcription through SUMO-1 modification of Smad4 J. Biol. Chem. 278 2003 50833 50842
    • (2003) J. Biol. Chem. , vol.278 , pp. 50833-50842
    • Ohshima, T.1    Shimotohno, K.2
  • 120
    • 0041731797 scopus 로고    scopus 로고
    • SUMO-1/Ubc9 promotes nuclear accumulation and metabolic stability of tumor suppressor Smad4
    • X. Lin, M. Liang, Y.Y. Liang, F.C. Brunicardi, and X.H. Feng SUMO-1/Ubc9 promotes nuclear accumulation and metabolic stability of tumor suppressor Smad4 J. Biol. Chem. 278 2003 31043 31048
    • (2003) J. Biol. Chem. , vol.278 , pp. 31043-31048
    • Lin, X.1    Liang, M.2    Liang, Y.Y.3    Brunicardi, F.C.4    Feng, X.H.5
  • 121
    • 0042867243 scopus 로고    scopus 로고
    • Sumoylation of Smad4, the common Smad mediator of transforming growth factor-β family signaling
    • P.S. Lee, C. Chang, D. Liu, and R. Derynck Sumoylation of Smad4, the common Smad mediator of transforming growth factor-β family signaling J. Biol. Chem. 278 2003 27853 27863
    • (2003) J. Biol. Chem. , vol.278 , pp. 27853-27863
    • Lee, P.S.1    Chang, C.2    Liu, D.3    Derynck, R.4
  • 122
    • 15444380557 scopus 로고    scopus 로고
    • Daxx mediates the small ubiquitin-like modifier-dependent transcriptional repression of Smad4
    • C.C. Chang, D.Y. Lin, H.I. Fang, R.H. Chen, and H.M. Shih Daxx mediates the small ubiquitin-like modifier-dependent transcriptional repression of Smad4 J. Biol. Chem. 280 2005 10164 10173
    • (2005) J. Biol. Chem. , vol.280 , pp. 10164-10173
    • Chang, C.C.1    Lin, D.Y.2    Fang, H.I.3    Chen, R.H.4    Shih, H.M.5
  • 123
    • 0036198412 scopus 로고    scopus 로고
    • Jab1 antagonizes TGF-β signaling by inducing Smad4 degradation
    • M. Wan, X. Cao, Y. Wu, S. Bai, L. Wu, X. Shi, N. Wang, and X. Cao Jab1 antagonizes TGF-β signaling by inducing Smad4 degradation EMBO Rep. 3 2002 171 176
    • (2002) EMBO Rep. , vol.3 , pp. 171-176
    • Wan, M.1    Cao, X.2    Wu, Y.3    Bai, S.4    Wu, L.5    Shi, X.6    Wang, N.7    Cao, X.8
  • 126
    • 17044365440 scopus 로고    scopus 로고
    • Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase
    • S. Dupont, L. Zacchigna, M. Cordenonsi, S. Soligo, M. Adorno, M. Rugge, and S. Piccolo Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase Cell 121 2005 87 99
    • (2005) Cell , vol.121 , pp. 87-99
    • Dupont, S.1    Zacchigna, L.2    Cordenonsi, M.3    Soligo, S.4    Adorno, M.5    Rugge, M.6    Piccolo, S.7
  • 127
    • 33646876973 scopus 로고    scopus 로고
    • Hematopoiesis controlled by distinct TIF1γ and Smad4 branches of the TGFβ pathway
    • W. He, D.C. Dorn, H. Erdjument-Bromage, P. Tempst, M.A. Moore, and J. Massague Hematopoiesis controlled by distinct TIF1γ and Smad4 branches of the TGFβ pathway Cell 125 2006 929 941
    • (2006) Cell , vol.125 , pp. 929-941
    • He, W.1    Dorn, D.C.2    Erdjument-Bromage, H.3    Tempst, P.4    Moore, M.A.5    Massague, J.6
  • 129
    • 79959891289 scopus 로고    scopus 로고
    • Recruitment of TIF1γ to chromatin via its PHD finger-bromodomain activates its ubiquitin ligase and transcriptional repressor activities
    • E. Agricola, R.A. Randall, T. Gaarenstroom, S. Dupont, and C.S. Hill Recruitment of TIF1γ to chromatin via its PHD finger-bromodomain activates its ubiquitin ligase and transcriptional repressor activities Mol. Cell 43 2011 85 96
    • (2011) Mol. Cell , vol.43 , pp. 85-96
    • Agricola, E.1    Randall, R.A.2    Gaarenstroom, T.3    Dupont, S.4    Hill, C.S.5
  • 131
    • 0042858169 scopus 로고    scopus 로고
    • Differential ubiquitination defines the functional status of the tumor suppressor Smad4
    • A. Moren, U. Hellman, Y. Inada, T. Imamura, C.H. Heldin, and A. Moustakas Differential ubiquitination defines the functional status of the tumor suppressor Smad4 J. Biol. Chem. 278 2003 33571 33582
    • (2003) J. Biol. Chem. , vol.278 , pp. 33571-33582
    • Moren, A.1    Hellman, U.2    Inada, Y.3    Imamura, T.4    Heldin, C.H.5    Moustakas, A.6
  • 132
    • 34547122921 scopus 로고    scopus 로고
    • Selective inhibitory effects of Smad6 on bone morphogenetic protein type i receptors
    • K. Goto, Y. Kamiya, T. Imamura, K. Miyazono, and K. Miyazawa Selective inhibitory effects of Smad6 on bone morphogenetic protein type I receptors J. Biol. Chem. 282 2007 20603 20611
    • (2007) J. Biol. Chem. , vol.282 , pp. 20603-20611
    • Goto, K.1    Kamiya, Y.2    Imamura, T.3    Miyazono, K.4    Miyazawa, K.5
  • 135
    • 34250203586 scopus 로고    scopus 로고
    • Smad7 antagonizes transforming growth factor β signaling in the nucleus by interfering with functional Smad-DNA complex formation
    • S. Zhang, T. Fei, L. Zhang, R. Zhang, F. Chen, Y. Ning, Y. Han, X.H. Feng, A. Meng, and Y.G. Chen Smad7 antagonizes transforming growth factor β signaling in the nucleus by interfering with functional Smad-DNA complex formation Mol. Cell Biol. 27 2007 4488 4499
    • (2007) Mol. Cell Biol. , vol.27 , pp. 4488-4499
    • Zhang, S.1    Fei, T.2    Zhang, L.3    Zhang, R.4    Chen, F.5    Ning, Y.6    Han, Y.7    Feng, X.H.8    Meng, A.9    Chen, Y.G.10
  • 136
    • 75149171091 scopus 로고    scopus 로고
    • Nuclear function of Smad7 promotes myogenesis
    • T. Miyake, N.S. Alli, and J.C. McDermott Nuclear function of Smad7 promotes myogenesis Mol. Cell Biol. 30 2010 722 735
    • (2010) Mol. Cell Biol. , vol.30 , pp. 722-735
    • Miyake, T.1    Alli, N.S.2    McDermott, J.C.3
  • 137
    • 58149216052 scopus 로고    scopus 로고
    • Signaling cross-talk between TGF-β/BMP and other pathways
    • X. Guo, and X.F. Wang Signaling cross-talk between TGF-β/BMP and other pathways Cell Res. 19 2009 71 88
    • (2009) Cell Res. , vol.19 , pp. 71-88
    • Guo, X.1    Wang, X.F.2
  • 139
    • 0033602101 scopus 로고    scopus 로고
    • Inhibition of transforming growth factor-β/SMAD signalling by the interferon-gamma/STAT pathway
    • L. Ulloa, J. Doody, and J. Massague Inhibition of transforming growth factor-β/SMAD signalling by the interferon-gamma/STAT pathway Nature 397 1999 710 713
    • (1999) Nature , vol.397 , pp. 710-713
    • Ulloa, L.1    Doody, J.2    Massague, J.3
  • 142
    • 84871246002 scopus 로고    scopus 로고
    • The miR-106b-25 cluster targets Smad7, activates TGF-β signaling, and induces EMT and tumor initiating cell characteristics downstream of Six1 in human breast cancer
    • [Epub ahead of print]
    • Smith, A.L., Iwanaga, R., Drasin, D.J., Micalizzi, D.S., Vartuli, R.L., Tan, A.C., and Ford, H.L. (2012) The miR-106b-25 cluster targets Smad7, activates TGF-β signaling, and induces EMT and tumor initiating cell characteristics downstream of Six1 in human breast cancer. Oncogene, http://dx.doi.org/10.1038/onc.2012.11 [Epub ahead of print].
    • (2012) Oncogene
    • Smith, A.L.1    Iwanaga, R.2    Drasin, D.J.3    Micalizzi, D.S.4    Vartuli, R.L.5    Tan, A.C.6    Ford, H.L.7
  • 146
    • 0034976149 scopus 로고    scopus 로고
    • TGF-β induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation
    • S. Bonni, H.R. Wang, C.G. Causing, P. Kavsak, S.L. Stroschein, K. Luo, and J.L. Wrana TGF-β induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation Nat. Cell Biol. 3 2001 587 595
    • (2001) Nat. Cell Biol. , vol.3 , pp. 587-595
    • Bonni, S.1    Wang, H.R.2    Causing, C.G.3    Kavsak, P.4    Stroschein, S.L.5    Luo, K.6    Wrana, J.L.7
  • 147
    • 80054044729 scopus 로고    scopus 로고
    • Enhancement of TGF-β signaling responses by the E3 ubiquitin ligase Arkadia provides tumor suppression in colorectal cancer
    • V. Sharma, A.G. Antonacopoulou, S. Tanaka, A.A. Panoutsopoulos, V. Bravou, H.P. Kalofonos, and V. Episkopou Enhancement of TGF-β signaling responses by the E3 ubiquitin ligase Arkadia provides tumor suppression in colorectal cancer Cancer Res. 71 2011 6438 6449
    • (2011) Cancer Res. , vol.71 , pp. 6438-6449
    • Sharma, V.1    Antonacopoulou, A.G.2    Tanaka, S.3    Panoutsopoulos, A.A.4    Bravou, V.5    Kalofonos, H.P.6    Episkopou, V.7
  • 148
    • 81755189052 scopus 로고    scopus 로고
    • The deubiquitinase CYLD targets Smad7 protein to regulate transforming growth factor β (TGF-β) signaling and the development of regulatory T cells
    • Y. Zhao, A.M. Thornton, M.C. Kinney, C.A. Ma, J.J. Spinner, I.J. Fuss, E.M. Shevach, and A. Jain The deubiquitinase CYLD targets Smad7 protein to regulate transforming growth factor β (TGF-β) signaling and the development of regulatory T cells J. Biol. Chem. 286 2011 40520 40530
    • (2011) J. Biol. Chem. , vol.286 , pp. 40520-40530
    • Zhao, Y.1    Thornton, A.M.2    Kinney, M.C.3    Ma, C.A.4    Spinner, J.J.5    Fuss, I.J.6    Shevach, E.M.7    Jain, A.8
  • 149
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • E. Gronroos, U. Hellman, C.H. Heldin, and J. Ericsson Control of Smad7 stability by competition between acetylation and ubiquitination Mol. Cell 10 2002 483 493
    • (2002) Mol. Cell , vol.10 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 150
    • 20444474176 scopus 로고    scopus 로고
    • The balance between acetylation and deacetylation controls Smad7 stability
    • M. Simonsson, C.H. Heldin, J. Ericsson, and E. Gronroos The balance between acetylation and deacetylation controls Smad7 stability J. Biol. Chem. 280 2005 21797 21803
    • (2005) J. Biol. Chem. , vol.280 , pp. 21797-21803
    • Simonsson, M.1    Heldin, C.H.2    Ericsson, J.3    Gronroos, E.4
  • 152
    • 58149468095 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation on microarray analysis of Smad2/3 binding sites reveals roles of ETS1 and TFAP2A in transforming growth factor β signaling
    • D. Koinuma, S. Tsutsumi, N. Kamimura, H. Taniguchi, K. Miyazawa, M. Sunamura, T. Imamura, K. Miyazono, and H. Aburatani Chromatin immunoprecipitation on microarray analysis of Smad2/3 binding sites reveals roles of ETS1 and TFAP2A in transforming growth factor β signaling Mol. Cell Biol. 29 2009 172 186
    • (2009) Mol. Cell Biol. , vol.29 , pp. 172-186
    • Koinuma, D.1    Tsutsumi, S.2    Kamimura, N.3    Taniguchi, H.4    Miyazawa, K.5    Sunamura, M.6    Imamura, T.7    Miyazono, K.8    Aburatani, H.9
  • 154
    • 0034682515 scopus 로고    scopus 로고
    • Association of Smads with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor-β and wnt pathways
    • E. Labbe, A. Letamendia, and L. Attisano Association of Smads with lymphoid enhancer binding factor 1/T cell-specific factor mediates cooperative signaling by the transforming growth factor-β and wnt pathways Proc. Natl. Acad. Sci. U S A 97 2000 8358 8363
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 8358-8363
    • Labbe, E.1    Letamendia, A.2    Attisano, L.3
  • 155
    • 5644261271 scopus 로고    scopus 로고
    • The murine gastrin promoter is synergistically activated by transforming growth factor-β/Smad and Wnt signaling pathways
    • S. Lei, A. Dubeykovskiy, A. Chakladar, L. Wojtukiewicz, and T.C. Wang The murine gastrin promoter is synergistically activated by transforming growth factor-β/Smad and Wnt signaling pathways J. Biol. Chem. 279 2004 42492 42502
    • (2004) J. Biol. Chem. , vol.279 , pp. 42492-42502
    • Lei, S.1    Dubeykovskiy, A.2    Chakladar, A.3    Wojtukiewicz, L.4    Wang, T.C.5
  • 156
    • 33645007189 scopus 로고    scopus 로고
    • Smad3-dependent nuclear translocation of β-catenin is required for TGF-β1-induced proliferation of bone marrow-derived adult human mesenchymal stem cells
    • H. Jian, X. Shen, I. Liu, M. Semenov, X. He, and X.F. Wang Smad3-dependent nuclear translocation of β-catenin is required for TGF-β1-induced proliferation of bone marrow-derived adult human mesenchymal stem cells Genes Dev. 20 2006 666 674
    • (2006) Genes Dev. , vol.20 , pp. 666-674
    • Jian, H.1    Shen, X.2    Liu, I.3    Semenov, M.4    He, X.5    Wang, X.F.6
  • 157
    • 0345166971 scopus 로고    scopus 로고
    • Cross-talk between the Notch and TGF-β signaling pathways mediated by interaction of the Notch intracellular domain with Smad3
    • A. Blokzijl, C. Dahlqvist, E. Reissmann, A. Falk, A. Moliner, U. Lendahl, and C.F. Ibanez Cross-talk between the Notch and TGF-β signaling pathways mediated by interaction of the Notch intracellular domain with Smad3 J. Cell. Biol. 163 2003 723 728
    • (2003) J. Cell. Biol. , vol.163 , pp. 723-728
    • Blokzijl, A.1    Dahlqvist, C.2    Reissmann, E.3    Falk, A.4    Moliner, A.5    Lendahl, U.6    Ibanez, C.F.7
  • 158
    • 52649179291 scopus 로고    scopus 로고
    • Notch1 and TGFβ1 cooperatively regulate Foxp3 expression and the maintenance of peripheral regulatory T cells
    • J.B. Samon, A. Champhekar, L.M. Minter, J.C. Telfer, L. Miele, A. Fauq, P. Das, T.E. Golde, and B.A. Osborne Notch1 and TGFβ1 cooperatively regulate Foxp3 expression and the maintenance of peripheral regulatory T cells Blood 112 2008 1813 1821
    • (2008) Blood , vol.112 , pp. 1813-1821
    • Samon, J.B.1    Champhekar, A.2    Minter, L.M.3    Telfer, J.C.4    Miele, L.5    Fauq, A.6    Das, P.7    Golde, T.E.8    Osborne, B.A.9
  • 160
    • 67649658549 scopus 로고    scopus 로고
    • Non-Smad TGF-β Signaling Pathways
    • R. Derynck, K. Miyazono, Cold Spring Harbor Laboratory Press
    • Y. Zhang Non-Smad TGF-β Signaling Pathways R. Derynck, K. Miyazono, The TGF-β Family 2008 Cold Spring Harbor Laboratory Press 419 438
    • (2008) The TGF-β Family , pp. 419-438
    • Zhang, Y.1
  • 161
    • 0032572723 scopus 로고    scopus 로고
    • Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-β-induced transcription
    • Y. Zhang, X.H. Feng, and R. Derynck Smad3 and Smad4 cooperate with c-Jun/c-Fos to mediate TGF-β-induced transcription Nature 394 1998 909 913
    • (1998) Nature , vol.394 , pp. 909-913
    • Zhang, Y.1    Feng, X.H.2    Derynck, R.3
  • 162
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • E. Shaulian, and M. Karin AP-1 as a regulator of cell life and death Nat. Cell Biol. 4 2002 E131 E136
    • (2002) Nat. Cell Biol. , vol.4
    • Shaulian, E.1    Karin, M.2
  • 163
    • 24644476507 scopus 로고    scopus 로고
    • Crosstalk mechanisms between the mitogen-activated protein kinase pathways and Smad signaling downstream of TGF-β: Implications for carcinogenesis
    • D. Javelaud, and A. Mauviel Crosstalk mechanisms between the mitogen-activated protein kinase pathways and Smad signaling downstream of TGF-β: implications for carcinogenesis Oncogene 24 2005 5742 5750
    • (2005) Oncogene , vol.24 , pp. 5742-5750
    • Javelaud, D.1    Mauviel, A.2
  • 164
    • 0038369998 scopus 로고    scopus 로고
    • A self-enabling TGFβ response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells
    • Y. Kang, C.R. Chen, and J. Massague A self-enabling TGFβ response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells Mol. Cell 11 2003 915 926
    • (2003) Mol. Cell , vol.11 , pp. 915-926
    • Kang, Y.1    Chen, C.R.2    Massague, J.3
  • 166
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor
    • T. Tsukazaki, T.A. Chiang, A.F. Davison, L. Attisano, and J.L. Wrana SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor Cell 95 1998 779 791
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5
  • 168
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • H.K. Lin, S. Bergmann, and P.P. Pandolfi Cytoplasmic PML function in TGF-β signalling Nature 431 2004 205 211
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 169
    • 0035355473 scopus 로고    scopus 로고
    • The adaptor molecule Disabled-2 links the transforming growth factor β receptors to the Smad pathway
    • B.A. Hocevar, A. Smine, X.X. Xu, and P.H. Howe The adaptor molecule Disabled-2 links the transforming growth factor β receptors to the Smad pathway EMBO J. 20 2001 2789 2801
    • (2001) EMBO J. , vol.20 , pp. 2789-2801
    • Hocevar, B.A.1    Smine, A.2    Xu, X.X.3    Howe, P.H.4
  • 171
    • 84857890422 scopus 로고    scopus 로고
    • Modulation of noncanonical TGF-β signaling prevents cleft palate in TGFbr2 mutant mice
    • J. Iwata, J.G. Hacia, A. Suzuki, P.A. Sanchez-Lara, M. Urata, and Y. Chai Modulation of noncanonical TGF-β signaling prevents cleft palate in TGFbr2 mutant mice J. Clin. Invest. 122 2012 873 885
    • (2012) J. Clin. Invest. , vol.122 , pp. 873-885
    • Iwata, J.1    Hacia, J.G.2    Suzuki, A.3    Sanchez-Lara, P.A.4    Urata, M.5    Chai, Y.6
  • 174
    • 52049111663 scopus 로고    scopus 로고
    • TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β
    • M. Yamashita, K. Fatyol, C. Jin, X. Wang, Z. Liu, and Y.E. Zhang TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-β Mol. Cell 31 2008 918 924
    • (2008) Mol. Cell , vol.31 , pp. 918-924
    • Yamashita, M.1    Fatyol, K.2    Jin, C.3    Wang, X.4    Liu, Z.5    Zhang, Y.E.6
  • 177
    • 4444249880 scopus 로고    scopus 로고
    • α(v)β(3) Integrin interacts with the transforming growth factor β (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts
    • A.K. Scaffidi, N. Petrovic, Y.P. Moodley, M. Fogel-Petrovic, K.M. Kroeger, R.M. Seeber, K.A. Eidne, P.J. Thompson, and D.A. Knight α(v)β(3) Integrin interacts with the transforming growth factor β (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts J. Biol. Chem. 279 2004 37726 37733
    • (2004) J. Biol. Chem. , vol.279 , pp. 37726-37733
    • Scaffidi, A.K.1    Petrovic, N.2    Moodley, Y.P.3    Fogel-Petrovic, M.4    Kroeger, K.M.5    Seeber, R.M.6    Eidne, K.A.7    Thompson, P.J.8    Knight, D.A.9
  • 178
    • 0037131169 scopus 로고    scopus 로고
    • Hyaluronan promotes signaling interaction between CD44 and the transforming growth factor β receptor i in metastatic breast tumor cells
    • L.Y. Bourguignon, P.A. Singleton, H. Zhu, and B. Zhou Hyaluronan promotes signaling interaction between CD44 and the transforming growth factor β receptor I in metastatic breast tumor cells J. Biol. Chem. 277 2002 39703 39712
    • (2002) J. Biol. Chem. , vol.277 , pp. 39703-39712
    • Bourguignon, L.Y.1    Singleton, P.A.2    Zhu, H.3    Zhou, B.4
  • 181
    • 50349094328 scopus 로고    scopus 로고
    • BAT3 interacts with transforming growth factor-β (TGF-β) receptors and enhances TGF-β1-induced type i collagen expression in mesangial cells
    • J.H. Kwak, S.I. Kim, J.K. Kim, and M.E. Choi BAT3 interacts with transforming growth factor-β (TGF-β) receptors and enhances TGF-β1-induced type I collagen expression in mesangial cells J. Biol. Chem. 283 2008 19816 19825
    • (2008) J. Biol. Chem. , vol.283 , pp. 19816-19825
    • Kwak, J.H.1    Kim, S.I.2    Kim, J.K.3    Choi, M.E.4
  • 182
    • 34547105808 scopus 로고    scopus 로고
    • Requirement for the dynein light chain km23-1 in a Smad2-dependent transforming growth factor-β signaling pathway
    • Q. Jin, W. Ding, and K.M. Mulder Requirement for the dynein light chain km23-1 in a Smad2-dependent transforming growth factor-β signaling pathway J. Biol. Chem. 282 2007 19122 19132
    • (2007) J. Biol. Chem. , vol.282 , pp. 19122-19132
    • Jin, Q.1    Ding, W.2    Mulder, K.M.3
  • 183
    • 69249126664 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein and its E3 ligase activity promote transforming growth factor-{β}-mediated nuclear factor-{kappa}B activation during breast cancer progression
    • J.R. Neil, M. Tian, and W.P. Schiemann X-linked inhibitor of apoptosis protein and its E3 ligase activity promote transforming growth factor-{β}-mediated nuclear factor-{kappa}B activation during breast cancer progression J. Biol. Chem. 284 2009 21209 21217
    • (2009) J. Biol. Chem. , vol.284 , pp. 21209-21217
    • Neil, J.R.1    Tian, M.2    Schiemann, W.P.3
  • 185
    • 33745197796 scopus 로고    scopus 로고
    • FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type i receptor
    • T. Yamaguchi, A. Kurisaki, N. Yamakawa, K. Minakuchi, and H. Sugino FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor J. Mol. Endocrinol. 36 2006 569 579
    • (2006) J. Mol. Endocrinol. , vol.36 , pp. 569-579
    • Yamaguchi, T.1    Kurisaki, A.2    Yamakawa, N.3    Minakuchi, K.4    Sugino, H.5
  • 187
    • 33847379496 scopus 로고    scopus 로고
    • The evolutionally conserved activity of Dapper2 in antagonizing TGF-β signaling
    • Y. Su, L. Zhang, X. Gao, F. Meng, J. Wen, H. Zhou, A. Meng, and Y.G. Chen The evolutionally conserved activity of Dapper2 in antagonizing TGF-β signaling Faseb J. 21 2007 682 690
    • (2007) Faseb J. , vol.21 , pp. 682-690
    • Su, Y.1    Zhang, L.2    Gao, X.3    Meng, F.4    Wen, J.5    Zhou, H.6    Meng, A.7    Chen, Y.G.8
  • 189
    • 69449094525 scopus 로고    scopus 로고
    • Rock2 controls TGFβ signaling and inhibits mesoderm induction in zebrafish embryos
    • Y. Zhang, X. Li, J. Qi, J. Wang, X. Liu, H. Zhang, S.C. Lin, and A. Meng Rock2 controls TGFβ signaling and inhibits mesoderm induction in zebrafish embryos J. Cell Sci. 122 2009 2197 2207
    • (2009) J. Cell Sci. , vol.122 , pp. 2197-2207
    • Zhang, Y.1    Li, X.2    Qi, J.3    Wang, J.4    Liu, X.5    Zhang, H.6    Lin, S.C.7    Meng, A.8
  • 190
    • 0033996038 scopus 로고    scopus 로고
    • STRAP and Smad7 synergize in the inhibition of transforming growth factor β signaling
    • P.K. Datta, and H.L. Moses STRAP and Smad7 synergize in the inhibition of transforming growth factor β signaling Mol. Cell Biol. 20 2000 3157 3167
    • (2000) Mol. Cell Biol. , vol.20 , pp. 3157-3167
    • Datta, P.K.1    Moses, H.L.2
  • 191
    • 84859765672 scopus 로고    scopus 로고
    • Transcriptional induction of salt-inducible kinase 1 by transforming growth factor β leads to negative regulation of type i receptor signaling in cooperation with the Smurf2 ubiquitin ligase
    • P. Lonn, M. Vanlandewijck, E. Raja, M. Kowanetz, Y. Watanabe, K. Kowanetz, E. Vasilaki, C.H. Heldin, and A. Moustakas Transcriptional induction of salt-inducible kinase 1 by transforming growth factor β leads to negative regulation of type I receptor signaling in cooperation with the Smurf2 ubiquitin ligase J. Biol. Chem. 287 2012 12867 12878
    • (2012) J. Biol. Chem. , vol.287 , pp. 12867-12878
    • Lonn, P.1    Vanlandewijck, M.2    Raja, E.3    Kowanetz, M.4    Watanabe, Y.5    Kowanetz, K.6    Vasilaki, E.7    Heldin, C.H.8    Moustakas, A.9
  • 192
    • 30044434463 scopus 로고    scopus 로고
    • Regulation of transforming growth factor-β signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein
    • H.A. Seong, H. Jung, H.S. Choi, K.T. Kim, and H. Ha Regulation of transforming growth factor-β signaling and PDK1 kinase activity by physical interaction between PDK1 and serine-threonine kinase receptor-associated protein J. Biol. Chem. 280 2005 42897 42908
    • (2005) J. Biol. Chem. , vol.280 , pp. 42897-42908
    • Seong, H.A.1    Jung, H.2    Choi, H.S.3    Kim, K.T.4    Ha, H.5
  • 193
    • 71049139747 scopus 로고    scopus 로고
    • Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-β signaling
    • X. Yan, Z. Lin, F. Chen, X. Zhao, H. Chen, Y. Ning, and Y.G. Chen Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-β signaling J. Biol. Chem. 284 2009 30097 30104
    • (2009) J. Biol. Chem. , vol.284 , pp. 30097-30104
    • Yan, X.1    Lin, Z.2    Chen, F.3    Zhao, X.4    Chen, H.5    Ning, Y.6    Chen, Y.G.7
  • 197
    • 0037173716 scopus 로고    scopus 로고
    • Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-β/Smad signaling
    • O. Ferrigno, F. Lallemand, F. Verrecchia, S. L'Hoste, J. Camonis, A. Atfi, and A. Mauviel Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-β/Smad signaling Oncogene 21 2002 4879 4884
    • (2002) Oncogene , vol.21 , pp. 4879-4884
    • Ferrigno, O.1    Lallemand, F.2    Verrecchia, F.3    L'Hoste, S.4    Camonis, J.5    Atfi, A.6    Mauviel, A.7
  • 198
    • 78449269819 scopus 로고    scopus 로고
    • The oncoprotein c-ski functions as a direct antagonist of the transforming growth factor-{β} type i receptor
    • N. Ferrand, A. Atfi, and C. Prunier The oncoprotein c-ski functions as a direct antagonist of the transforming growth factor-{β} type I receptor Cancer Res. 70 2010 8457 8466
    • (2010) Cancer Res. , vol.70 , pp. 8457-8466
    • Ferrand, N.1    Atfi, A.2    Prunier, C.3
  • 199
    • 36849008767 scopus 로고    scopus 로고
    • TrkC binds to the type II TGF-β receptor to suppress TGF-β signaling
    • W. Jin, C. Yun, M.K. Kwak, T.A. Kim, and S.J. Kim TrkC binds to the type II TGF-β receptor to suppress TGF-β signaling Oncogene 26 2007 7684 7691
    • (2007) Oncogene , vol.26 , pp. 7684-7691
    • Jin, W.1    Yun, C.2    Kwak, M.K.3    Kim, T.A.4    Kim, S.J.5


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