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Volumn 430, Issue 2, 2010, Pages 191-198

Regulation of TGF-β signalling by protein phosphatases

Author keywords

Dephosphorylation; Phosphorylation; Protein phosphatase; Smad; Transforming growth factor (TGF ) signalling

Indexed keywords

CELLULAR FUNCTION; CRITICAL STEPS; DEPHOSPHORYLATIONS; HOMOEOSTASIS; PROTEIN PHOSPHATASE; REVERSIBLE PHOSPHORYLATION; SIGNAL TRANSDUCERS; SIGNALLING PATHWAYS; SMAD; TRANSFORMING GROWTH FACTORS;

EID: 77956682613     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100427     Document Type: Review
Times cited : (85)

References (95)
  • 1
    • 0035480050 scopus 로고    scopus 로고
    • TGF-β signalling pathways in early Xenopus development
    • Hill, C. S. (2001) TGF-β signalling pathways in early Xenopus development. Curr. Opin. Genet. Dev. 11, 533-540
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 533-540
    • Hill, C.S.1
  • 2
    • 0035504887 scopus 로고    scopus 로고
    • Intracellular BMP signaling regulation in vertebrates: Pathway or network?
    • von Bubnoff, A. and Cho, K. W. (2001) Intracellular BMP signaling regulation in vertebrates: pathway or network? Dev. Biol. 239, 1-14
    • (2001) Dev. Biol. , vol.239 , pp. 1-14
    • Bubnoff, A.1    Cho, K.W.2
  • 3
    • 0032529159 scopus 로고    scopus 로고
    • Smads and early developmental signaling by the TGFβ superfamily
    • Whitman, M. (1998) Smads and early developmental signaling by the TGFβ superfamily. Genes Dev. 12, 2445-2462
    • (1998) Genes Dev. , vol.12 , pp. 2445-2462
    • Whitman, M.1
  • 4
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi, Y. and Massague, J. (2003) Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113, 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 5
    • 40849133772 scopus 로고    scopus 로고
    • Role of transforming growth factor-β superfamily signaling pathways in human disease
    • Gordon, K. J. and Blobe, G. C. (2008) Role of transforming growth factor-β superfamily signaling pathways in human disease. Biochim. Biophys. Acta 1782, 197-228
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 197-228
    • Gordon, K.J.1    Blobe, G.C.2
  • 8
    • 7244253108 scopus 로고    scopus 로고
    • Transforming growth factor-β (TGF-β) activates cytosolic phospholipase A2α (cPLA2α)-mediated prostaglandin E2 (PGE)2/EP1 and peroxisome proliferator-activated receptor-γ (PPAR-γ)/Smad signaling pathways in human liver cancer cells. A novel mechanism for subversion of TGF-β-induced mitoinhibition
    • Han, C., Demetris, A. J., Liu, Y., Shelhamer, J. H. and Wu, T. (2004) Transforming growth factor-β (TGF-β) activates cytosolic phospholipase A2α (cPLA2α)-mediated prostaglandin E2 (PGE)2/EP1 and peroxisome proliferator-activated receptor-γ (PPAR-γ)/Smad signaling pathways in human liver cancer cells. A novel mechanism for subversion of TGF-β-induced mitoinhibition. J. Biol. Chem. 279, 44344-44354
    • (2004) J. Biol. Chem. , vol.279 , pp. 44344-44354
    • Han, C.1    Demetris, A.J.2    Liu, Y.3    Shelhamer, J.H.4    Wu, T.5
  • 9
    • 0242499448 scopus 로고    scopus 로고
    • Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer
    • Siegel, P. M. and Massague, J. (2003) Cytostatic and apoptotic actions of TGF-β in homeostasis and cancer. Nat. Rev. Cancer 3, 807-821
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 807-821
    • Siegel, P.M.1    Massague, J.2
  • 10
    • 2942519197 scopus 로고    scopus 로고
    • Antifibrotic therapy in scleroderma: Extracellular or intracellular targeting of activated fibroblasts?
    • Varga, J. (2004) Antifibrotic therapy in scleroderma: extracellular or intracellular targeting of activated fibroblasts? Curr. Rheumatol. Rep. 6, 164-170
    • (2004) Curr. Rheumatol. Rep. , vol.6 , pp. 164-170
    • Varga, J.1
  • 11
    • 0036467496 scopus 로고    scopus 로고
    • TGF-β signaling: Positive and negative effects on tumorigenesis
    • Wakefield, L. M. and Roberts, A. B. (2002) TGF-β signaling: positive and negative effects on tumorigenesis. Curr. Opin. Genet. Dev. 12, 22-29
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 22-29
    • Wakefield, L.M.1    Roberts, A.B.2
  • 12
    • 33847716712 scopus 로고    scopus 로고
    • Negative regulation of TGF-β receptor/Smad signal transduction
    • Itoh, S. and ten Dijke, P. (2007) Negative regulation of TGF-β receptor/Smad signal transduction. Curr. Opin. Cell Biol. 19, 176-184
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 176-184
    • Itoh, S.1    Ten Dijke, P.2
  • 13
    • 0037351880 scopus 로고    scopus 로고
    • The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly
    • DOI 10.1016/S1097-2765(03)00094-7
    • Greenwald, J., Groppe, J., Gray, P., Wiater, E., Kwiatkowski, W., Vale, W. and Choe, S. (2003) The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly. Mol. Cell 11, 605-617 (Pubitemid 36385117)
    • (2003) Molecular Cell , vol.11 , Issue.3 , pp. 605-617
    • Greenwald, J.1    Groppe, J.2    Gray, P.3    Wiater, E.4    Kwiatkowski, W.5    Vale, W.6    Choe, S.7
  • 15
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch, T., Sebald, W. and Dreyer, M. K. (2000) Crystal structure of the BMP-2-BRIA ectodomain complex. Nat. Struct. Biol. 7, 492-496
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 16
    • 0036069143 scopus 로고    scopus 로고
    • The 1.1 A crystal structure of human TGF-β type II receptor ligand binding domain
    • Boesen, C. C., Radaev, S., Motyka, S. A., Patamawenu, A. and Sun, P. D. (2002) The 1.1 A crystal structure of human TGF-β type II receptor ligand binding domain. Structure 10, 913-919
    • (2002) Structure , vol.10 , pp. 913-919
    • Boesen, C.C.1    Radaev, S.2    Motyka, S.A.3    Patamawenu, A.4    Sun, P.D.5
  • 17
    • 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
    • Galliher, A. J. and Schiemann, W. P. (2007) 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, 3752-3758
    • (2007) Cancer Res. , vol.67 , pp. 3752-3758
    • Galliher, A.J.1    Schiemann, W.P.2
  • 18
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues
    • Luo, K. and Lodish, H. F. (1997) Positive and negative regulation of type II TGF-β receptor signal transduction by autophosphorylation on multiple serine residues. EMBO J. 16, 1970-1981
    • (1997) EMBO J. , vol.16 , pp. 1970-1981
    • Luo, K.1    Lodish, H.F.2
  • 19
    • 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
    • Lawler, S., Feng, X. H., Chen, R. H., Maruoka, E. M., Turck, C. W., Griswold-Prenner, I. and Derynck, R. (1997) The type II transforming growth factor-β receptor autophosphorylates not only on serine and threonine but also on tyrosine residues. J. Biol. Chem. 272, 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
  • 21
    • 1442299193 scopus 로고    scopus 로고
    • Lateral signaling enhances TGF-β response complexity
    • Byfield, S. D. and Roberts, A. B. (2004) Lateral signaling enhances TGF-β response complexity. Trends Cell Biol. 14, 107-111
    • (2004) Trends Cell Biol. , vol.14 , pp. 107-111
    • Byfield, S.D.1    Roberts, A.B.2
  • 22
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-β family signalling
    • Derynck, R. and Zhang, Y. E. (2003) Smad-dependent and Smad-independent pathways in TGF-β family signalling. Nature 425, 577-584
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 23
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in TGF-β signaling through Smads
    • Feng, X. H. and Derynck, R. (2005) Specificity and versatility in TGF-β signaling through Smads. Annu. Rev. Cell. Dev. Biol. 21, 659-693
    • (2005) Annu. Rev. Cell. Dev. Biol. , vol.21 , pp. 659-693
    • Feng, X.H.1    Derynck, R.2
  • 24
    • 0034678908 scopus 로고    scopus 로고
    • Transcriptional control by the TGF-β/Smad signaling system
    • Massague, J. and Wotton, D. (2000) Transcriptional control by the TGF-β/Smad signaling system. EMBO J. 19, 1745-1754 (Pubitemid 30204386)
    • (2000) EMBO Journal , vol.19 , Issue.8 , pp. 1745-1754
    • Massague, J.1    Wotton, D.2
  • 25
    • 2342488852 scopus 로고    scopus 로고
    • New insights into TGF-β-Smad signalling
    • ten Dijke, P. and Hill, C. S. (2004) New insights into TGF-β-Smad signalling. Trends Biochem. Sci. 29, 265-273
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 265-273
    • Ten Dijke, P.1    Hill, C.S.2
  • 26
    • 0029931509 scopus 로고    scopus 로고
    • A human Mad protein acting as a BMP-regulated transcriptional activator
    • Liu, F., Hata, A., Baker, J. C., Doody, J., Carcamo, J., Harland, R. M. and Massague, J. (1996) A human Mad protein acting as a BMP-regulated transcriptional activator. Nature 381, 620-623
    • (1996) Nature , vol.381 , pp. 620-623
    • Liu, F.1    Hata, A.2    Baker, J.C.3    Doody, J.4    Carcamo, J.5    Harland, R.M.6    Massague, J.7
  • 27
    • 0034252221 scopus 로고    scopus 로고
    • Regulation of intracellular dynamics of Smad4 by its leucine-rich nuclear export signal
    • Watanabe, M., Masuyama, N., Fukuda, M. and Nishida, E. (2000) Regulation of intracellular dynamics of Smad4 by its leucine-rich nuclear export signal. EMBO Rep. 1, 176-182
    • (2000) EMBO Rep. , vol.1 , pp. 176-182
    • Watanabe, M.1    Masuyama, N.2    Fukuda, M.3    Nishida, E.4
  • 28
    • 0034608799 scopus 로고    scopus 로고
    • A distinct nuclear localization signal in the N terminus of Smad 3 determines its ligand-induced nuclear translocation
    • Xiao, Z., Liu, X., Henis, Y. I. and Lodish, H. F. (2000) A distinct nuclear localization signal in the N terminus of Smad 3 determines its ligand-induced nuclear translocation. Proc. Natl. Acad. Sci. U.S.A. 97, 7853-7858
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7853-7858
    • Xiao, Z.1    Liu, X.2    Henis, Y.I.3    Lodish, H.F.4
  • 29
    • 0034253480 scopus 로고    scopus 로고
    • The nuclear import function of Smad2 is masked by SARA and unmasked by TGFβ-dependent phosphorylation
    • Xu, L., Chen, Y. G. and Massague, J. (2000) The nuclear import function of Smad2 is masked by SARA and unmasked by TGFβ-dependent phosphorylation. Nat. Cell Biol. 2, 559-562
    • (2000) Nat. Cell Biol. , vol.2 , pp. 559-562
    • Xu, L.1    Chen, Y.G.2    Massague, J.3
  • 30
    • 0033956131 scopus 로고    scopus 로고
    • Signaling inputs converge on nuclear effectors in TGF-β signaling
    • ten Dijke, P., Miyazono, K. and Heldin, C. H. (2000) Signaling inputs converge on nuclear effectors in TGF-β signaling. Trends Biochem. Sci. 25, 64-70
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 64-70
    • Ten Dijke, P.1    Miyazono, K.2    Heldin, C.H.3
  • 31
    • 0033380665 scopus 로고    scopus 로고
    • TGF-β signaling from receptors to the nucleus
    • Roberts, A. B. (1999) TGF-β signaling from receptors to the nucleus. Microbes Infect. 1, 1265-1273
    • (1999) Microbes Infect. , vol.1 , pp. 1265-1273
    • Roberts, A.B.1
  • 32
    • 70450187617 scopus 로고    scopus 로고
    • The regulation of TGFβ signal transduction
    • Moustakas, A. and Heldin, C. H. (2009) The regulation of TGFβ signal transduction. Development 136, 3699-3714
    • (2009) Development , vol.136 , pp. 3699-3714
    • Moustakas, A.1    Heldin, C.H.2
  • 33
    • 33745188200 scopus 로고    scopus 로고
    • Smad7 and protein phosphatase 1α are critical determinants in the duration of TGF-β/ALK1 signaling in endothelial cells
    • Valdimarsdottir, G., Goumans, M. J., Itoh, F., Itoh, S., Heldin, C. H. and ten Dijke, P. (2006) Smad7 and protein phosphatase 1α are critical determinants in the duration of TGF-β/ALK1 signaling in endothelial cells. BMC Cell Biol. 7, 16
    • (2006) BMC Cell Biol. , vol.7 , pp. 16
    • Valdimarsdottir, G.1    Goumans, M.J.2    Itoh, F.3    Itoh, S.4    Heldin, C.H.5    Ten Dijke, P.6
  • 34
    • 58249089671 scopus 로고    scopus 로고
    • Holding their own: The noncanonical roles of Smad proteins
    • Hoover, L. L. and Kubalak, S. W. (2008) Holding their own: the noncanonical roles of Smad proteins. Sci. Signaling 1, pe48
    • (2008) Sci. Signaling , vol.1 , pp. 48
    • Hoover, L.L.1    Kubalak, S.W.2
  • 35
    • 35048875855 scopus 로고    scopus 로고
    • TGF-β signaling: A tale of two responses
    • Rahimi, R. A. and Leof, E. B. (2007) TGF-β signaling: a tale of two responses. J. Cell. Biochem. 102, 593-608
    • (2007) J. Cell. Biochem. , vol.102 , pp. 593-608
    • Rahimi, R.A.1    Leof, E.B.2
  • 36
    • 55449107515 scopus 로고    scopus 로고
    • Regulation of TGF-β family signaling by E3 ubiquitin ligases
    • Inoue, Y. and Imamura, T. (2008) Regulation of TGF-β family signaling by E3 ubiquitin ligases. Cancer Sci. 99, 2107-2112
    • (2008) Cancer Sci. , vol.99 , pp. 2107-2112
    • Inoue, Y.1    Imamura, T.2
  • 37
    • 0033549789 scopus 로고    scopus 로고
    • A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation
    • Zhu, H., Kavsak, P., Abdollah, S., Wrana, J. L. and Thomsen, G. H. (1999) A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400, 687-693
    • (1999) Nature , vol.400 , pp. 687-693
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 38
    • 0034711290 scopus 로고    scopus 로고
    • Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-β signaling
    • Lin, X., Liang, M. and Feng, X. H. (2000) Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-β signaling. J. Biol. Chem. 275, 36818-36822
    • (2000) J. Biol. Chem. , vol.275 , pp. 36818-36822
    • Lin, X.1    Liang, M.2    Feng, X.H.3
  • 40
    • 15944370597 scopus 로고    scopus 로고
    • NEDD4-NEDD2 (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
    • Kuratomi, G., Komuro, A., Goto, K., Shinozaki, M., Miyazawa, K., Miyazono, K. and Imamura, T. (2005) NEDD4-NEDD2 (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, 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
  • 42
    • 0034767430 scopus 로고    scopus 로고
    • Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins
    • Fukuchi, M., Imamura, T., Chiba, T., Ebisawa, T., Kawabata, M., Tanaka, K. and Miyazono, K. (2001) Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins. Mol. Biol. Cell 12, 1431-1443
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1431-1443
    • Fukuchi, M.1    Imamura, T.2    Chiba, T.3    Ebisawa, T.4    Kawabata, M.5    Tanaka, K.6    Miyazono, K.7
  • 43
    • 20144385807 scopus 로고    scopus 로고
    • CHIP controls the sensitivity of transforming growth factor-β signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation
    • Xin, H., Xu, X., Li, L., Ning, H., Rong, Y., Shang, Y., Wang, Y., Fu, X. Y. and Chang, Z. (2005) CHIP controls the sensitivity of transforming growth factor-β signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation. J. Biol. Chem. 280, 20842-20850
    • (2005) J. Biol. Chem. , vol.280 , pp. 20842-20850
    • Xin, H.1    Xu, X.2    Li, L.3    Ning, H.4    Rong, Y.5    Shang, Y.6    Wang, Y.7    Fu, X.Y.8    Chang, Z.9
  • 44
    • 0347986662 scopus 로고    scopus 로고
    • CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription
    • Li, L., Xin, H., Xu, X., Huang, M., Zhang, X., Chen, Y., Zhang, S., Fu, X. Y. and Chang, Z. (2004) CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription. Mol. Cell. Biol. 24, 856-864
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 856-864
    • Li, L.1    Xin, H.2    Xu, X.3    Huang, M.4    Zhang, X.5    Chen, Y.6    Zhang, S.7    Fu, X.Y.8    Chang, Z.9
  • 46
    • 0036198412 scopus 로고    scopus 로고
    • Jab1 antagonizes TGF-β signaling by inducing Smad4 degradation
    • Wan, M., Cao, X., Wu, Y., Bai, S., Wu, L., Shi, X. and Wang, N. (2002) Jab1 antagonizes TGF-β signaling by inducing Smad4 degradation. EMBO Rep. 3, 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
  • 47
    • 20444439172 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases
    • Moren, A., Imamura, T., Miyazono, K., Heldin, C. H. and Moustakas, A. (2005) Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases. J. Biol. Chem. 280, 22115-22123
    • (2005) J. Biol. Chem. , vol.280 , pp. 22115-22123
    • Moren, A.1    Imamura, T.2    Miyazono, K.3    Heldin, C.H.4    Moustakas, A.5
  • 48
    • 0042858169 scopus 로고    scopus 로고
    • Differential ubiquitination defines the functional status of the tumor suppressor Smad4
    • Moren, A., Hellman, U., Inada, Y., Imamura, T., Heldin, C. H. and Moustakas, A. (2003) Differential ubiquitination defines the functional status of the tumor suppressor Smad4. J. Biol. Chem. 278, 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
  • 50
    • 0037805684 scopus 로고    scopus 로고
    • Activation of transforming growth factor-β signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4
    • Lin, X., Liang, M., Liang, Y. Y., Brunicardi, F. C., Melchior, F. and Feng, X. H. (2003) Activation of transforming growth factor-β signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4. J. Biol. Chem. 278, 18714-18719
    • (2003) J. Biol. Chem. , vol.278 , pp. 18714-18719
    • Lin, X.1    Liang, M.2    Liang, Y.Y.3    Brunicardi, F.C.4    Melchior, F.5    Feng, X.H.6
  • 51
    • 0042867243 scopus 로고    scopus 로고
    • Sumoylation of Smad4, the common Smad mediator of transforming growth factor-β family signaling
    • Lee, P. S., Chang, C., Liu, D. and Derynck, R. (2003) Sumoylation of Smad4, the common Smad mediator of transforming growth factor-β family signaling. J. Biol. Chem. 278, 27853-27863
    • (2003) J. Biol. Chem. , vol.278 , pp. 27853-27863
    • Lee, P.S.1    Chang, C.2    Liu, D.3    Derynck, R.4
  • 52
    • 0035918274 scopus 로고    scopus 로고
    • Smurf1 interacts with transforming growth factor-β type I receptor through Smad7 and induces receptor degradation
    • Ebisawa, T., Fukuchi, M., Murakami, G., Chiba, T., Tanaka, K., Imamura, T. and Miyazono, K. (2001) Smurf1 interacts with transforming growth factor-β type I receptor through Smad7 and induces receptor degradation. J. Biol. Chem. 276, 12477-12480
    • (2001) J. Biol. Chem. , vol.276 , pp. 12477-12480
    • Ebisawa, T.1    Fukuchi, M.2    Murakami, G.3    Chiba, T.4    Tanaka, K.5    Imamura, T.6    Miyazono, K.7
  • 53
    • 0038363366 scopus 로고    scopus 로고
    • Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-β signaling by Smad7
    • Tajima, Y., Goto, K., Yoshida, M., Shinomiya, K., Sekimoto, T., Yoneda, Y., Miyazono, K. and Imamura, T. (2003) Chromosomal region maintenance 1 (CRM1)-dependent nuclear export of Smad ubiquitin regulatory factor 1 (Smurf1) is essential for negative regulation of transforming growth factor-β signaling by Smad7. J. Biol. Chem. 278, 10716-10721
    • (2003) J. Biol. Chem. , vol.278 , pp. 10716-10721
    • Tajima, Y.1    Goto, K.2    Yoshida, M.3    Shinomiya, K.4    Sekimoto, T.5    Yoneda, Y.6    Miyazono, K.7    Imamura, T.8
  • 55
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF β receptor for degradation
    • Kavsak, P., Rasmussen, R. K., Causing, C. G., Bonni, S., Zhu, H., Thomsen, G. H. and Wrana, J. L. (2000) Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF β receptor for degradation. Mol. Cell 6, 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
  • 58
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • DOI 10.1016/S1097-2765(02)00639-1
    • Gronroos, E., Hellman, U., Heldin, C. H. and Ericsson, J. (2002) Control of Smad7 stability by competition between acetylation and ubiquitination. Mol. Cell 10, 483-493 (Pubitemid 35284169)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.-H.3    Ericsson, J.4
  • 59
    • 20444474176 scopus 로고    scopus 로고
    • The balance between acetylation and deacetylation controls Smad7 stability
    • Simonsson, M., Heldin, C. H., Ericsson, J. and Gronroos, E. (2005) The balance between acetylation and deacetylation controls Smad7 stability. J. Biol. Chem. 280, 21797-21803
    • (2005) J. Biol. Chem. , vol.280 , pp. 21797-21803
    • Simonsson, M.1    Heldin, C.H.2    Ericsson, J.3    Gronroos, E.4
  • 61
    • 15044348175 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatases: Life, death, and sleeping
    • Gallego, M. and Virshup, D. M. (2005) Protein serine/threonine phosphatases: life, death, and sleeping. Curr. Opin. Cell Biol. 17, 197-202
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 197-202
    • Gallego, M.1    Virshup, D.M.2
  • 62
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi, Y. (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139, 468-484
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 63
    • 0035489955 scopus 로고    scopus 로고
    • Control of RNA polymerase II activity by dedicated CTD kinases and phosphatases
    • Majello, B. and Napolitano, G. (2001) Control of RNA polymerase II activity by dedicated CTD kinases and phosphatases. Front. Biosci. 6, D1358-D1368
    • (2001) Front. Biosci. , vol.6
    • Majello, B.1    Napolitano, G.2
  • 64
    • 0036699073 scopus 로고    scopus 로고
    • PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster
    • Bennett, D. and Alphey, L. (2002) PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster. Nat. Genet. 31, 419-423
    • (2002) Nat. Genet. , vol.31 , pp. 419-423
    • Bennett, D.1    Alphey, L.2
  • 65
    • 1642539976 scopus 로고    scopus 로고
    • GADD34-PP1c recruited by Smad7 dephosphorylates TGFβ type I receptor
    • Shi, W., Sun, C., He, B., Xiong, W., Shi, X., Yao, D. and Cao, X. (2004) GADD34-PP1c recruited by Smad7 dephosphorylates TGFβ type I receptor. J. Cell Biol. 164, 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
  • 66
    • 53349156578 scopus 로고    scopus 로고
    • Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling
    • Batut, J., Schmierer, B., Cao, J., Raftery, L. A., Hill, C. S. and Howell, M. (2008) Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling. Development 135, 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
  • 68
    • 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
    • Griswold-Prenner, I., Kamibayashi, C., Maruoka, E. M., Mumby, M. C. and Derynck, R. (1998) 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, 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
  • 70
    • 0036670339 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of Smads 2, 3, and 4 permits sensing of TGF-β receptor activity
    • Inman, G. J., Nicolas, F. J. and Hill, C. S. (2002) Nucleocytoplasmic shuttling of Smads 2, 3, and 4 permits sensing of TGF-β receptor activity. Mol. Cell 10, 283-294
    • (2002) Mol. Cell , vol.10 , pp. 283-294
    • Inman, G.J.1    Nicolas, F.J.2    Hill, C.S.3
  • 71
    • 27644583784 scopus 로고    scopus 로고
    • Kinetic analysis of Smad nucleocytoplasmic shuttling reveals a mechanism for transforming growth factor β-dependent nuclear accumulation of Smads
    • Schmierer, B. and Hill, C. S. (2005) Kinetic analysis of Smad nucleocytoplasmic shuttling reveals a mechanism for transforming growth factor β-dependent nuclear accumulation of Smads. Mol. Cell. Biol. 25, 9845-9858
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9845-9858
    • Schmierer, B.1    Hill, C.S.2
  • 72
    • 0036670359 scopus 로고    scopus 로고
    • Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFβ signaling complexes in the cytoplasm and nucleus
    • Xu, L., Kang, Y., Col, S. and Massague, J. (2002) Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGFβ signaling complexes in the cytoplasm and nucleus. Mol. Cell 10, 271-282
    • (2002) Mol. Cell , vol.10 , pp. 271-282
    • Xu, L.1    Kang, Y.2    Col, S.3    Massague, J.4
  • 73
    • 33947617324 scopus 로고    scopus 로고
    • Termination of TGF-β superfamily signaling through SMAD dephosphorylation: A functional genomic view
    • Lin, X., Chen, Y., Meng, A. and Feng, X. (2007) Termination of TGF-β superfamily signaling through SMAD dephosphorylation: a functional genomic view. J. Genet. Genomics 34, 1-9
    • (2007) J. Genet. Genomics , vol.34 , pp. 1-9
    • Lin, X.1    Chen, Y.2    Meng, A.3    Feng, X.4
  • 75
    • 61749096309 scopus 로고    scopus 로고
    • Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-β signaling
    • Dai, F., Lin, X., Chang, C. and Feng, X. H. (2009) Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-β signaling. Dev. Cell 16, 345-357
    • (2009) Dev. Cell , vol.16 , pp. 345-357
    • Dai, F.1    Lin, X.2    Chang, C.3    Feng, X.H.4
  • 76
    • 77950874802 scopus 로고    scopus 로고
    • MTMR4 attenuates TGFβ signaling by dephosphorylating R-Smads in endosomes
    • Yu, J., Pan, L., Qin, X., Chen, H., Xu, Y., Chen, Y. and Tang, H. (2010) MTMR4 attenuates TGFβ signaling by dephosphorylating R-Smads in endosomes. J. Biol. Chem. 285, 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
  • 77
    • 33846002754 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatase PPM1A dephosphorylates Smad1 in the bone morphogenetic protein signaling pathway
    • Duan, X., Liang, Y. Y., Feng, X. H. and Lin, X. (2006) Protein serine/threonine phosphatase PPM1A dephosphorylates Smad1 in the bone morphogenetic protein signaling pathway. J. Biol. Chem. 281, 36526-36532
    • (2006) J. Biol. Chem. , vol.281 , pp. 36526-36532
    • Duan, X.1    Liang, Y.Y.2    Feng, X.H.3    Lin, X.4
  • 78
    • 33747044916 scopus 로고    scopus 로고
    • Unique players in the BMP pathway: Small C-terminal domain phosphatases dephosphorylate Smad1 to attenuate BMP signaling
    • Knockaert, M., Sapkota, G., Alarcon, C., Massague, J. and Brivanlou, A. H. (2006) 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, 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
  • 79
    • 33644996932 scopus 로고    scopus 로고
    • Identification of phosphatases for Smad in the BMP/DPP pathway
    • Chen, H. B., Shen, J., Ip, Y. T. and Xu, L. (2006) Identification of phosphatases for Smad in the BMP/DPP pathway. Genes Dev. 20, 648-653
    • (2006) Genes Dev. , vol.20 , pp. 648-653
    • Chen, H.B.1    Shen, J.2    Ip, Y.T.3    Xu, L.4
  • 80
    • 24944497786 scopus 로고    scopus 로고
    • Non-Smad TGF-β signals
    • Moustakas, A. and Heldin, C. H. (2005) Non-Smad TGF-β signals. J. Cell Sci. 118, 3573-3584
    • (2005) J. Cell Sci. , vol.118 , pp. 3573-3584
    • Moustakas, A.1    Heldin, C.H.2
  • 81
    • 3142546336 scopus 로고    scopus 로고
    • Cyclin-dependent kinases regulate the antiproliferative function of Smads
    • Matsuura, I., Denissova, N. G., Wang, G., He, D., Long, J. and Liu, F. (2004) Cyclin-dependent kinases regulate the antiproliferative function of Smads. Nature 430, 226-231
    • (2004) Nature , vol.430 , pp. 226-231
    • Matsuura, I.1    Denissova, N.G.2    Wang, G.3    He, D.4    Long, J.5    Liu, F.6
  • 82
    • 0033106484 scopus 로고    scopus 로고
    • A mechanism of repression of TGFβ/ Smad signaling by oncogenic Ras
    • Kretzschmar, M., Doody, J., Timokhina, I. and Massague, J. (1999) A mechanism of repression of TGFβ/ Smad signaling by oncogenic Ras. Genes Dev. 13, 804-816
    • (1999) Genes Dev. , vol.13 , pp. 804-816
    • Kretzschmar, M.1    Doody, J.2    Timokhina, I.3    Massague, J.4
  • 83
    • 0036829567 scopus 로고    scopus 로고
    • Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase
    • Funaba, M., Zimmerman, C. M. and Mathews, L. S. (2002) Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase. J. Biol. Chem. 277, 41361-41368
    • (2002) J. Biol. Chem. , vol.277 , pp. 41361-41368
    • Funaba, M.1    Zimmerman, C.M.2    Mathews, L.S.3
  • 84
    • 0033601179 scopus 로고    scopus 로고
    • Interdependent SMAD and JNK signaling in transforming growth factor-β-mediated transcription
    • Engel, M. E., McDonnell, M. A., Law, B. K. and Moses, H. L. (1999) Interdependent SMAD and JNK signaling in transforming growth factor-β-mediated transcription. J. Biol. Chem. 274, 37413-37420
    • (1999) J. Biol. Chem. , vol.274 , pp. 37413-37420
    • Engel, M.E.1    McDonnell, M.A.2    Law, B.K.3    Moses, H.L.4
  • 86
    • 12544257249 scopus 로고    scopus 로고
    • Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-β-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo
    • Kamaraju, A. K. and Roberts, A. B. (2005) Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-β-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo. J. Biol. Chem. 280, 1024-1036
    • (2005) J. Biol. Chem. , vol.280 , pp. 1024-1036
    • Kamaraju, A.K.1    Roberts, A.B.2
  • 88
    • 46849092804 scopus 로고    scopus 로고
    • To (TGF)β or not to (TGF)β: Fine-tuning of Smad signaling via post-translational modifications
    • Wrighton, K. H. and Feng, X. H. (2008) To (TGF)β or not to (TGF)β: fine-tuning of Smad signaling via post-translational modifications. Cell. Signalling 20, 1579-1591
    • (2008) Cell. Signalling , vol.20 , pp. 1579-1591
    • Wrighton, K.H.1    Feng, X.H.2
  • 89
    • 58149239730 scopus 로고    scopus 로고
    • Phospho-control of TGF-β superfamily signaling
    • Wrighton, K. H., Lin, X. and Feng, X. H. (2009) Phospho-control of TGF-β superfamily signaling. Cell. Res. 19, 8-20
    • (2009) Cell. Res. , vol.19 , pp. 8-20
    • Wrighton, K.H.1    Lin, X.2    Feng, X.H.3
  • 90
    • 0030773834 scopus 로고    scopus 로고
    • Opposing BMP and EGF signalling pathways converge on the TGF-β family mediator Smad1
    • Kretzschmar, M., Doody, J. and Massague, J. (1997) Opposing BMP and EGF signalling pathways converge on the TGF-β family mediator Smad1. Nature 389, 618-622
    • (1997) Nature , vol.389 , pp. 618-622
    • Kretzschmar, M.1    Doody, J.2    Massague, J.3
  • 91
    • 2942650916 scopus 로고    scopus 로고
    • In vivo convergence of BMP and MAPK signaling pathways: Impact of differential Smad1 phosphorylation on development and homeostasis
    • Aubin, J., Davy, A. and Soriano, P. (2004) In vivo convergence of BMP and MAPK signaling pathways: impact of differential Smad1 phosphorylation on development and homeostasis. Genes Dev. 18, 1482-1494
    • (2004) Genes Dev. , vol.18 , pp. 1482-1494
    • Aubin, J.1    Davy, A.2    Soriano, P.3
  • 92
    • 33846688094 scopus 로고    scopus 로고
    • Balancing BMP Signaling through Integrated Inputs into the Smad1 Linker
    • DOI 10.1016/j.molcel.2007.01.006, PII S109727650700010X
    • Sapkota, G., Alarcon, C., Spagnoli, F. M., Brivanlou, A. H. and Massague, J. (2007) Balancing BMP signaling through integrated inputs into the Smad1 linker. Mol. Cell 25, 441-454 (Pubitemid 46199289)
    • (2007) Molecular Cell , vol.25 , Issue.3 , pp. 441-454
    • Sapkota, G.1    Alarcon, C.2    Spagnoli, F.M.3    Brivanlou, A.H.4    Massague, J.5
  • 93
    • 36248995245 scopus 로고    scopus 로고
    • Integrating patterning signals: Wnt/GSK3 regulates the duration of the BMP/Smad1 signal
    • Fuentealba, L. C., Eivers, E., Ikeda, A., Hurtado, C., Kuroda, H., Pera, E. M. and De Robertis, E. M. (2007) Integrating patterning signals: Wnt/GSK3 regulates the duration of the BMP/Smad1 signal. Cell 131, 980-993
    • (2007) Cell , vol.131 , pp. 980-993
    • Fuentealba, L.C.1    Eivers, E.2    Ikeda, A.3    Hurtado, C.4    Kuroda, H.5    Pera, E.M.6    De Robertis, E.M.7
  • 94
    • 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
    • Wrighton, K. H., Willis, D., Long, J., Liu, F., Lin, X. and Feng, X. H. (2006) 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, 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
  • 95
    • 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
    • Sapkota, G., Knockaert, M., Alarcon, C., Montalvo, E., Brivanlou, A. H. and Massague, J. (2006) 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, 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


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