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Volumn 39, Issue 8, 2012, Pages 661-667

Cell biology of Smad2/3 linker region phosphorylation in vascular smooth muscle

Author keywords

Phosphorylation; Signalling; Smads; Transforming growth factor ; Vascular smooth muscle

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; MITOGEN ACTIVATED PROTEIN KINASE; RHO KINASE; SMAD2 PROTEIN; SMAD3 PROTEIN; SMAD4 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 1;

EID: 84864317948     PISSN: 03051870     EISSN: 14401681     Source Type: Journal    
DOI: 10.1111/j.1440-1681.2011.05592.x     Document Type: Review
Times cited : (34)

References (62)
  • 1
    • 30944439493 scopus 로고    scopus 로고
    • TGFbeta pathobiology in the eye
    • Saika S. TGFbeta pathobiology in the eye. Lab. Invest. 2006; 86: 106-15.
    • (2006) Lab. Invest. , vol.86 , pp. 106-115
    • Saika, S.1
  • 2
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • Derynck R, Zhang YE. Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 2003; 425: 577-84.
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 3
    • 43149103190 scopus 로고    scopus 로고
    • Smad and p38 MAP kinase-mediated signaling of proteoglycan synthesis in vascular smooth muscle
    • Dadlani H, Ballinger ML, Osman N, Getachew R, Little PJ. Smad and p38 MAP kinase-mediated signaling of proteoglycan synthesis in vascular smooth muscle. J. Biol. Chem. 2008; 283: 7844-52.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7844-7852
    • Dadlani, H.1    Ballinger, M.L.2    Osman, N.3    Getachew, R.4    Little, P.J.5
  • 4
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague J. TGF-beta signal transduction. Annu. Rev. Biochem. 1998; 67: 753-91.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 5
  • 7
    • 11844263366 scopus 로고    scopus 로고
    • Transforming growth factor-beta, cell signaling and cardiovascular disorders
    • Agrotis A, Kalinina N, Bobik A. Transforming growth factor-beta, cell signaling and cardiovascular disorders. Curr. Vasc. Pharmacol. 2005; 3: 55-61.
    • (2005) Curr. Vasc. Pharmacol. , vol.3 , pp. 55-61
    • Agrotis, A.1    Kalinina, N.2    Bobik, A.3
  • 8
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • Huse M, Chen YG, Massague J, Kuriyan J. Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12. Cell 1999; 96: 425-36.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 9
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi Y, Massague J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 2003; 113: 685-700.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 10
    • 78649982907 scopus 로고    scopus 로고
    • The dynamic roles of TGF-beta in cancer
    • Meulmeester E, Ten Dijke P. The dynamic roles of TGF-beta in cancer. J. Pathol. 2011; 223: 205-18.
    • (2011) J. Pathol. , vol.223 , pp. 205-218
    • Meulmeester, E.1    Ten Dijke, P.2
  • 11
    • 0034796457 scopus 로고    scopus 로고
    • The TGF beta receptor activation process: An inhibitor- to substrate-binding switch
    • Huse M, Muir TW, Xu L, Chen YG, Kuriyan J, Massague J. The TGF beta receptor activation process: An inhibitor- to substrate-binding switch. Mol. Cell 2001; 8: 671-82.
    • (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
  • 12
    • 67650466368 scopus 로고    scopus 로고
    • Smad2 and Smad3 phosphorylated at both linker and COOH-terminal regions transmit malignant TGF-beta signal in later stages of human colorectal cancer
    • Matsuzaki K, Kitano C, Murata M et al. Smad2 and Smad3 phosphorylated at both linker and COOH-terminal regions transmit malignant TGF-beta signal in later stages of human colorectal cancer. Cancer Res. 2009; 69: 5321-30.
    • (2009) Cancer Res. , vol.69 , pp. 5321-5330
    • Matsuzaki, K.1    Kitano, C.2    Murata, M.3
  • 13
    • 34247539528 scopus 로고    scopus 로고
    • A tale of two proteins. Differential roles and regulation of Smad2 and Smad3 in TGF-beta signaling
    • Brown KA, Pietenpol JA, Moses HL. A tale of two proteins. Differential roles and regulation of Smad2 and Smad3 in TGF-beta signaling. J. Cell. Biochem. 2007; 101: 9-33.
    • (2007) J. Cell. Biochem. , vol.101 , pp. 9-33
    • Brown, K.A.1    Pietenpol, J.A.2    Moses, H.L.3
  • 14
    • 58149216052 scopus 로고    scopus 로고
    • Signaling cross-talk between TGF-beta/BMP and other pathways
    • Guo X, Wang XF. Signaling cross-talk between TGF-beta/BMP and other pathways. Cell Res. 2009; 19: 71-88.
    • (2009) Cell Res. , vol.19 , pp. 71-88
    • Guo, X.1    Wang, X.F.2
  • 15
    • 44349085416 scopus 로고    scopus 로고
    • Structure-function relationship of inhibitory Smads: Structural flexibility contributes to functional divergence
    • Hariharan R, Pillai MR. Structure-function relationship of inhibitory Smads: Structural flexibility contributes to functional divergence. Proteins 2008; 71: 1853-62.
    • (2008) Proteins , vol.71 , pp. 1853-1862
    • Hariharan, R.1    Pillai, M.R.2
  • 16
    • 0035116044 scopus 로고    scopus 로고
    • Structural insights on Smad function in TGFbeta signaling
    • Shi Y. Structural insights on Smad function in TGFbeta signaling. Bioessays 2001; 23: 223-32.
    • (2001) Bioessays , vol.23 , pp. 223-232
    • Shi, Y.1
  • 17
    • 58149264873 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of Smad proteins
    • Hill CS. Nucleocytoplasmic shuttling of Smad proteins. Cell Res. 2009; 19: 36-46.
    • (2009) Cell Res. , vol.19 , pp. 36-46
    • Hill, C.S.1
  • 18
    • 10744224961 scopus 로고    scopus 로고
    • Ecsit is required for Bmp signaling and mesoderm formation during mouse embryogenesis
    • Xiao C, Shim JH, Kluppel M et al. Ecsit is required for Bmp signaling and mesoderm formation during mouse embryogenesis. Genes Dev. 2003; 17: 2933-49.
    • (2003) Genes Dev. , vol.17 , pp. 2933-2949
    • Xiao, C.1    Shim, J.H.2    Kluppel, M.3
  • 20
    • 0032483544 scopus 로고    scopus 로고
    • Crystal structure of a Smad MH1 domain bound to DNA. Insights on DNA binding in TGF-beta signaling
    • Shi Y, Wang YF, Jayaraman L, Yang H, Massague J, Pavletich NP. Crystal structure of a Smad MH1 domain bound to DNA. Insights on DNA binding in TGF-beta signaling. Cell 1998; 94: 585-94.
    • (1998) Cell , vol.94 , pp. 585-594
    • Shi, Y.1    Wang, Y.F.2    Jayaraman, L.3    Yang, H.4    Massague, J.5    Pavletich, N.P.6
  • 21
    • 0033104503 scopus 로고    scopus 로고
    • Targeted disruption of SMAD3 results in impaired mucosal immunity and diminished T cell responsiveness to TGF-beta
    • Yang X, Letterio JJ, Lechleider RJ et al. Targeted disruption of SMAD3 results in impaired mucosal immunity and diminished T cell responsiveness to TGF-beta. EMBO J. 1999; 18: 1280-91.
    • (1999) EMBO J. , vol.18 , pp. 1280-1291
    • Yang, X.1    Letterio, J.J.2    Lechleider, R.J.3
  • 22
    • 70349659185 scopus 로고    scopus 로고
    • Angiotensin II induces connective tissue growth factor and collagen I expression via transforming growth factor-beta-dependent and -independent Smad pathways. The role of Smad3
    • Yang F, Chung AC, Huang XR, Lan HY. Angiotensin II induces connective tissue growth factor and collagen I expression via transforming growth factor-beta-dependent and -independent Smad pathways. The role of Smad3. Hypertension 2009; 54: 877-84.
    • (2009) Hypertension , vol.54 , pp. 877-884
    • Yang, F.1    Chung, A.C.2    Huang, X.R.3    Lan, H.Y.4
  • 23
    • 0033602186 scopus 로고    scopus 로고
    • A short amino-acid sequence in MH1 domain is responsible for functional differences between Smad2 and Smad3
    • Dennler S, Huet S, Gauthier JM. A short amino-acid sequence in MH1 domain is responsible for functional differences between Smad2 and Smad3. Oncogene 1999; 18: 1643-8.
    • (1999) Oncogene , vol.18 , pp. 1643-1648
    • Dennler, S.1    Huet, S.2    Gauthier, J.M.3
  • 24
    • 0033534573 scopus 로고    scopus 로고
    • Alternatively spliced variant of Smad2 lacking exon 3. Comparison with wild-type Smad2 and Smad3
    • Yagi K, Goto D, Hamamoto T, Takenoshita S, Kato M, Miyazono K. Alternatively spliced variant of Smad2 lacking exon 3. Comparison with wild-type Smad2 and Smad3. J. Biol. Chem. 1999; 274: 703-9.
    • (1999) J. Biol. Chem. , vol.274 , pp. 703-709
    • Yagi, K.1    Goto, D.2    Hamamoto, T.3    Takenoshita, S.4    Kato, M.5    Miyazono, K.6
  • 25
    • 65649084845 scopus 로고    scopus 로고
    • Transforming growth factor-{beta}-inducible phosphorylation of Smad3
    • Wang G, Matsuura I, He D, Liu F. Transforming growth factor-{beta}-inducible phosphorylation of Smad3. J. Biol. Chem. 2009; 284: 9663-73.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9663-9673
    • Wang, G.1    Matsuura, I.2    He, D.3    Liu, F.4
  • 26
    • 78650982203 scopus 로고    scopus 로고
    • Smad linker region phosphorylation in the regulation of extracellular matrix synthesis
    • Burch ML, Zheng W, Little PJ. Smad linker region phosphorylation in the regulation of extracellular matrix synthesis. Cell. Mol. Life Sci. 2011; 68: 97-107.
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 97-107
    • Burch, M.L.1    Zheng, W.2    Little, P.J.3
  • 27
    • 0033106484 scopus 로고    scopus 로고
    • A mechanism of repression of TGFbeta/Smad signaling by oncogenic Ras
    • Kretzschmar M, Doody J, Timokhina I, Massague J. A mechanism of repression of TGFbeta/Smad signaling by oncogenic Ras. Genes Dev. 1999; 13: 804-16.
    • (1999) Genes Dev. , vol.13 , pp. 804-816
    • Kretzschmar, M.1    Doody, J.2    Timokhina, I.3    Massague, J.4
  • 28
  • 30
    • 58149239730 scopus 로고    scopus 로고
    • Phospho-control of TGF-beta superfamily signaling
    • Wrighton KH, Lin X, Feng XH. Phospho-control of TGF-beta superfamily signaling. Cell Res. 2009; 19: 8-20.
    • (2009) Cell Res. , vol.19 , pp. 8-20
    • Wrighton, K.H.1    Lin, X.2    Feng, X.H.3
  • 31
    • 0031773264 scopus 로고    scopus 로고
    • TGF-beta-induced phosphorylation of Smad3 regulates its interaction with coactivator p300/CREB-binding protein
    • Shen X, Hu PP, Liberati NT, Datto MB, Frederick JP, Wang XF. TGF-beta-induced phosphorylation of Smad3 regulates its interaction with coactivator p300/CREB-binding protein. Mol. Biol. Cell 1998; 9: 3309-19.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3309-3319
    • Shen, X.1    Hu, P.P.2    Liberati, N.T.3    Datto, M.B.4    Frederick, J.P.5    Wang, X.F.6
  • 32
    • 0039925710 scopus 로고    scopus 로고
    • Relationship between the renin-angiotensin system genes and diabetic nephropathy in the Chinese
    • Wu S, Xiang K, Zheng T et al. Relationship between the renin-angiotensin system genes and diabetic nephropathy in the Chinese. Chin. Med. J. 2000; 113: 437-41.
    • (2000) Chin. Med. J. , vol.113 , pp. 437-441
    • Wu, S.1    Xiang, K.2    Zheng, T.3
  • 33
    • 18244362844 scopus 로고    scopus 로고
    • Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling
    • Wu JW, Hu M, Chai J et al. Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. Mol. Cell 2001; 8: 1277-89.
    • (2001) Mol. Cell , vol.8 , pp. 1277-1289
    • Wu, J.W.1    Hu, M.2    Chai, J.3
  • 34
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-beta (TGF-beta) type I receptor determines the TGF-beta intracellular signaling specificity
    • Feng XH, Derynck R. A kinase subdomain of transforming growth factor-beta (TGF-beta) type I receptor determines the TGF-beta intracellular signaling specificity. EMBO J. 1997; 16: 3912-23.
    • (1997) EMBO J. , vol.16 , pp. 3912-3923
    • Feng, X.H.1    Derynck, R.2
  • 35
    • 0030613249 scopus 로고    scopus 로고
    • TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling
    • Abdollah S, Macias-Silva M, Tsukazaki T, Hayashi H, Attisano L, Wrana JL. TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling. J. Biol. Chem. 1997; 272: 27678-85.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27678-27685
    • Abdollah, S.1    Macias-Silva, M.2    Tsukazaki, T.3    Hayashi, H.4    Attisano, L.5    Wrana, J.L.6
  • 37
    • 0033568923 scopus 로고    scopus 로고
    • Xenopus Smad4beta is the co-Smad component of developmentally regulated transcription factor complexes responsible for induction of early mesodermal genes
    • Howell M, Itoh F, Pierreux CE et al. Xenopus Smad4beta is the co-Smad component of developmentally regulated transcription factor complexes responsible for induction of early mesodermal genes. Dev. Biol. 1999; 214: 354-69.
    • (1999) Dev. Biol. , vol.214 , pp. 354-369
    • Howell, M.1    Itoh, F.2    Pierreux, C.E.3
  • 38
    • 0035814804 scopus 로고    scopus 로고
    • Sedimentation studies reveal a direct role of phosphorylation in Smad3. Smad4 homo- and hetero-trimerization
    • Correia JJ, Chacko BM, Lam SS, Lin K. Sedimentation studies reveal a direct role of phosphorylation in Smad3. Smad4 homo- and hetero-trimerization. Biochemistry 2001; 40: 1473-82.
    • (2001) Biochemistry , vol.40 , pp. 1473-1482
    • Correia, J.J.1    Chacko, B.M.2    Lam, S.S.3    Lin, K.4
  • 39
    • 0030773834 scopus 로고    scopus 로고
    • Opposing BMP and EGF signalling pathways converge on the TGF-beta family mediator Smad1
    • Kretzschmar M, Doody J, Massague J. Opposing BMP and EGF signalling pathways converge on the TGF-beta family mediator Smad1. Nature 1997; 389: 618-22.
    • (1997) Nature , vol.389 , pp. 618-622
    • Kretzschmar, M.1    Doody, J.2    Massague, J.3
  • 40
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L, Karin M. Mammalian MAP kinase signalling cascades. Nature 2001; 410: 37-40.
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 41
    • 20244376914 scopus 로고    scopus 로고
    • Transforming growth factor-beta and platelet-derived growth factor signal via c-Jun N-terminal kinase-dependent Smad2/3 phosphorylation in rat hepatic stellate cells after acute liver injury
    • Yoshida K, Matsuzaki K, Mori S et al. Transforming growth factor-beta and platelet-derived growth factor signal via c-Jun N-terminal kinase-dependent Smad2/3 phosphorylation in rat hepatic stellate cells after acute liver injury. Am. J. Pathol. 2005; 166: 1029-39.
    • (2005) Am. J. Pathol. , vol.166 , pp. 1029-1039
    • Yoshida, K.1    Matsuzaki, K.2    Mori, S.3
  • 42
    • 0029551805 scopus 로고
    • Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction
    • Yamaguchi K, Shirakabe K, Shibuya H et al. Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction. Science 1995; 270: 2008-11.
    • (1995) Science , vol.270 , pp. 2008-2011
    • Yamaguchi, K.1    Shirakabe, K.2    Shibuya, H.3
  • 43
    • 24644476507 scopus 로고    scopus 로고
    • Crosstalk mechanisms between the mitogen-activated protein kinase pathways and Smad signaling downstream of TGF-beta: Implications for carcinogenesis
    • Javelaud D, Mauviel A. Crosstalk mechanisms between the mitogen-activated protein kinase pathways and Smad signaling downstream of TGF-beta: Implications for carcinogenesis. Oncogene 2005; 24: 5742-50.
    • (2005) Oncogene , vol.24 , pp. 5742-5750
    • Javelaud, D.1    Mauviel, A.2
  • 44
    • 24944497786 scopus 로고    scopus 로고
    • Non-Smad TGF-beta signals
    • Moustakas A, Heldin CH. Non-Smad TGF-beta signals. J. Cell Sci. 2005; 118: 3573-84.
    • (2005) J. Cell Sci. , vol.118 , pp. 3573-3584
    • Moustakas, A.1    Heldin, C.H.2
  • 45
    • 0346594337 scopus 로고    scopus 로고
    • Integration of IGF, FGF, and anti-BMP signals via Smad1 phosphorylation in neural induction
    • Pera EM, Ikeda A, Eivers E, De Robertis EM. Integration of IGF, FGF, and anti-BMP signals via Smad1 phosphorylation in neural induction. Genes Dev. 2003; 17: 3023-8.
    • (2003) Genes Dev. , vol.17 , pp. 3023-3028
    • Pera, E.M.1    Ikeda, A.2    Eivers, E.3    De Robertis, E.M.4
  • 46
    • 6044261233 scopus 로고    scopus 로고
    • TGF-beta and HGF transmit the signals through JNK-dependent Smad2/3 phosphorylation at the linker regions
    • Mori S, Matsuzaki K, Yoshida K et al. TGF-beta and HGF transmit the signals through JNK-dependent Smad2/3 phosphorylation at the linker regions. Oncogene 2004; 23: 7416-29.
    • (2004) Oncogene , vol.23 , pp. 7416-7429
    • Mori, S.1    Matsuzaki, K.2    Yoshida, K.3
  • 47
    • 67749106488 scopus 로고    scopus 로고
    • A negative feedback control of transforming growth factor-beta signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204
    • Millet C, Yamashita M, Heller M, Yu LR, Veenstra TD, Zhang YE. A negative feedback control of transforming growth factor-beta signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204. J. Biol. Chem. 2009; 284: 19808-16.
    • (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
  • 48
    • 19944429743 scopus 로고    scopus 로고
    • Acceleration of Smad2 and Smad3 phosphorylation via c-Jun NH(2)-terminal kinase during human colorectal carcinogenesis
    • Yamagata H, Matsuzaki K, Mori S et al. Acceleration of Smad2 and Smad3 phosphorylation via c-Jun NH(2)-terminal kinase during human colorectal carcinogenesis. Cancer Res. 2005; 65: 157-65.
    • (2005) Cancer Res. , vol.65 , pp. 157-165
    • Yamagata, H.1    Matsuzaki, K.2    Mori, S.3
  • 49
    • 33646794060 scopus 로고    scopus 로고
    • Essential role of Smad3 in angiotensin II-induced vascular fibrosis
    • Wang W, Huang XR, Canlas E et al. Essential role of Smad3 in angiotensin II-induced vascular fibrosis. Circ. Res. 2006; 98: 1032-9.
    • (2006) Circ. Res. , vol.98 , pp. 1032-1039
    • Wang, W.1    Huang, X.R.2    Canlas, E.3
  • 50
    • 1342268353 scopus 로고    scopus 로고
    • Advanced glycation end products activate Smad signaling via TGF-beta-dependent and independent mechanisms: Implications for diabetic renal and vascular disease
    • Li JH, Huang XR, Zhu HJ et al. Advanced glycation end products activate Smad signaling via TGF-beta-dependent and independent mechanisms: Implications for diabetic renal and vascular disease. FASEB J. 2004; 18: 176-8.
    • (2004) FASEB J. , vol.18 , pp. 176-178
    • Li, J.H.1    Huang, X.R.2    Zhu, H.J.3
  • 51
    • 73849126315 scopus 로고    scopus 로고
    • Rho-kinase inhibitors as therapeutics: From pan inhibition to isoform selectivity
    • Hahmann C, Schroeter T. Rho-kinase inhibitors as therapeutics: From pan inhibition to isoform selectivity. Cell. Mol. Life Sci. 2010; 67: 171-7.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 171-177
    • Hahmann, C.1    Schroeter, T.2
  • 52
    • 0346690411 scopus 로고    scopus 로고
    • TGF-beta-induced RhoA and p160ROCK activation is involved in the inhibition of Cdc25A with resultant cell-cycle arrest
    • Bhowmick NA, Ghiassi M, Aakre M, Brown K, Singh V, Moses HL. TGF-beta-induced RhoA and p160ROCK activation is involved in the inhibition of Cdc25A with resultant cell-cycle arrest. Proc. Natl Acad. Sci. USA 2003; 100: 15548-53.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15548-15553
    • Bhowmick, N.A.1    Ghiassi, M.2    Aakre, M.3    Brown, K.4    Singh, V.5    Moses, H.L.6
  • 53
    • 12544257249 scopus 로고    scopus 로고
    • Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-beta-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo
    • Kamaraju AK, Roberts AB. Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-beta-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo. J. Biol. Chem. 2005; 280: 1024-36.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1024-1036
    • Kamaraju, A.K.1    Roberts, A.B.2
  • 54
    • 33644974307 scopus 로고    scopus 로고
    • RhoA modulates Smad signaling during transforming growth factor-beta-induced smooth muscle differentiation
    • Chen S, Crawford M, Day RM et al. RhoA modulates Smad signaling during transforming growth factor-beta-induced smooth muscle differentiation. J. Biol. Chem. 2006; 281: 1765-70.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1765-1770
    • Chen, S.1    Crawford, M.2    Day, R.M.3
  • 55
    • 3142546336 scopus 로고    scopus 로고
    • Cyclin-dependent kinases regulate the antiproliferative function of Smads
    • Matsuura I, Denissova NG, Wang G, He D, Long J, Liu F. Cyclin-dependent kinases regulate the antiproliferative function of Smads. Nature 2004; 430: 226-31.
    • (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
  • 56
    • 70350780570 scopus 로고    scopus 로고
    • Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathways
    • Alarcon C, Zaromytidou AI, Xi Q et al. Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathways. Cell 2009; 139: 757-69.
    • (2009) Cell , vol.139 , pp. 757-769
    • Alarcon, C.1    Zaromytidou, A.I.2    Xi, Q.3
  • 58
    • 59049094551 scopus 로고    scopus 로고
    • A last-minute rescue of trapped chromatin
    • Chen CT, Doxsey S. A last-minute rescue of trapped chromatin. Cell 2009; 136: 397-9.
    • (2009) Cell , vol.136 , pp. 397-399
    • Chen, C.T.1    Doxsey, S.2
  • 59
    • 0347991862 scopus 로고    scopus 로고
    • Integration of Smad and MAPK pathways: A link and a linker revisited
    • Massague J. Integration of Smad and MAPK pathways: A link and a linker revisited. Genes Dev. 2003; 17: 2993-7.
    • (2003) Genes Dev. , vol.17 , pp. 2993-2997
    • Massague, J.1
  • 60
    • 0028168242 scopus 로고
    • p15INK4B is a potential effector of TGF-beta-induced cell cycle arrest
    • Hannon GJ, Beach D. p15INK4B is a potential effector of TGF-beta-induced cell cycle arrest. Nature 1994; 371: 257-61.
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 61
    • 58149218252 scopus 로고    scopus 로고
    • Regulating the stability of TGFbeta receptors and Smads
    • Lonn P, Moren A, Raja E, Dahl M, Moustakas A. Regulating the stability of TGFbeta receptors and Smads. Cell Res. 2009; 19: 21-35.
    • (2009) Cell Res. , vol.19 , pp. 21-35
    • Lonn, P.1    Moren, A.2    Raja, E.3    Dahl, M.4    Moustakas, A.5
  • 62
    • 70350785179 scopus 로고    scopus 로고
    • Ubiquitin ligase Nedd4L targets activated Smad2/3 to limit TGF-beta signaling
    • Gao S, Alarcon C, Sapkota G et al. Ubiquitin ligase Nedd4L targets activated Smad2/3 to limit TGF-beta signaling. Mol. Cell 2009; 36: 457-68.
    • (2009) Mol. Cell , vol.36 , pp. 457-468
    • Gao, S.1    Alarcon, C.2    Sapkota, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.