메뉴 건너뛰기




Volumn 8, Issue 9, 2016, Pages

TGF-β signaling from receptors to smads

Author keywords

[No Author keywords available]

Indexed keywords

SMAD PROTEIN; TRANSFORMING GROWTH FACTOR BETA;

EID: 84986210662     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a022061     Document Type: Article
Times cited : (663)

References (302)
  • 1
    • 0030613249 scopus 로고    scopus 로고
    • TβRI 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. 1997. TβRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2–Smad4 complex formation and signaling. J Biol Chem 272: 27678–27685.
    • (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
  • 2
    • 79959891289 scopus 로고    scopus 로고
    • Recruitment of TIF1γ to chromatin via its PHD finger-bromodomain activates its ubiquitin ligase and transcriptional repressor activities
    • Agricola E, Randall RA, Gaarenstroom T, Dupont S, Hill CS. 2011. Recruitment of TIF1γ to chromatin via its PHD finger-bromodomain activates its ubiquitin ligase and transcriptional repressor activities. Mol Cell 43: 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
  • 3
    • 84857227258 scopus 로고    scopus 로고
    • MicroRNA-21 is an important downstream component of BMP signalling in epidermal keratinocytes
    • Ahmed MI, Mardaryev AN, Lewis CJ, Sharov AA, Botchkareva NV. 2011. MicroRNA-21 is an important downstream component of BMP signalling in epidermal keratinocytes. J Cell Sci 124: 3399–3404.
    • (2011) J Cell Sci , vol.124 , pp. 3399-3404
    • Ahmed, M.I.1    Mardaryev, A.N.2    Lewis, C.J.3    Sharov, A.A.4    Botchkareva, N.V.5
  • 8
    • 84862576527 scopus 로고    scopus 로고
    • Downregulated miR-195 detected in preeclamptic placenta affects trophoblast cell invasion via modulating ActRIIA expression
    • Bai Y, Yang W, Yang HX, Liao Q, Ye G, Fu G, Ji L, Xu P, Wang H, Li YX, et al. 2012. Downregulated miR-195 detected in preeclamptic placenta affects trophoblast cell invasion via modulating ActRIIA expression. PLoS ONE 7: e38875.
    • (2012) Plos ONE , vol.7
    • Bai, Y.1    Yang, W.2    Yang, H.X.3    Liao, Q.4    Ye, G.5    Fu, G.6    Ji, L.7    Xu, P.8    Wang, H.9    Li, Y.X.10
  • 11
    • 84928961742 scopus 로고    scopus 로고
    • Tumor suppressor microRNA-27a in colorectal carcinogenesis and progression by targeting SGPP1 and Smad2
    • Bao Y, Chen Z, Guo Y, Feng Y, Li Z, Han W, Wang J, Zhao W, Jiao Y, Li K, et al. 2014. Tumor suppressor microRNA-27a in colorectal carcinogenesis and progression by targeting SGPP1 and Smad2. PLoS ONE 9: e105991.
    • (2014) Plos ONE , vol.9
    • Bao, Y.1    Chen, Z.2    Guo, Y.3    Feng, Y.4    Li, Z.5    Han, W.6    Wang, J.7    Zhao, W.8    Jiao, Y.9    Li, K.10
  • 13
    • 33846599302 scopus 로고    scopus 로고
    • Kinesin-mediated transport of Smad2 is required for signaling in response to TGF-β ligands
    • Batut J, Howell M, Hill CS. 2007. Kinesin-mediated transport of Smad2 is required for signaling in response to TGF-β ligands. Dev Cell 12: 261–274.
    • (2007) Dev Cell , vol.12 , pp. 261-274
    • Batut, J.1    Howell, M.2    Hill, C.S.3
  • 14
    • 66849138206 scopus 로고    scopus 로고
    • PP2A regulates BMP signalling by interacting with BMP receptor complexes and by dephosphorylating both the C-terminus and the linker region of Smad1
    • Bengtsson L, Schwappacher R, Roth M, Boergermann JH, Hassel S, Knaus P. 2009. PP2A regulates BMP signalling by interacting with BMP receptor complexes and by dephosphorylating both the C-terminus and the linker region of Smad1. J Cell Sci 122: 1248–1257.
    • (2009) J Cell Sci , vol.122 , pp. 1248-1257
    • Bengtsson, L.1    Schwappacher, R.2    Roth, M.3    Boergermann, J.H.4    Hassel, S.5    Knaus, P.6
  • 15
    • 0036699073 scopus 로고    scopus 로고
    • PP1 binds Sara and negatively regulates Dpp signaling in Drosophila melanogaster
    • Bennett D, 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
  • 17
    • 84862758071 scopus 로고    scopus 로고
    • Smad-mediated regulation of microRNA biosynthesis
    • Blahna MT, Hata A. 2012. Smad-mediated regulation of microRNA biosynthesis. FEBS Lett 586: 1906–1912.
    • (2012) FEBS Lett , vol.586 , pp. 1906-1912
    • Blahna, M.T.1    Hata, A.2
  • 18
    • 84877928475 scopus 로고    scopus 로고
    • Regulation of miRNA biogenesis as an integrated component of growth factor signaling
    • Blahna MT, Hata A. 2013. Regulation of miRNA biogenesis as an integrated component of growth factor signaling. Curr Opin Cell Biol 25: 233–240.
    • (2013) Curr Opin Cell Biol , vol.25 , pp. 233-240
    • Blahna, M.T.1    Hata, A.2
  • 20
    • 84865315657 scopus 로고    scopus 로고
    • Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-β pathway
    • Bruce DL, Macartney T, Yong W, Shou W, Sapkota GP. 2012. Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-β pathway. Cell Signal 24: 1999–2006.
    • (2012) Cell Signal , vol.24 , pp. 1999-2006
    • Bruce, D.L.1    Macartney, T.2    Yong, W.3    Shou, W.4    Sapkota, G.P.5
  • 21
    • 44649163918 scopus 로고    scopus 로고
    • A reciprocal repression between ZEB1 and members of the miR-200 family promotes EMT and invasion in cancer cells
    • Burk U, Schubert J, Wellner U, Schmalhofer O, Vincan E, Spaderna S, Brabletz T. 2008. A reciprocal repression between ZEB1 and members of the miR-200 family promotes EMT and invasion in cancer cells. EMBO Rep 9: 582–589.
    • (2008) EMBO Rep , vol.9 , pp. 582-589
    • Burk, U.1    Schubert, J.2    Wellner, U.3    Schmalhofer, O.4    Vincan, E.5    Spaderna, S.6    Brabletz, T.7
  • 23
    • 0028894025 scopus 로고
    • Disruption of transforming growth factor β signaling by a mutation that prevents transphosphorylation within the receptor complex
    • Cárcamo J, Zentella A, Massagué J. 1995. Disruption of transforming growth factor β signaling by a mutation that prevents transphosphorylation within the receptor complex. Mol Cell Biol 15: 1573–1581.
    • (1995) Mol Cell Biol , vol.15 , pp. 1573-1581
    • Cárcamo, J.1    Zentella, A.2    Massagué, J.3
  • 24
    • 0028059199 scopus 로고
    • Homomeric interactions between type II transforming growth factor-β receptors
    • Chen RH, Derynck R. 1994. Homomeric interactions between type II transforming growth factor-β receptors. J Biol Chem 269: 22868–22874.
    • (1994) J Biol Chem , vol.269 , pp. 22868-22874
    • Chen, R.H.1    Derynck, R.2
  • 25
    • 0029157432 scopus 로고
    • AWD-domain protein that is associated with and phosphorylated by the type II TGF-β receptor
    • Chen RH, Miettinen PJ, Maruoka EM, Choy L, Derynck R. 1995. AWD-domain protein that is associated with and phosphorylated by the type II TGF-β receptor. Nature 377: 548–552.
    • (1995) Nature , vol.377 , pp. 548-552
    • Chen, R.H.1    Miettinen, P.J.2    Maruoka, E.M.3    Choy, L.4    Derynck, R.5
  • 26
    • 0030926004 scopus 로고    scopus 로고
    • Mechanism of TGF-β receptor inhibition by FKBP12
    • Chen YG, Liu F, Massagué J. 1997. Mechanism of TGF-β receptor inhibition by FKBP12. EMBO J 16: 3866–3876.
    • (1997) EMBO J , vol.16 , pp. 3866-3876
    • Chen, Y.G.1    Liu, F.2    Massagué, J.3
  • 28
    • 20444430827 scopus 로고    scopus 로고
    • Nuclear targeting of transforming growth factor-β-activated Smad complexes
    • Chen HB, Rud JG, Lin K, Xu L. 2005. Nuclear targeting of transforming growth factor-β-activated Smad complexes. J Biol Chem 280: 21329–21336.
    • (2005) J Biol Chem , vol.280 , pp. 21329-21336
    • Chen, H.B.1    Rud, J.G.2    Lin, K.3    Xu, L.4
  • 29
    • 33644996932 scopus 로고    scopus 로고
    • Identification of phosphatases for Smad in the BMP/DPP pathway
    • Chen HB, Shen J, Ip YT, 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
  • 30
    • 34248149074 scopus 로고    scopus 로고
    • Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-β signaling
    • Chen YG, Wang Z, Ma J, Zhang L, Lu Z. 2007. Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-β signaling. J Biol Chem 282: 9688–9695.
    • (2007) J Biol Chem , vol.282 , pp. 9688-9695
    • Chen, Y.G.1    Wang, Z.2    Ma, J.3    Zhang, L.4    Lu, Z.5
  • 31
    • 84929170080 scopus 로고    scopus 로고
    • Nuclear export of Smads by RanBP3L regulates bone morphogenetic protein signaling and mesenchymal stem cell differentiation
    • Chen F, Lin X, Xu P, Zhang Z, Chen Y, Wang C, Han J, Zhao B, Xiao M, Feng XH. 2015. Nuclear export of Smads by RanBP3L regulates bone morphogenetic protein signaling and mesenchymal stem cell differentiation. Mol Cell Biol 35: 1700–1711.
    • (2015) Mol Cell Biol , vol.35 , pp. 1700-1711
    • Chen, F.1    Lin, X.2    Xu, P.3    Zhang, Z.4    Chen, Y.5    Wang, C.6    Han, J.7    Zhao, B.8    Xiao, M.9    Feng, X.H.10
  • 32
    • 84902437542 scopus 로고    scopus 로고
    • MicroRNA-146a regulates human foetal femur derived skeletal stem cell differentiation by down-regulating SMAD2 and SMAD3
    • Cheung KS, Sposito N, Stumpf PS, Wilson DI, SanchezElsner T, Oreffo RO. 2014. MicroRNA-146a regulates human foetal femur derived skeletal stem cell differentiation by down-regulating SMAD2 and SMAD3. PLoS ONE 9: e98063.
    • (2014) Plos ONE , vol.9
    • Cheung, K.S.1    Sposito, N.2    Stumpf, P.S.3    Wilson, D.I.4    Sanchezelsner, T.5    Oreffo, R.O.6
  • 33
    • 17244368330 scopus 로고    scopus 로고
    • Tsc-22 enhances TGF-β signaling by associating with Smad4 and induces erythroid cell differentiation
    • Choi SJ, Moon JH, Ahn YW, Ahn JH, Kim DU, Han TH. 2005. Tsc-22 enhances TGF-β signaling by associating with Smad4 and induces erythroid cell differentiation. Mol Cell Biochem 271: 23–28.
    • (2005) Mol Cell Biochem , vol.271 , pp. 23-28
    • Choi, S.J.1    Moon, J.H.2    Ahn, Y.W.3    Ahn, J.H.4    Kim, D.U.5    Han, T.H.6
  • 34
    • 0032553555 scopus 로고    scopus 로고
    • The type II transforming growth factor (TGF)-β receptor-interacting protein TRIP-1 acts as a modulator of the TGF-β response
    • Choy L, Derynck R. 1998. The type II transforming growth factor (TGF)-β receptor-interacting protein TRIP-1 acts as a modulator of the TGF-β response. J Biol Chem 273: 31455–31462.
    • (1998) J Biol Chem , vol.273 , pp. 31455-31462
    • Choy, L.1    Derynck, R.2
  • 36
    • 2342471301 scopus 로고    scopus 로고
    • Akt interacts directly with Smad3 to regulate the sensitivity to TGF-β induced apoptosis
    • Conery AR, Cao Y, Thompson EA, Townsend CM Jr, Ko TC, Luo K. 2004. Akt interacts directly with Smad3 to regulate the sensitivity to TGF-β induced apoptosis. Nat Cell Biol 6: 366–372.
    • (2004) Nat Cell Biol , vol.6 , pp. 366-372
    • Conery, A.R.1    Cao, Y.2    Thompson, E.A.3    Townsend, C.M.4    Ko, T.C.5    Luo, K.6
  • 37
  • 38
    • 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, Feng XH. 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
  • 39
    • 0033996038 scopus 로고    scopus 로고
    • STRAP and Smad7 synergize in the inhibition of transforming growth factorβ signaling
    • Datta PK, Moses HL. 2000. STRAP and Smad7 synergize in the inhibition of transforming growth factorβ signaling. Mol Cell Biol 20: 3157–3167.
    • (2000) Mol Cell Biol , vol.20 , pp. 3157-3167
    • Datta, P.K.1    Moses, H.L.2
  • 40
    • 0032567487 scopus 로고    scopus 로고
    • Identification of STRAP, a novel WD domain protein in transforming growth factor-β signaling
    • Datta PK, Chytil A, Gorska AE, Moses HL. 1998. Identification of STRAP, a novel WD domain protein in transforming growth factor-β signaling. J Biol Chem 273: 34671–34674.
    • (1998) J Biol Chem , vol.273 , pp. 34671-34674
    • Datta, P.K.1    Chytil, A.2    Gorska, A.E.3    Moses, H.L.4
  • 41
    • 46449128469 scopus 로고    scopus 로고
    • SMAD proteins control DROSHA-mediated microRNA maturation
    • Davis BN, Hilyard AC, Lagna G, Hata A. 2008. SMAD proteins control DROSHA-mediated microRNA maturation. Nature 454: 56–61.
    • (2008) Nature , vol.454 , pp. 56-61
    • Davis, B.N.1    Hilyard, A.C.2    Lagna, G.3    Hata, A.4
  • 42
    • 77955484492 scopus 로고    scopus 로고
    • Smad proteins bind a conserved RNA sequence to promote microRNA maturation by Drosha
    • Davis BN, Hilyard AC, Nguyen PH, Lagna G, Hata A. 2010. Smad proteins bind a conserved RNA sequence to promote microRNA maturation by Drosha. Mol Cell 39: 373–384.
    • (2010) Mol Cell , vol.39 , pp. 373-384
    • Davis, B.N.1    Hilyard, A.C.2    Nguyen, P.H.3    Lagna, G.4    Hata, A.5
  • 43
    • 80051532504 scopus 로고    scopus 로고
    • Down-regulation of Krüppel-like factor-4 (KLF4) by microRNA-143/145 is critical for modulation of vascular smooth muscle cell phenotype by transforming growth factor-β and bone morphogenetic protein 4
    • Davis-Dusenbery BN, Chan MC, Reno KE, Weisman AS, Layne MD, Lagna G, Hata A. 2011. Down-regulation of Krüppel-like factor-4 (KLF4) by microRNA-143/145 is critical for modulation of vascular smooth muscle cell phenotype by transforming growth factor-β and bone morphogenetic protein 4. J Biol Chem 286: 28097– 28110.
    • (2011) J Biol Chem , vol.286
    • Davis-Dusenbery, B.N.1    Chan, M.C.2    Reno, K.E.3    Weisman, A.S.4    Layne, M.D.5    Lagna, G.6    Hata, A.7
  • 44
    • 58149239731 scopus 로고    scopus 로고
    • Ski and SnoN, potent negative regulators of TGF-β signaling
    • Deheuninck J, Luo K. 2009. Ski and SnoN, potent negative regulators of TGF-β signaling. Cell Res 19: 47–57.
    • (2009) Cell Res , vol.19 , pp. 47-57
    • Deheuninck, J.1    Luo, K.2
  • 45
    • 84863939887 scopus 로고    scopus 로고
    • Presenilins and γ-secretase: Structure, function, and role in Alzheimer disease
    • De Strooper B, Iwatsubo T, Wolfe MS. 2012. Presenilins and γ-secretase: Structure, function, and role in Alzheimer disease. Cold Spring Harb Perspect Med 2: a006304.
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • De Strooper, B.1    Iwatsubo, T.2    Wolfe, M.S.3
  • 46
    • 64149085515 scopus 로고    scopus 로고
    • BMP-6 inhibits microRNA-21 expression in breast cancer through repressing δEF1 and AP-1
    • Du J, Yang S, An D, Hu F, Yuan W, Zhai C, Zhu T. 2009. BMP-6 inhibits microRNA-21 expression in breast cancer through repressing δEF1 and AP-1. Cell Res 19: 487–496.
    • (2009) Cell Res , vol.19 , pp. 487-496
    • Du, J.1    Yang, S.2    An, D.3    Hu, F.4    Yuan, W.5    Zhai, C.6    Zhu, T.7
  • 47
    • 33846002754 scopus 로고    scopus 로고
    • Protein serine/ threonine phosphatase PPM1A dephosphorylates Smad1 in the bone morphogenetic protein signaling pathway
    • Duan X, Liang YY, Feng XH, 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
  • 49
    • 17044365440 scopus 로고    scopus 로고
    • Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase
    • Dupont S, Zacchigna L, Cordenonsi M, Soligo S, Adorno M, Rugge M, Piccolo S. 2005. Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase. Cell 121: 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
  • 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, 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
    • 0030926005 scopus 로고    scopus 로고
    • A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity
    • Feng XH, Derynck R. 1997. A kinase subdomain of transforming growth factor-β (TGF-β) type I receptor determines the TGF-β intracellular signaling specificity. EMBO J 16: 3912–3923.
    • (1997) EMBO J , vol.16 , pp. 3912-3923
    • Feng, X.H.1    Derynck, R.2
  • 54
    • 23044466047 scopus 로고    scopus 로고
    • Specificity and versatility in TGF-β signaling through Smads
    • Feng XH, 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
  • 55
    • 78449269819 scopus 로고    scopus 로고
    • The oncoprotein c-ski functions as a direct antagonist of the transforming growth factor-β type I receptor
    • Ferrand N, Atfi A, Prunier C. 2010. The oncoprotein c-ski functions as a direct antagonist of the transforming growth factor-β type I receptor. Cancer Res 70: 8457–8466.
    • (2010) Cancer Res , vol.70 , pp. 8457-8466
    • Ferrand, N.1    Atfi, A.2    Prunier, C.3
  • 56
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho A, Melchior F. 2013. Sumoylation: A regulatory protein modification in health and disease. Annu Rev Biochem 82: 357–385.
    • (2013) Annu Rev Biochem , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 57
    • 84875228517 scopus 로고    scopus 로고
    • MicroRNA-376c impairs transforming growth factor-β and nodal signaling to promote trophoblast cell proliferation and invasion
    • Fu G, Ye G, Nadeem L, Ji L, Manchanda T, Wang Y, Zhao Y, Qiao J, Wang YL, Lye S, et al. 2013. MicroRNA-376c impairs transforming growth factor-β and nodal signaling to promote trophoblast cell proliferation and invasion. Hypertension 61: 864–872.
    • (2013) Hypertension , vol.61 , pp. 864-872
    • Fu, G.1    Ye, G.2    Nadeem, L.3    Ji, L.4    Manchanda, T.5    Wang, Y.6    Zhao, Y.7    Qiao, J.8    Wang, Y.L.9    Lye, S.10
  • 59
    • 77956566522 scopus 로고    scopus 로고
    • Reduction of transforming growth factor-β type II receptor is caused by the enhanced ubiquitin-dependent degradation in human renal cell carcinoma
    • Fukasawa H, Yamamoto T, Fujigaki Y, Misaki T, Ohashi N, Takayama T, Suzuki S, Mugiya S, Oda T, Uchida C, et al. 2010. Reduction of transforming growth factor-β type II receptor is caused by the enhanced ubiquitin-dependent degradation in human renal cell carcinoma. Int J Cancer 127: 1517–1525.
    • (2010) Int J Cancer , vol.127 , pp. 1517-1525
    • Fukasawa, H.1    Yamamoto, T.2    Fujigaki, Y.3    Misaki, T.4    Ohashi, N.5    Takayama, T.6    Suzuki, S.7    Mugiya, S.8    Oda, T.9    Uchida, C.10
  • 60
    • 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, 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
  • 64
    • 79960752625 scopus 로고    scopus 로고
    • Stage-specific modulation of cortical neuronal development by Mμ-miR-134
    • Gaughwin P, Ciesla M, Yang H, Lim B, Brundin P. 2011. Stage-specific modulation of cortical neuronal development by Mμ-miR-134. Cereb Cortex 21: 1857–1869.
    • (2011) Cereb Cortex , vol.21 , pp. 1857-1869
    • Gaughwin, P.1    Ciesla, M.2    Yang, H.3    Lim, B.4    Brundin, P.5
  • 65
    • 0032559594 scopus 로고    scopus 로고
    • Oligomeric structure of type I and type II transforming growth factor β receptors: Homodimers form in the ER and persist at the plasma membrane
    • Gilboa L, Wells RG, Lodish HF, Henis YI. 1998. Oligomeric structure of type I and type II transforming growth factor β receptors: Homodimers form in the ER and persist at the plasma membrane. J Cell Biol 140: 767–777.
    • (1998) J Cell Biol , vol.140 , pp. 767-777
    • Gilboa, L.1    Wells, R.G.2    Lodish, H.F.3    Henis, Y.I.4
  • 66
    • 84941588340 scopus 로고    scopus 로고
    • Endofin, a novel BMP-SMAD regulator of the iron-regulatory hormone, hepcidin
    • Goh JB, Wallace DF, Hong W, Subramaniam VN. 2015. Endofin, a novel BMP-SMAD regulator of the iron-regulatory hormone, hepcidin. Sci Rep 5: 13986.
    • (2015) Sci Rep , vol.5 , pp. 13986
    • Goh, J.B.1    Wallace, D.F.2    Hong, W.3    Subramaniam, V.N.4
  • 68
    • 0031741865 scopus 로고    scopus 로고
    • Physical and functional interactions between type I transforming growth factor β receptors and Ba, a WD-40 repeat subunit of phosphatase 2A
    • Griswold-Prenner I, Kamibayashi C, Maruoka EM, Mumby MC, Derynck R. 1998. Physical and functional interactions between type I transforming growth factor β receptors and Ba, 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
  • 69
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetyla-tion and ubiquitination
    • Grönroos E, Hellman U, Heldin CH, Ericsson J. 2002. Control of Smad7 stability by competition between acetyla-tion and ubiquitination. Mol Cell 10: 483–493.
    • (2002) Mol Cell , vol.10 , pp. 483-493
    • Grönroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 71
    • 84892389396 scopus 로고    scopus 로고
    • TRAF6 stimulates the tumor-promoting effects of TGF-β type I receptor through polyubiquitination and activation of presenilin 1
    • Gudey SK, Sundar R, Mu Y, Wallenius A, Zang G, Bergh A, Heldin CH, Landstrom M. 2014. TRAF6 stimulates the tumor-promoting effects of TGF-β type I receptor through polyubiquitination and activation of presenilin 1. Sci Signal 7: ra2.
    • (2014) Sci Signal , vol.7
    • Gudey, S.K.1    Sundar, R.2    Mu, Y.3    Wallenius, A.4    Zang, G.5    Bergh, A.6    Heldin, C.H.7    Landstrom, M.8
  • 72
    • 38149054804 scopus 로고    scopus 로고
    • Axin and GSK3-β control Smad3 protein stability and modulate TGF-β signaling
    • Guo X, Ramirez A, Waddell DS, Li Z, Liu X, Wang XF. 2008. Axin and GSK3-β control Smad3 protein stability and modulate TGF-β signaling. Genes Dev 22: 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
  • 74
    • 84904985459 scopus 로고    scopus 로고
    • Regulation of microRNA biogenesis
    • Ha M, Kim VN. 2014. Regulation of microRNA biogenesis. Nat Rev Mol Cell Biol 15: 509–524.
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 509-524
    • Ha, M.1    Kim, V.N.2
  • 76
    • 84924962270 scopus 로고    scopus 로고
    • Dysregulation of microRNA biogenesis and gene silencing in cancer
    • Hata A, Lieberman J. 2015. Dysregulation of microRNA biogenesis and gene silencing in cancer. Sci Signal 8: re3.
    • (2015) Sci Signal , vol.8
    • Hata, A.1    Lieberman, J.2
  • 78
    • 33646876973 scopus 로고    scopus 로고
    • Hematopoiesis controlled by distinct TIF1γ and Smad4 branches of the TGF-β pathway
    • He W, Dorn DC, Erdjument-Bromage H, Tempst P, Moore MA, Massagué J. 2006. Hematopoiesis controlled by distinct TIF1γ and Smad4 branches of the TGF-β pathway. Cell 125: 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    Massagué, J.6
  • 79
    • 0028291369 scopus 로고
    • The types II and III transforming growth factor-β receptors form homo-oligomers
    • Henis YI, Moustakas A, Lin HY, Lodish HF. 1994. The types II and III transforming growth factor-β receptors form homo-oligomers. J Cell Biol 126: 139–154.
    • (1994) J Cell Biol , vol.126 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 80
    • 58149264873 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of Smad proteins
    • Hill CS. 2009. Nucleocytoplasmic shuttling of Smad proteins. Cell Res 19: 36–46.
    • (2009) Cell Res , vol.19 , pp. 36-46
    • Hill, C.S.1
  • 81
    • 0035355473 scopus 로고    scopus 로고
    • The adaptor molecule disabled-2 links the transforming growth factor β receptors to the Smad pathway
    • Hocevar BA, Smine A, Xu XX, Howe PH. 2001. The adaptor molecule disabled-2 links the transforming growth factor β receptors to the Smad pathway. EMBO J 20: 2789– 2801.
    • (2001) EMBO J , vol.20
    • Hocevar, B.A.1    Smine, A.2    Xu, X.X.3    Howe, P.H.4
  • 82
    • 84885895325 scopus 로고    scopus 로고
    • BMP-6 inhibits cell proliferation by targeting mi-croRNA-192 in breast cancer
    • Hu F, Meng X, Tong Q, Liang L, Xiang R, Zhu T, Yang S. 2013. BMP-6 inhibits cell proliferation by targeting mi-croRNA-192 in breast cancer. Biochim Biophys Acta 1832: 2379–2390.
    • (2013) Biochim Biophys Acta , vol.1832 , pp. 2379-2390
    • Hu, F.1    Meng, X.2    Tong, Q.3    Liang, L.4    Xiang, R.5    Zhu, T.6    Yang, S.7
  • 83
    • 84862890645 scopus 로고    scopus 로고
    • Regulation of TGF-β receptor activity
    • Huang F, Chen YG. 2012. Regulation of TGF-β receptor activity. Cell Biosci 2: 9.
    • (2012) Cell Biosci , vol.2 , pp. 9
    • Huang, F.1    Chen, Y.G.2
  • 84
    • 47049125858 scopus 로고    scopus 로고
    • Upregulation of miR-23aα 27aα24 decreases transforming growth factor-β-induced tumor-suppressive activities in human hepatocellular carcinoma cells
    • Huang S, He X, Ding J, Liang L, Zhao Y, Zhang Z, Yao X, Pan Z, Zhang P, Li J, et al. 2008. Upregulation of miR-23aα 27aα24 decreases transforming growth factor-β-induced tumor-suppressive activities in human hepatocellular carcinoma cells. Int J Cancer 123: 972–978.
    • (2008) Int J Cancer , vol.123 , pp. 972-978
    • Huang, S.1    He, X.2    Ding, J.3    Liang, L.4    Zhao, Y.5    Zhang, Z.6    Yao, X.7    Pan, Z.8    Zhang, P.9    Li, J.10
  • 86
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12
    • Huse M, Chen YG, Massagué J, Kuriyan J. 1999. Crystal structure of the cytoplasmic domain of the type I TGFβ receptor in complex with FKBP12. Cell 96: 425–436.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massagué, J.3    Kuriyan, J.4
  • 87
    • 0034796457 scopus 로고    scopus 로고
    • The TGFβ receptor activation process: An inhibitorto substrate-binding switch
    • Huse M, Muir TW, Xu L, Chen YG, Kuriyan J, Massagué J. 2001. The TGFβ receptor activation process: An inhibitorto substrate-binding switch. Mol Cell 8: 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    Massagué, J.6
  • 88
    • 84906265350 scopus 로고    scopus 로고
    • Suh N. 2014. miR-140–5p suppresses BMP2mediated osteogenesis in undifferentiated human mesenchymal stem cells
    • Hwang S, Park SK, Lee HY, Kim SW, Lee JS, Choi EK, You D, Kim CS, Suh N. 2014. miR-140–5p suppresses BMP2mediated osteogenesis in undifferentiated human mesenchymal stem cells. FEBS Lett 588: 2957–2963.
    • FEBS Lett , vol.588 , pp. 2957-2963
    • Hwang, S.1    Park, S.K.2    Lee, H.Y.3    Kim, S.W.4    Lee, J.S.5    Choi, E.K.6    You, D.7    Kim, C.S.8
  • 89
    • 84890534490 scopus 로고    scopus 로고
    • Regulation of TGF-β family signalling by ubiquitination and deubiquitination
    • Imamura T, Oshima Y, Hikita A. 2013. Regulation of TGF-β family signalling by ubiquitination and deubiquitination. J Biochem 154: 481–489.
    • (2013) J Biochem , vol.154 , pp. 481-489
    • Imamura, T.1    Oshima, Y.2    Hikita, A.3
  • 92
    • 0036201871 scopus 로고    scopus 로고
    • The FYVE domain in Smad anchor for receptor activation (SARA) is sufficient for localization of SARA in early endosomes and regulates TGF-β/Smad signalling
    • Itoh F, Divecha N, Brocks L, Oomen L, Janssen H, Calafat J, Itoh S, Dijke Pt P. 2002. The FYVE domain in Smad anchor for receptor activation (SARA) is sufficient for localization of SARA in early endosomes and regulates TGF-β/Smad signalling. Genes Cells 7: 321–331.
    • (2002) Genes Cells , vol.7 , pp. 321-331
    • Itoh, F.1    Divecha, N.2    Brocks, L.3    Oomen, L.4    Janssen, H.5    Calafat, J.6    Itoh, S.7    Dijke Pt, P.8
  • 93
    • 0037423374 scopus 로고    scopus 로고
    • Elucidation of Smad requirement in transforming growth factor-β type I receptor-induced responses
    • Itoh S, Thorikay M, Kowanetz M, Moustakas A, Itoh F, Heldin CH, ten Dijke P. 2003. Elucidation of Smad requirement in transforming growth factor-β type I receptor-induced responses. J Biol Chem 278: 3751–3761.
    • (2003) J Biol Chem , vol.278 , pp. 3751-3761
    • Itoh, S.1    Thorikay, M.2    Kowanetz, M.3    Moustakas, A.4    Itoh, F.5    Heldin, C.H.6    Ten Dijke, P.7
  • 94
    • 67749145694 scopus 로고    scopus 로고
    • MicroRNA-141 and -200a are involved in bone morphogenetic protein-2-induced mouse pre-osteoblast differentiation by targeting distalless homeobox 5
    • Itoh T, Nozawa Y, Akao Y. 2009. MicroRNA-141 and -200a are involved in bone morphogenetic protein-2-induced mouse pre-osteoblast differentiation by targeting distalless homeobox 5. J Biol Chem 284: 19272–19279.
    • (2009) J Biol Chem , vol.284 , pp. 19272-19279
    • Itoh, T.1    Nozawa, Y.2    Akao, Y.3
  • 95
    • 70449726627 scopus 로고    scopus 로고
    • Requirement of a dynein light chain in TGF-β/Smad3 signaling
    • Jin Q, Gao G, Mulder KM. 2009. Requirement of a dynein light chain in TGF-β/Smad3 signaling. J Cell Physiol 221: 707–715.
    • (2009) J Cell Physiol , vol.221 , pp. 707-715
    • Jin, Q.1    Gao, G.2    Mulder, K.M.3
  • 96
    • 0038369998 scopus 로고    scopus 로고
    • A self-enabling TGF-β response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells
    • Kang Y, Chen CR, Massagué J. 2003. A self-enabling TGF-β response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells. Mol Cell 11: 915–926.
    • (2003) Mol Cell , vol.11 , pp. 915-926
    • Kang, Y.1    Chen, C.R.2    Massagué, J.3
  • 97
    • 44649163272 scopus 로고    scopus 로고
    • The type I TGF-β receptor is covalently modified and regulated by sumoylation
    • Kang JS, Saunier EF, Akhurst RJ, Derynck R. 2008. The type I TGF-β receptor is covalently modified and regulated by sumoylation. Nat Cell Biol 10: 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
  • 98
    • 68549123472 scopus 로고    scopus 로고
    • New regulatory mechanisms of TGF-β receptor function
    • Kang JS, Liu C, Derynck R. 2009. New regulatory mechanisms of TGF-β receptor function. Trends Cell Biol 19: 385–394.
    • (2009) Trends Cell Biol , vol.19 , pp. 385-394
    • Kang, J.S.1    Liu, C.2    Derynck, R.3
  • 99
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation
    • Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, Wrana JL. 2000. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ 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
  • 100
    • 4644286291 scopus 로고    scopus 로고
    • TSC-22 (TGF-β stimulated clone-22): A novel molecular target for differentiation-inducing therapy in salivary gland cancer
    • Kawamata H, Fujimori T, Imai Y. 2004. TSC-22 (TGF-β stimulated clone-22): A novel molecular target for differentiation-inducing therapy in salivary gland cancer. Curr Cancer Drug Targets 4: 521–529.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 521-529
    • Kawamata, H.1    Fujimori, T.2    Imai, Y.3
  • 102
    • 73349117464 scopus 로고    scopus 로고
    • MiR-21 regulates adipogenic differentiation through the modulation of TGF-β signaling in mesenchymal stem cells derived from human adipose tissue
    • Kim YJ, Hwang SJ, Bae YC, Jung JS. 2009. MiR-21 regulates adipogenic differentiation through the modulation of TGF-β signaling in mesenchymal stem cells derived from human adipose tissue. Stem Cells 27: 3093–3102.
    • (2009) Stem Cells , vol.27 , pp. 3093-3102
    • Kim, Y.J.1    Hwang, S.J.2    Bae, Y.C.3    Jung, J.S.4
  • 104
    • 84895544024 scopus 로고    scopus 로고
    • Down-regulation of miR-96 by bone morphogenetic protein signaling is critical for vascular smooth muscle cell phenotype modulation
    • Kim S, Hata A, Kang H. 2014. Down-regulation of miR-96 by bone morphogenetic protein signaling is critical for vascular smooth muscle cell phenotype modulation. J Cell Biochem 115: 889–895.
    • (2014) J Cell Biochem , vol.115 , pp. 889-895
    • Kim, S.1    Hata, A.2    Kang, H.3
  • 105
    • 4644312604 scopus 로고    scopus 로고
    • Negative regulation of transforming growth factor-β (TGF-β) signaling by WW domain-containing protein 1 (WWP1)
    • Komuro A, Imamura T, Saitoh M, Yoshida Y, Yamori T, Miyazono K, Miyazawa K. 2004. Negative regulation of transforming growth factor-β (TGF-β) signaling by WW domain-containing protein 1 (WWP1). Oncogene 23: 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
  • 106
    • 47249091921 scopus 로고    scopus 로고
    • The miR-200 family inhibits epithelial-mesenchymal transition and cancer cell migration by direct targeting of E-cadherin transcriptional repressors ZEB1 and ZEB2
    • Korpal M, Lee ES, Hu G, Kang Y. 2008. The miR-200 family inhibits epithelial-mesenchymal transition and cancer cell migration by direct targeting of E-cadherin transcriptional repressors ZEB1 and ZEB2. J Biol Chem 283: 14910–14914.
    • (2008) J Biol Chem , vol.283 , pp. 14910-14914
    • Korpal, M.1    Lee, E.S.2    Hu, G.3    Kang, Y.4
  • 108
    • 0030773834 scopus 로고    scopus 로고
    • Opposing BMP and EGF signalling pathways converge on the TGF-β family mediator Smad1
    • Kretzschmar M, Doody J, Massagué 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    Massagué, J.3
  • 109
    • 15944370597 scopus 로고    scopus 로고
    • NEDD 4–2 (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
    • Kuratomi G, Komuro A, Goto K, Shinozaki M, Miyazawa K, Miyazono K, Imamura T. 2005. NEDD 4–2 (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: 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
  • 110
    • 0035167095 scopus 로고    scopus 로고
    • Transforming growth factor-β induces nuclear import of Smad3 in an importin-β1 and Ran-dependent manner
    • Kurisaki A, Kose S, Yoneda Y, Heldin CH, Moustakas A. 2001. Transforming growth factor-β induces nuclear import of Smad3 in an importin-β1 and Ran-dependent manner. Mol Biol Cell 12: 1079–1091.
    • (2001) Mol Biol Cell , vol.12 , pp. 1079-1091
    • Kurisaki, A.1    Kose, S.2    Yoneda, Y.3    Heldin, C.H.4    Moustakas, A.5
  • 112
    • 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
    • Labbé E, Letamendia A, Attisano L. 2000. 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 97: 8358–8363.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 8358-8363
    • Labbé, E.1    Letamendia, A.2    Attisano, L.3
  • 113
    • 33846456632 scopus 로고    scopus 로고
    • Transcriptional cooperation between the transforming growth factor-β and Wnt pathways in mammary and intestinal tumorigenesis
    • Labbé E, Lock L, Letamendia A, Gorska AE, Gryfe R, Gallinger S, Moses HL, Attisano L. 2007. Transcriptional cooperation between the transforming growth factor-β and Wnt pathways in mammary and intestinal tumorigenesis. Cancer Res 67: 75–84.
    • (2007) Cancer Res , vol.67 , pp. 75-84
    • Labbé, E.1    Lock, L.2    Letamendia, A.3    Gorska, A.E.4    Gryfe, R.5    Gallinger, S.6    Moses, H.L.7    Attisano, L.8
  • 114
    • 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 XH, Chen RH, Maruoka EM, Turck CW, Griswold-Prenner I, 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
  • 115
    • 0042867243 scopus 로고    scopus 로고
    • Sumoylation of Smad4, the common Smad mediator of transforming growth factor-β family signaling
    • Lee PS, Chang C, Liu D, 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
  • 117
    • 44849143723 scopus 로고    scopus 로고
    • Transforming growth factor-β suppresses the ability of Ski to inhibit tumor metastasis by inducing its degradation
    • Le Scolan E, Zhu Q, Wang L, Bandyopadhyay A, Javelaud D, Mauviel A, Sun L, Luo K. 2008. Transforming growth factor-β suppresses the ability of Ski to inhibit tumor metastasis by inducing its degradation. Cancer Res 68: 3277–3285.
    • (2008) Cancer Res , vol.68 , pp. 3277-3285
    • Le Scolan, E.1    Zhu, Q.2    Wang, L.3    Bandyopadhyay, A.4    Javelaud, D.5    Mauviel, A.6    Sun, L.7    Luo, K.8
  • 118
    • 34548238145 scopus 로고    scopus 로고
    • Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation
    • Levy L, Howell M, Das D, Harkin S, Episkopou V, Hill CS. 2007. Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Mol Cell Biol 27: 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
  • 119
    • 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 XY, 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
  • 121
    • 84863138752 scopus 로고    scopus 로고
    • MiR-17–92 cluster regulates cell proliferation and collagen synthesis by targeting TGFβ pathway in mouse palatal mesenchymal cells
    • Li L, Shi JY, Zhu GQ, Shi B. 2012. MiR-17–92 cluster regulates cell proliferation and collagen synthesis by targeting TGFβ pathway in mouse palatal mesenchymal cells. J Cell Biochem 113: 1235–1244.
    • (2012) J Cell Biochem , vol.113 , pp. 1235-1244
    • Li, L.1    Shi, J.Y.2    Zhu, G.Q.3    Shi, B.4
  • 122
    • 84902154205 scopus 로고    scopus 로고
    • The antifibrotic effects and mechanisms of microRNA-26a action in idiopathic pulmonary fibrosis
    • Liang H, Xu C, Pan Z, Zhang Y, Xu Z, Chen Y, Li T, Li X, Liu Y, Huangfu L, et al. 2014. The antifibrotic effects and mechanisms of microRNA-26a action in idiopathic pulmonary fibrosis. Mol Ther 22: 1122–1133.
    • (2014) Mol Ther , vol.22 , pp. 1122-1133
    • Liang, H.1    Xu, C.2    Pan, Z.3    Zhang, Y.4    Xu, Z.5    Chen, Y.6    Li, T.7    Li, X.8    Liu, Y.9    Huangfu, L.10
  • 124
    • 0026680532 scopus 로고
    • Expression cloning of TGF-β receptors
    • Lin HY, Wang XF. 1992. Expression cloning of TGF-β receptors. Mol Reprod Dev 32: 105–110.
    • (1992) Mol Reprod Dev , vol.32 , pp. 105-110
    • Lin, H.Y.1    Wang, X.F.2
  • 125
    • 0026537831 scopus 로고
    • Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase
    • Lin HY, Wang XF, Ng-Eaton E, Weinberg RA, Lodish HF. 1992. Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase. Cell 68: 775–785.
    • (1992) Cell , vol.68 , pp. 775-785
    • Lin, H.Y.1    Wang, X.F.2    Ng-Eaton, E.3    Weinberg, R.A.4    Lodish, H.F.5
  • 126
    • 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, Feng XH. 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
  • 127
    • 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 YY, Brunicardi FC, Melchior F, Feng XH. 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
  • 128
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-β signalling
    • Lin HK, Bergmann S, Pandolfi PP. 2004. Cytoplasmic PML function in TGF-β signalling. Nature 431: 205–211.
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 130
    • 66449127376 scopus 로고    scopus 로고
    • Liu CJ. 2009. miR-199a, a bone morphogenic protein 2-responsive MicroRNA, regulates chondrogenesis via direct targeting to Smad1
    • Lin EA, Kong L, Bai XH, Luan Y, Liu CJ. 2009. miR-199a, a bone morphogenic protein 2-responsive MicroRNA, regulates chondrogenesis via direct targeting to Smad1. J Biol Chem 284: 11326–11335.
    • J Biol Chem , vol.284 , pp. 11326-11335
    • Lin, E.A.1    Kong, L.2    Bai, X.H.3    Luan, Y.4
  • 131
    • 84914142033 scopus 로고    scopus 로고
    • miR-199a-5p inhibits monocyte/macrophage differentiation by targeting the activin A type 1B receptor gene and finally reducing C/ EBPα expression
    • Lin HS, Gong JN, Su R, Chen MT, Song L, Shen C, Wang F, Ma YN, Zhao HL, Yu J, et al. 2014. miR-199a-5p inhibits monocyte/macrophage differentiation by targeting the activin A type 1B receptor gene and finally reducing C/ EBPα expression. J Leukoc Biol 96: 1023–1035.
    • J Leukoc Biol , vol.96 , pp. 1023-1035
    • Lin, H.S.1    Gong, J.N.2    Su, R.3    Chen, M.T.4    Song, L.5    Shen, C.6    Wang, F.7    Ma, Y.N.8    Zhao, H.L.9    Yu, J.10
  • 132
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG. 2001. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol 153: 1391–1402.
    • (2001) J Cell Biol , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1    Holaska, J.M.2    Welch, K.3    Paschal, B.M.4    Macara, I.G.5
  • 134
    • 0030886204 scopus 로고    scopus 로고
    • Transforming growth factor β-induced phosphorylation of Smad3 is required for growth inhibition and transcriptional induction in epithelial cells
    • Liu X, Sun Y, Constantinescu SN, Karam E, Weinberg RA, Lodish HF. 1997. Transforming growth factor β-induced phosphorylation of Smad3 is required for growth inhibition and transcriptional induction in epithelial cells. Proc Natl Acad Sci 94: 10669–10674.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 10669-10674
    • Liu, X.1    Sun, Y.2    Constantinescu, S.N.3    Karam, E.4    Weinberg, R.A.5    Lodish, H.F.6
  • 135
    • 33646132747 scopus 로고    scopus 로고
    • Axin is a scaffold protein in TGF-β signaling that promotes degradation of Smad7 by Arkadia
    • Liu W, Rui H, Wang J, Lin S, He Y, Chen M, Li Q, Ye Z, Zhang S, Chan SC, et al. 2006. Axin is a scaffold protein in TGF-β signaling that promotes degradation of Smad7 by Arkadia. EMBO J 25: 1646–1658.
    • (2006) EMBO J , vol.25 , pp. 1646-1658
    • Liu, W.1    Rui, H.2    Wang, J.3    Lin, S.4    He, Y.5    Chen, M.6    Li, Q.7    Ye, Z.8    Zhang, S.9    Chan, S.C.10
  • 136
    • 67649664111 scopus 로고    scopus 로고
    • TACE-mediated ectodomain shedding of the type I TGF-β receptor downregulates TGF-β signaling
    • Liu C, Xu P, Lamouille S, Xu J, Derynck R. 2009. TACE-mediated ectodomain shedding of the type I TGF-β receptor downregulates TGF-β signaling. Mol Cell 35: 26– 36.
    • (2009) Mol Cell , vol.35
    • Liu, C.1    Xu, P.2    Lamouille, S.3    Xu, J.4    Derynck, R.5
  • 137
    • 84885955083 scopus 로고    scopus 로고
    • Nodal promotes mir206 expression to control convergence and extension movements during zebrafish gastrulation
    • Liu X, Ma Y, Zhang C, Wei S, Cao Y, Wang Q. 2013. Nodal promotes mir206 expression to control convergence and extension movements during zebrafish gastrulation. J Genet Genomics 40: 515–521.
    • (2013) J Genet Genomics , vol.40 , pp. 515-521
    • Liu, X.1    Ma, Y.2    Zhang, C.3    Wei, S.4    Cao, Y.5    Wang, Q.6
  • 138
    • 0032481351 scopus 로고    scopus 로고
    • The L3 loop: A structural motif determining specific interactions between SMAD proteins and TGF-β receptors
    • Lo RS, Chen YG, Shi Y, Pavletich NP, Massagué J. 1998. The L3 loop: A structural motif determining specific interactions between SMAD proteins and TGF-β receptors. EMBO J 17: 996–1005.
    • (1998) EMBO J , vol.17 , pp. 996-1005
    • Lo, R.S.1    Chen, Y.G.2    Shi, Y.3    Pavletich, N.P.4    Massagué, J.5
  • 139
    • 84855803816 scopus 로고    scopus 로고
    • Overexpression of miR-370 and downregulation of its novel target TGF-β-RII contribute to the progression of gastric carcinoma
    • Lo SS, Hung PS, Chen JH, Tu HF, Fang WL, Chen CY, Chen WT, Gong NR, Wu CW. 2012. Overexpression of miR-370 and downregulation of its novel target TGF-β-RII contribute to the progression of gastric carcinoma. Oncogene 31: 226–237.
    • (2012) Oncogene , vol.31 , pp. 226-237
    • Lo, S.S.1    Hung, P.S.2    Chen, J.H.3    Tu, H.F.4    Fang, W.L.5    Chen, C.Y.6    Chen, W.T.7    Gong, N.R.8    Wu, C.W.9
  • 140
    • 1842844308 scopus 로고    scopus 로고
    • Repression of Smad4 transcriptional activity by SUMO modification
    • Long J, Wang G, He D, Liu F. 2004. Repression of Smad4 transcriptional activity by SUMO modification. Biochem J 379: 23–29.
    • (2004) Biochem J , vol.379 , pp. 23-29
    • Long, J.1    Wang, G.2    He, D.3    Liu, F.4
  • 141
    • 84890904166 scopus 로고    scopus 로고
    • MicroRNA-22 is a master regulator of bone morphogenetic protein-7/6 homeostasis in the kidney
    • Long J, Badal SS, Wang Y, Chang BH, Rodriguez A, Danesh FR. 2013. MicroRNA-22 is a master regulator of bone morphogenetic protein-7/6 homeostasis in the kidney. J Biol Chem 288: 36202–36214.
    • (2013) J Biol Chem , vol.288 , pp. 36202-36214
    • Long, J.1    Badal, S.S.2    Wang, Y.3    Chang, B.H.4    Rodriguez, A.5    Danesh, F.R.6
  • 142
    • 58149218252 scopus 로고    scopus 로고
    • Regulating the stability of TGF-β receptors and Smads
    • Lönn P, Morén A, Raja E, Dahl M, Moustakas A. 2009. Regulating the stability of TGF-β receptors and Smads. Cell Res 19: 21–35.
    • (2009) Cell Res , vol.19 , pp. 21-35
    • Lönn, P.1    Morén, A.2    Raja, E.3    Dahl, M.4    Moustakas, A.5
  • 144
    • 79953045754 scopus 로고    scopus 로고
    • TGF-β1 promotes motility and inva-siveness of glioma cells through activation of ADAM17
    • Lu Y, Jiang F, Zheng X, Katakowski M, Buller B, To SS, Chopp M. 2011. TGF-β1 promotes motility and inva-siveness of glioma cells through activation of ADAM17. Oncol Rep 25: 1329–1335.
    • (2011) Oncol Rep , vol.25 , pp. 1329-1335
    • Lu, Y.1    Jiang, F.2    Zheng, X.3    Katakowski, M.4    Buller, B.5    To, S.S.6    Chopp, M.7
  • 145
    • 0030972496 scopus 로고    scopus 로고
    • Positive and negative regulation of type II TGF-β receptor signal transduction by autophos-phorylation on multiple serine residues
    • Luo K, Lodish HF. 1997. Positive and negative regulation of type II TGF-β receptor signal transduction by autophos-phorylation on multiple serine residues. EMBO J 16: 1970–1981.
    • (1997) EMBO J , vol.16 , pp. 1970-1981
    • Luo, K.1    Lodish, H.F.2
  • 146
    • 84865858694 scopus 로고    scopus 로고
    • MicroRNA-378a-5p promotes trophoblast cell survival, migration and invasion by targeting Nodal
    • Luo L, Ye G, Nadeem L, Fu G, Yang BB, Honarparvar E, Dunk C, Lye S, Peng C. 2012. MicroRNA-378a-5p promotes trophoblast cell survival, migration and invasion by targeting Nodal. J Cell Sci 125: 3124–3132.
    • (2012) J Cell Sci , vol.125 , pp. 3124-3132
    • Luo, L.1    Ye, G.2    Nadeem, L.3    Fu, G.4    Yang, B.B.5    Honarparvar, E.6    Dunk, C.7    Lye, S.8    Peng, C.9
  • 147
    • 84896545297 scopus 로고    scopus 로고
    • Crosstalk between TGF-β/ Smad3 and BMP/BMPR2 signaling pathways via miR-17–92 cluster in carotid artery restenosis
    • Luo T, Cui S, Bian C, Yu X. 2014. Crosstalk between TGF-β/ Smad3 and BMP/BMPR2 signaling pathways via miR-17–92 cluster in carotid artery restenosis. Mol Cell Biochem 389: 169–176.
    • (2014) Mol Cell Biochem , vol.389 , pp. 169-176
    • Luo, T.1    Cui, S.2    Bian, C.3    Yu, X.4
  • 148
    • 84942821307 scopus 로고    scopus 로고
    • The downregulation of microRNA-146a modulates TGF-β signaling pathways activity in glioblastoma
    • Lv S, Sun B, Dai C, Shi R, Zhou X, Lv W, Zhong X, Wang R, Ma W. 2014. The downregulation of microRNA-146a modulates TGF-β signaling pathways activity in glioblastoma. Mol Neurobiol 52: 1257–1262
    • (2014) Mol Neurobiol , vol.52 , pp. 1257-1262
    • Lv, S.1    Sun, B.2    Dai, C.3    Shi, R.4    Zhou, X.5    Lv, W.6    Zhong, X.7    Wang, R.8    Ma, W.9
  • 149
    • 79955479177 scopus 로고    scopus 로고
    • ADAM17 (TACE) regulates TGF-β signaling through the cleavage of vasorin
    • Malapeira J, Esselens C, Bech-Serra JJ, Canals F, Arribas J. 2011. ADAM17 (TACE) regulates TGF-β signaling through the cleavage of vasorin. Oncogene 30: 1912–1922.
    • (2011) Oncogene , vol.30 , pp. 1912-1922
    • Malapeira, J.1    Esselens, C.2    Bech-Serra, J.J.3    Canals, F.4    Arribas, J.5
  • 151
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué J. 1998. TGF-β signal transduction. Annu Rev Biochem 67: 753–791.
    • (1998) Annu Rev Biochem , vol.67 , pp. 753-791
    • Massagué, J.1
  • 152
    • 84866742560 scopus 로고    scopus 로고
    • TGF-β signalling in context
    • Massagué J. 2012. TGF-β signalling in context. Nat Rev Mol Cell Biol 13: 616–630.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 616-630
    • Massagué, J.1
  • 153
    • 0034654497 scopus 로고    scopus 로고
    • Controlling TGF-β signaling
    • Massagué J, Chen YG. 2000. Controlling TGF-β signaling. Genes Dev 14: 627–644.
    • (2000) Genes Dev , vol.14 , pp. 627-644
    • Massagué, J.1    Chen, Y.G.2
  • 154
    • 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. 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
  • 156
    • 0035830756 scopus 로고    scopus 로고
    • Conserved role for 14–3-3ε downstream of type I TGF-β receptors
    • McGonigle S, Beall MJ, Feeney EL, Pearce EJ. 2001. Conserved role for 14–3-3ε downstream of type I TGF-β receptors. FEBS Lett 490: 65–69.
    • (2001) FEBS Lett , vol.490 , pp. 65-69
    • McGonigle, S.1    Beall, M.J.2    Feeney, E.L.3    Pearce, E.J.4
  • 157
    • 0037080168 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2α subunit associates with TGF-β receptors and 14-3-3ε and acts as a modulator of the TGF-β response
    • McGonigle S, Beall MJ, Pearce EJ. 2002. Eukaryotic initiation factor 2α subunit associates with TGF-β receptors and 14-3-3ε and acts as a modulator of the TGF-β response. Biochemistry 41: 579–587.
    • (2002) Biochemistry , vol.41 , pp. 579-587
    • McGonigle, S.1    Beall, M.J.2    Pearce, E.J.3
  • 158
    • 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
    • Millet C, Yamashita M, Heller M, Yu LR, Veenstra TD, Zhang YE. 2009. 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: 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
  • 161
    • 20444439172 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases
    • Morén A, Imamura T, Miyazono K, Heldin CH, 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
    • Morén, A.1    Imamura, T.2    Miyazono, K.3    Heldin, C.H.4    Moustakas, A.5
  • 162
    • 84896847445 scopus 로고    scopus 로고
    • Hippo signaling regulates microprocessor and links cell-density-dependent miRNA biogenesis to cancer
    • Mori M, Triboulet R, Mohseni M, Schlegelmilch K, Shrestha K, Camargo FD, Gregory RI. 2014. Hippo signaling regulates microprocessor and links cell-density-dependent miRNA biogenesis to cancer. Cell 156: 893–906.
    • (2014) Cell , vol.156 , pp. 893-906
    • Mori, M.1    Triboulet, R.2    Mohseni, M.3    Schlegelmilch, K.4    Shrestha, K.5    Camargo, F.D.6    Gregory, R.I.7
  • 163
    • 70450187617 scopus 로고    scopus 로고
    • The regulation of TGF-β signal transduction
    • Moustakas A, Heldin CH. 2009. The regulation of TGF-β signal transduction. Development 136: 3699–3714.
    • (2009) Development , vol.136 , pp. 3699-3714
    • Moustakas, A.1    Heldin, C.H.2
  • 165
    • 0038107486 scopus 로고    scopus 로고
    • Cooperative inhibition of bone morphogenetic protein signaling by Smurf1 and inhibitory Smads
    • Murakami G, Watabe T, Takaoka K, Miyazono K, Imamura T. 2003. Cooperative inhibition of bone morphogenetic protein signaling by Smurf1 and inhibitory Smads. Mol Biol Cell 14: 2809–2817.
    • (2003) Mol Biol Cell , vol.14 , pp. 2809-2817
    • Murakami, G.1    Watabe, T.2    Takaoka, K.3    Miyazono, K.4    Imamura, T.5
  • 166
    • 77953797876 scopus 로고    scopus 로고
    • Smurf1 ubiquitin ligase causes downregulation of BMP receptors and is induced in monocrotaline and hypoxia models of pulmonary arterial hypertension
    • Murakami K, Mathew R, Huang J, Farahani R, Peng H, Olson SC, Etlinger JD. 2010. Smurf1 ubiquitin ligase causes downregulation of BMP receptors and is induced in monocrotaline and hypoxia models of pulmonary arterial hypertension. Exp Biol Med 235: 805–813.
    • (2010) Exp Biol Med , vol.235 , pp. 805-813
    • Murakami, K.1    Mathew, R.2    Huang, J.3    Farahani, R.4    Peng, H.5    Olson, S.C.6    Etlinger, J.D.7
  • 167
    • 84953242016 scopus 로고    scopus 로고
    • ShcA protects against epithelial-mesenchymal transition through compartmentalized inhibition of TGF-β-induced Smad activation
    • Muthusamy BP, Budi EH, Katsuno Y, Lee MK, Smith SM, Mirza AM, Akhurst RJ, Derynck R. 2015. ShcA protects against epithelial-mesenchymal transition through compartmentalized inhibition of TGF-β-induced Smad activation. PLoS Biol 13: e1002325.
    • (2015) Plos Biol , vol.13
    • Muthusamy, B.P.1    Budi, E.H.2    Katsuno, Y.3    Lee, M.K.4    Smith, S.M.5    Mirza, A.M.6    Akhurst, R.J.7    Derynck, R.8
  • 168
    • 84907584470 scopus 로고    scopus 로고
    • Deficiency of cardiomyocyte-specific microRNA-378 contributes to the development of cardiac fibrosis involving a transforming growth factor β1 (TGF-β1)-dependent paracrine mechanism
    • Nagalingam RS, Sundaresan NR, Noor M, Gupta MP, Solaro RJ, Gupta M. 2014. Deficiency of cardiomyocyte-specific microRNA-378 contributes to the development of cardiac fibrosis involving a transforming growth factor β1 (TGF-β1)-dependent paracrine mechanism. J Biol Chem 289: 27199–27214.
    • (2014) J Biol Chem , vol.289 , pp. 27199-27214
    • Nagalingam, R.S.1    Sundaresan, N.R.2    Noor, M.3    Gupta, M.P.4    Solaro, R.J.5    Gupta, M.6
  • 172
    • 78649661063 scopus 로고    scopus 로고
    • Requirement of TCF7L2 for TGF-β-dependent transcriptional activation of the TMEPAI gene
    • Nakano N, Itoh S, Watanabe Y, Maeyama K, Itoh F, Kato M. 2010. Requirement of TCF7L2 for TGF-β-dependent transcriptional activation of the TMEPAI gene. J Biol Chem 285: 38023–38033.
    • (2010) J Biol Chem , vol.285 , pp. 38023-38033
    • Nakano, N.1    Itoh, S.2    Watanabe, Y.3    Maeyama, K.4    Itoh, F.5    Kato, M.6
  • 175
    • 84877037101 scopus 로고    scopus 로고
    • Activin and TGF-β regulate expression of the microRNA-181 family to promote cell migration and invasion in breast cancer cells
    • Neel JC, Lebrun JJ. 2013. Activin and TGF-β regulate expression of the microRNA-181 family to promote cell migration and invasion in breast cancer cells. Cell Signal 25: 1556–1566.
    • (2013) Cell Signal , vol.25 , pp. 1556-1566
    • Neel, J.C.1    Lebrun, J.J.2
  • 176
    • 84873574889 scopus 로고    scopus 로고
    • MicroRNA-92a upholds Bmp signaling by targeting noggin3 during pharyngeal cartilage formation
    • Ning G, Liu X, Dai M, Meng A, Wang Q. 2013. MicroRNA-92a upholds Bmp signaling by targeting noggin3 during pharyngeal cartilage formation. Dev Cell 24: 283–295.
    • (2013) Dev Cell , vol.24 , pp. 283-295
    • Ning, G.1    Liu, X.2    Dai, M.3    Meng, A.4    Wang, Q.5
  • 177
    • 14644396524 scopus 로고    scopus 로고
    • Dynamics and interaction of caveolin-1 isoforms with BMP-receptors
    • Nohe A, Keating E, Underhill TM, Knaus P, Petersen NO. 2005. Dynamics and interaction of caveolin-1 isoforms with BMP-receptors. J Cell Sci 118: 643–650.
    • (2005) J Cell Sci , vol.118 , pp. 643-650
    • Nohe, A.1    Keating, E.2    Underhill, T.M.3    Knaus, P.4    Petersen, N.O.5
  • 181
    • 14844364701 scopus 로고    scopus 로고
    • Regulation of the polarity protein Par6 by TGF-β receptors controls epithelial cell plasticity
    • Ozdamar B, Bose R, Barrios-Rodiles M, Wang HR, Zhang Y, Wrana JL. 2005. Regulation of the polarity protein Par6 by TGF-β receptors controls epithelial cell plasticity. Science 307: 1603–1609.
    • (2005) Science , vol.307 , pp. 1603-1609
    • Ozdamar, B.1    Bose, R.2    Barrios-Rodiles, M.3    Wang, H.R.4    Zhang, Y.5    Wrana, J.L.6
  • 185
    • 0034460336 scopus 로고    scopus 로고
    • Transforming growth factor β-independent shuttling of Smad4 between the cytoplasm and nucleus
    • Pierreux CE, Nicolas FJ, Hill CS. 2000. Transforming growth factor β-independent shuttling of Smad4 between the cytoplasm and nucleus. Mol Cell Biol 20: 9041–9054.
    • (2000) Mol Cell Biol , vol.20 , pp. 9041-9054
    • Pierreux, C.E.1    Nicolas, F.J.2    Hill, C.S.3
  • 186
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation. “Protein modifications: Beyond the usual suspects” review series
    • Rabut G, Peter M. 2008. Function and regulation of protein neddylation. “Protein modifications: Beyond the usual suspects” review series. EMBO Rep 9: 969–976.
    • (2008) EMBO Rep , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 187
    • 77649242925 scopus 로고    scopus 로고
    • Targeting of SMAD5 links microRNA-155 to the TGF-β pathway and lymphomagenesis
    • Rai D, Kim SW, McKeller MR, Dahia PL, Aguiar RC. 2010. Targeting of SMAD5 links microRNA-155 to the TGF-β pathway and lymphomagenesis. Proc Natl Acad Sci 107: 3111–3116.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 3111-3116
    • Rai, D.1    Kim, S.W.2    McKeller, M.R.3    Dahia, P.L.4    Aguiar, R.C.5
  • 188
    • 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
    • Razani B, Zhang XL, Bitzer M, von Gersdorff G, Bottinger EP, Lisanti MP. 2001. Caveolin-1 regulates transforming growth factor (TGF)-β/SMAD signaling through an interaction with the TGF-β type I receptor. J Biol Chem 276: 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
  • 190
    • 0038400997 scopus 로고    scopus 로고
    • In or out? The dynamics of Smad nucleocytoplasmic shuttling
    • Reguly T, Wrana JL. 2003. In or out? The dynamics of Smad nucleocytoplasmic shuttling. Trends Cell Biol 13: 216– 220.
    • (2003) Trends Cell Biol , vol.13
    • Reguly, T.1    Wrana, J.L.2
  • 191
    • 2342647439 scopus 로고    scopus 로고
    • PKB/Akt modulates TGF-β signalling through a direct interaction with Smad3
    • Remy I, Montmarquette A, Michnick SW. 2004. PKB/Akt modulates TGF-β signalling through a direct interaction with Smad3. Nat Cell Biol 6: 358–365.
    • (2004) Nat Cell Biol , vol.6 , pp. 358-365
    • Remy, I.1    Montmarquette, A.2    Michnick, S.W.3
  • 192
    • 68949169031 scopus 로고    scopus 로고
    • MicroRNA-23b cluster micro-RNAs regulate transforming growth factor-β/bone morphogenetic protein signaling and liver stem cell differentiation by targeting Smads
    • Rogler CE, Levoci L, Ader T, Massimi A, Tchaikovskaya T, Norel R, Rogler LE. 2009. MicroRNA-23b cluster micro-RNAs regulate transforming growth factor-β/bone morphogenetic protein signaling and liver stem cell differentiation by targeting Smads. Hepatology 50: 575–584.
    • (2009) Hepatology , vol.50 , pp. 575-584
    • Rogler, C.E.1    Levoci, L.2    Ader, T.3    Massimi, A.4    Tchaikovskaya, T.5    Norel, R.6    Rogler, L.E.7
  • 194
    • 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 AH, Massagué 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    Massagué, J.6
  • 195
    • 64949115943 scopus 로고    scopus 로고
    • Bone morphogenetic protein-2 down-regulates miR-206 expression by blocking its maturation process
    • Sato MM, Nashimoto M, Katagiri T, Yawaka Y, Tamura M. 2009. Bone morphogenetic protein-2 down-regulates miR-206 expression by blocking its maturation process. Biochem Biophys Res Commun 383: 125–129.
    • (2009) Biochem Biophys Res Commun , vol.383 , pp. 125-129
    • Sato, M.M.1    Nashimoto, M.2    Katagiri, T.3    Yawaka, Y.4    Tamura, M.5
  • 196
    • 84884724979 scopus 로고    scopus 로고
    • Phosphatidyli-nositol 3-phosphate, a lipid that regulates membrane dynamics, protein sorting and cell signalling
    • Schink KO, Raiborg C, Stenmark H. 2013. Phosphatidyli-nositol 3-phosphate, a lipid that regulates membrane dynamics, protein sorting and cell signalling. BioEssays 35: 900–912.
    • (2013) Bioessays , vol.35 , pp. 900-912
    • Schink, K.O.1    Raiborg, C.2    Stenmark, H.3
  • 197
    • 44349125602 scopus 로고    scopus 로고
    • Mathematical modeling identifies Smad nucleocytoplasmic shuttling as a dynamic signal-interpreting system
    • Schmierer B, Tournier AL, Bates PA, Hill CS. 2008. Mathematical modeling identifies Smad nucleocytoplasmic shuttling as a dynamic signal-interpreting system. Proc Natl Acad Sci 105: 6608–6613.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 6608-6613
    • Schmierer, B.1    Tournier, A.L.2    Bates, P.A.3    Hill, C.S.4
  • 198
    • 0035834658 scopus 로고    scopus 로고
    • Endofin, an endosomal FYVE domain protein
    • Seet LF, Hong W. 2001. Endofin, an endosomal FYVE domain protein. J Biol Chem 276: 42445–42454.
    • (2001) J Biol Chem , vol.276 , pp. 42445-42454
    • Seet, L.F.1    Hong, W.2
  • 200
    • 10744228797 scopus 로고    scopus 로고
    • Identification of BMP and activin membrane-bound inhibitor (BAMBI), an inhibitor of transforming growth factor-β signaling, as a target of the β-catenin pathway in colorectal tumor cells
    • Sekiya T, Adachi S, Kohu K, Yamada T, Higuchi O, Furukawa Y, Nakamura Y, Nakamura T, Tashiro K, Kuhara S, et al. 2004a. Identification of BMP and activin membrane-bound inhibitor (BAMBI), an inhibitor of transforming growth factor-β signaling, as a target of the β-catenin pathway in colorectal tumor cells. J Biol Chem 279: 6840–6846.
    • (2004) J Biol Chem , vol.279 , pp. 6840-6846
    • Sekiya, T.1    Adachi, S.2    Kohu, K.3    Yamada, T.4    Higuchi, O.5    Furukawa, Y.6    Nakamura, Y.7    Nakamura, T.8    Tashiro, K.9    Kuhara, S.10
  • 201
    • 3042801616 scopus 로고    scopus 로고
    • Transcriptional regulation of the TGF-β pseudoreceptor BAMBI by TGF-β signaling
    • Sekiya T, Oda T, Matsuura K, Akiyama T. 2004b. Transcriptional regulation of the TGF-β pseudoreceptor BAMBI by TGF-β signaling. Biochem Biophys Res Commun 320: 680–684.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 680-684
    • Sekiya, T.1    Oda, T.2    Matsuura, K.3    Akiyama, T.4
  • 202
    • 84860488299 scopus 로고    scopus 로고
    • Guertl B. 2012. miR-192, miR-194, miR-215, miR-200c and miR-141 are downregulated and their common target ACVR2B is strongly expressed in renal childhood neoplasms
    • Senanayake U, Das S, Vesely P, Alzoughbi W, Frohlich LF, Chowdhury P, Leuschner I, Hoefler G, Guertl B. 2012. miR-192, miR-194, miR-215, miR-200c and miR-141 are downregulated and their common target ACVR2B is strongly expressed in renal childhood neoplasms. Carcinogenesis 33: 1014–1021.
    • Carcinogenesis , vol.33 , pp. 1014-1021
    • Senanayake, U.1    Das, S.2    Vesely, P.3    Alzoughbi, W.4    Frohlich, L.F.5    Chowdhury, P.6    Leuschner, I.7    Hoefler, G.8
  • 203
    • 1642332084 scopus 로고    scopus 로고
    • Integration of Smad and forkhead pathways in the control of neuroepithelial and glioblastoma cell proliferation
    • Seoane J, Le HV, Shen L, Anderson SA, Massagué J. 2004. Integration of Smad and forkhead pathways in the control of neuroepithelial and glioblastoma cell proliferation. Cell 117: 211–223.
    • (2004) Cell , vol.117 , pp. 211-223
    • Seoane, J.1    Le, H.V.2    Shen, L.3    Anderson, S.A.4    Massagué, J.5
  • 206
    • 84931267425 scopus 로고    scopus 로고
    • Human ortholog of Drosophila Melted impedes SMAD2 release from TGF-β receptor I to inhibit TGF-β signaling
    • Shathasivam P, Kollara A, Ringuette MJ, Virtanen C, Wrana JL, Brown TJ. 2015. Human ortholog of Drosophila Melted impedes SMAD2 release from TGF-β receptor I to inhibit TGF-β signaling. Proc Natl Acad Sci 112: 3000–3009.
    • (2015) Proc Natl Acad Sci , vol.112 , pp. 3000-3009
    • Shathasivam, P.1    Kollara, A.2    Ringuette, M.J.3    Virtanen, C.4    Wrana, J.L.5    Brown, T.J.6
  • 208
    • 84901844054 scopus 로고    scopus 로고
    • Specific control of BMP signaling and mesenchymal differentiation by cytoplasmic phosphatase PPM1H
    • Shen T, Sun C, Zhang Z, Xu N, Duan X, Feng XH, Lin X. 2014. Specific control of BMP signaling and mesenchymal differentiation by cytoplasmic phosphatase PPM1H. Cell Res 24: 724–741.
    • (2014) Cell Res , vol.24 , pp. 724-741
    • Shen, T.1    Sun, C.2    Zhang, Z.3    Xu, N.4    Duan, X.5    Feng, X.H.6    Lin, X.7
  • 209
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi Y, Massagué 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    Massagué, J.2
  • 210
    • 1642539976 scopus 로고    scopus 로고
    • GADD34-PP1c recruited by Smad7 dephosphorylates TGF-β type I receptor
    • Shi W, Sun C, He B, Xiong W, Shi X, Yao D, Cao X. 2004. GADD34-PP1c recruited by Smad7 dephosphorylates TGF-β 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
  • 211
    • 34248231196 scopus 로고    scopus 로고
    • Endofin acts as a Smad anchor for receptor activation in BMP signaling
    • Shi W, Chang C, Nie S, Xie S, Wan M, Cao X. 2007. Endofin acts as a Smad anchor for receptor activation in BMP signaling. J Cell Sci 120: 1216–1224.
    • (2007) J Cell Sci , vol.120 , pp. 1216-1224
    • Shi, W.1    Chang, C.2    Nie, S.3    Xie, S.4    Wan, M.5    Cao, X.6
  • 212
    • 41949094640 scopus 로고    scopus 로고
    • Ubc9 promotes the stability of Smad4 and the nuclear accumulation of Smad1 in osteoblast-like Saos-2 cells
    • Shimada K, Suzuki N, Ono Y, Tanaka K, Maeno M, Ito K. 2008. Ubc9 promotes the stability of Smad4 and the nuclear accumulation of Smad1 in osteoblast-like Saos-2 cells. Bone 42: 886–893.
    • (2008) Bone , vol.42 , pp. 886-893
    • Shimada, K.1    Suzuki, N.2    Ono, Y.3    Tanaka, K.4    Maeno, M.5    Ito, K.6
  • 213
    • 77951964981 scopus 로고    scopus 로고
    • Posttranscriptional regulation of microRNA biogenesis in animals
    • Siomi H, Siomi MC. 2010. Posttranscriptional regulation of microRNA biogenesis in animals. Mol Cell 38: 323–332.
    • (2010) Mol Cell , vol.38 , pp. 323-332
    • Siomi, H.1    Siomi, M.C.2
  • 214
    • 84872790880 scopus 로고    scopus 로고
    • MicroRNA miR-98 inhibits tumor angiogenesis and invasion by targeting activin receptor-like kinase-4 and matrix metalloprotein-ase-11
    • Siragam V, Rutnam ZJ, Yang W, Fang L, Luo L, Yang X, Li M, Deng Z, Qian J, Peng C, et al. 2012. MicroRNA miR-98 inhibits tumor angiogenesis and invasion by targeting activin receptor-like kinase-4 and matrix metalloprotein-ase-11. Oncotarget 3: 1370–1385.
    • (2012) Oncotarget , vol.3 , pp. 1370-1385
    • Siragam, V.1    Rutnam, Z.J.2    Yang, W.3    Fang, L.4    Luo, L.5    Yang, X.6    Li, M.7    Deng, Z.8    Qian, J.9    Peng, C.10
  • 215
    • 84863232852 scopus 로고    scopus 로고
    • ACVR1, a therapeutic target of fibrodysplasia ossificans progressiva, is negatively regulated by miR-148a
    • Song H, Wang Q, Wen J, Liu S, Gao X, Cheng J, Zhang D. 2012. ACVR1, a therapeutic target of fibrodysplasia ossificans progressiva, is negatively regulated by miR-148a. Int J Mol Sci 13: 2063–2077.
    • (2012) Int J Mol Sci , vol.13 , pp. 2063-2077
    • Song, H.1    Wang, Q.2    Wen, J.3    Liu, S.4    Gao, X.5    Cheng, J.6    Zhang, D.7
  • 216
    • 0029959774 scopus 로고    scopus 로고
    • Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses
    • Souchelnytskyi S, ten Dijke P, Miyazono K, Heldin CH. 1996. Phosphorylation of Ser165 in TGF-β type I receptor modulates TGF-β1-induced cellular responses. EMBO J 15: 6231–6240.
    • (1996) EMBO J , vol.15 , pp. 6231-6240
    • Souchelnytskyi, S.1    Ten Dijke, P.2    Miyazono, K.3    Heldin, C.H.4
  • 217
    • 0030613262 scopus 로고    scopus 로고
    • Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling
    • Souchelnytskyi S, Tamaki K, Engstrom U, Wernstedt C, ten Dijke P, Heldin CH. 1997. Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-β signaling. J Biol Chem 272: 28107–28115.
    • (1997) J Biol Chem , vol.272 , pp. 28107-28115
    • Souchelnytskyi, S.1    Tamaki, K.2    Engstrom, U.3    Wernstedt, C.4    Ten Dijke, P.5    Heldin, C.H.6
  • 219
    • 0037238014 scopus 로고    scopus 로고
    • Temporal and spatial parameters of skeletal gene expression: Targeting RUNX factors and their coregulatory proteins to subnuclear domains
    • Stein GS, Lian JB, Stein JL, van Wijnen AJ, Choi JY, Pratap J, Zaidi SK. 2003. Temporal and spatial parameters of skeletal gene expression: Targeting RUNX factors and their coregulatory proteins to subnuclear domains. Connect Tissue Res 44: 149–153.
    • (2003) Connect Tissue Res , vol.44 , pp. 149-153
    • Stein, G.S.1    Lian, J.B.2    Stein, J.L.3    Van Wijnen, A.J.4    Choi, J.Y.5    Pratap, J.6    Zaidi, S.K.7
  • 220
    • 0035498980 scopus 로고    scopus 로고
    • Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN
    • Stroschein SL, Bonni S, Wrana JL, Luo K. 2001. Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN. Genes Dev 15: 2822–2836.
    • (2001) Genes Dev , vol.15 , pp. 2822-2836
    • Stroschein, S.L.1    Bonni, S.2    Wrana, J.L.3    Luo, K.4
  • 221
    • 33847379496 scopus 로고    scopus 로고
    • The evolutionally conserved activity of Dapper2 in antagonizing TGF-β signaling
    • Su Y, Zhang L, Gao X, Meng F, Wen J, Zhou H, Meng A, Chen YG. 2007. The evolutionally conserved activity of Dapper2 in antagonizing TGF-β signaling. FASEB J 21: 682– 690.
    • (2007) FASEB J , vol.21
    • 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
  • 223
    • 80054771082 scopus 로고    scopus 로고
    • Low-dose paclitaxel ameliorates fibrosis in the remnant kidney model by down-regulating miR-192
    • Sun L, Zhang D, Liu F, Xiang X, Ling G, Xiao L, Liu Y, Zhu X, Zhan M, Yang Y, et al. 2011. Low-dose paclitaxel ameliorates fibrosis in the remnant kidney model by down-regulating miR-192. J Pathol 225: 364–377.
    • (2011) J Pathol , vol.225 , pp. 364-377
    • Sun, L.1    Zhang, D.2    Liu, F.3    Xiang, X.4    Ling, G.5    Xiao, L.6    Liu, Y.7    Zhu, X.8    Zhan, M.9    Yang, Y.10
  • 227
    • 82455210962 scopus 로고    scopus 로고
    • Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3
    • Tang LY, Yamashita M, Coussens NP, Tang Y, Wang X, Li C, Deng CX, Cheng SY, Zhang YE. 2011. Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3. EMBO J 30: 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
  • 228
    • 58149272219 scopus 로고    scopus 로고
    • The Smad family
    • ten Dijke P, Heldin CH, Springer, Dordrecht, The Netherlands
    • ten Dijke P, Heldin CH. 2006. The Smad family. In Smad Signal Transduction, Vol. 5 (ed. ten Dijke P, Heldin CH), pp. 1–13. Springer, Dordrecht, The Netherlands.
    • (2006) Smad Signal Transduction , vol.5 , pp. 1-13
    • Ten Dijke, P.1    Heldin, C.H.2
  • 229
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien CB, Langdon WY. 2001. Cbl: Many adaptations to regulate protein tyrosine kinases. Nat Rev Mol Cell Biol 2: 294–307.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 230
    • 84861968669 scopus 로고    scopus 로고
    • TGF-β-dependent active demethylation and expression of the p15ink4b tumor suppressor are impaired by the ZNF217/CoREST complex
    • Thillainadesan G, Chitilian JM, Isovic M, Ablack JN, Mym-ryk JS, Tini M, Torchia J. 2012. TGF-β-dependent active demethylation and expression of the p15ink4b tumor suppressor are impaired by the ZNF217/CoREST complex. Mol Cell 46: 636–649.
    • (2012) Mol Cell , vol.46 , pp. 636-649
    • Thillainadesan, G.1    Chitilian, J.M.2    Isovic, M.3    Ablack, J.N.4    Mym-Ryk, J.S.5    Tini, M.6    Torchia, J.7
  • 231
    • 84892628912 scopus 로고    scopus 로고
    • Mir-20a regulates in vitro mineralization and BMP signaling pathway by targeting BMP-2 transcript in fish
    • Tiago DM, Marques CL, Roberto VP, Cancela ML, Laize V. 2014. Mir-20a regulates in vitro mineralization and BMP signaling pathway by targeting BMP-2 transcript in fish. Arch Biochem Biophys 543: 23–30.
    • (2014) Arch Biochem Biophys , vol.543 , pp. 23-30
    • Tiago, D.M.1    Marques, C.L.2    Roberto, V.P.3    Cancela, M.L.4    Laize, V.5
  • 233
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGF-β receptor
    • Tsukazaki T, Chiang TA, Davison AF, Attisano L, Wrana JL. 1998. SARA, a FYVE domain protein that recruits Smad2 to the TGF-β receptor. Cell 95: 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
  • 234
    • 84897481114 scopus 로고    scopus 로고
    • Li QF. 2014. miR-34a targets the inhibin βB gene, promoting granulosa cell apoptosis in the porcine ovary
    • Tu F, Pan ZX, Yao Y, Liu HL, Liu SR, Xie Z, Li QF. 2014. miR-34a targets the inhibin βB gene, promoting granulosa cell apoptosis in the porcine ovary. Genet Mol Res 13: 2504– 2512.
    • Genet Mol Res , vol.13
    • Tu, F.1    Pan, Z.X.2    Yao, Y.3    Liu, H.L.4    Liu, S.R.5    Xie, Z.6
  • 240
    • 38349146518 scopus 로고    scopus 로고
    • MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4
    • Wang Q, Huang Z, Xue H, Jin C, Ju XL, Han JD, Chen YG. 2008. MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4. Blood 111: 588–595.
    • (2008) Blood , vol.111 , pp. 588-595
    • Wang, Q.1    Huang, Z.2    Xue, H.3    Jin, C.4    Ju, X.L.5    Han, J.D.6    Chen, Y.G.7
  • 241
    • 65649084845 scopus 로고    scopus 로고
    • Transforming growth factor-β-inducible phosphorylation of Smad3
    • Wang G, Matsuura I, He D, Liu F. 2009. Transforming growth factor-β-inducible phosphorylation of Smad3. J Biol Chem 284: 9663–9673.
    • (2009) J Biol Chem , vol.284 , pp. 9663-9673
    • Wang, G.1    Matsuura, I.2    He, D.3    Liu, F.4
  • 242
    • 77950095763 scopus 로고    scopus 로고
    • TGF-β-mediated upregulation of hepatic miR-181b promotes hepatocarcinogenesis by targeting TIMP3
    • Wang B, Hsu SH, Majumder S, Kutay H, Huang W, Jacob ST, Ghoshal K. 2010a. TGF-β-mediated upregulation of hepatic miR-181b promotes hepatocarcinogenesis by targeting TIMP3. Oncogene 29: 1787–1797.
    • (2010) Oncogene , vol.29 , pp. 1787-1797
    • Wang, B.1    Hsu, S.H.2    Majumder, S.3    Kutay, H.4    Huang, W.5    Jacob, S.T.6    Ghoshal, K.7
  • 243
    • 77957265786 scopus 로고    scopus 로고
    • miR-106b aberrantly expressed in a double transgenic mouse model for Alzheimer’s disease targets TGF-β type II receptor
    • Wang H, Liu J, Zong Y, Xu Y, Deng W, Zhu H, Liu Y, Ma C, Huang L, Zhang L, et al. 2010b. miR-106b aberrantly expressed in a double transgenic mouse model for Alzheimer’s disease targets TGF-β type II receptor. Brain Res 1357: 166–174.
    • (2010) Brain Res , vol.1357 , pp. 166-174
    • Wang, H.1    Liu, J.2    Zong, Y.3    Xu, Y.4    Deng, W.5    Zhu, H.6    Liu, Y.7    Ma, C.8    Huang, L.9    Zhang, L.10
  • 244
    • 84874547217 scopus 로고    scopus 로고
    • MicroRNA-204-5p regulates epithelial-to-mesen-chymal transition during human posterior capsule opacification by targeting SMAD4
    • Wang Y, Li W, Zang X, Chen N, Liu T, Tsonis PA, Huang Y. 2013. MicroRNA-204-5p regulates epithelial-to-mesen-chymal transition during human posterior capsule opacification by targeting SMAD4. Invest Ophthalmol Vis Sci 54: 323–332.
    • (2013) Invest Ophthalmol Vis Sci , vol.54 , pp. 323-332
    • Wang, Y.1    Li, W.2    Zang, X.3    Chen, N.4    Liu, T.5    Tsonis, P.A.6    Huang, Y.7
  • 245
    • 0034252221 scopus 로고    scopus 로고
    • Regulation of intracellular dynamics of Smad4 by its leucine-rich nuclear export signal
    • Watanabe M, Masuyama N, Fukuda M, 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
  • 246
    • 73649085521 scopus 로고    scopus 로고
    • TME-PAI, a transmembrane TGF-β-inducible protein, sequesters Smad proteins from active participation in TGF-β signaling
    • Watanabe Y, Itoh S, Goto T, Ohnishi E, Inamitsu M, Itoh F, Satoh K, Wiercinska E, Yang W, Shi L, et al. 2010. TME-PAI, a transmembrane TGF-β-inducible protein, sequesters Smad proteins from active participation in TGF-β signaling. Mol Cell 37: 123–134.
    • (2010) Mol Cell , vol.37 , pp. 123-134
    • Watanabe, Y.1    Itoh, S.2    Goto, T.3    Ohnishi, E.4    Inamitsu, M.5    Itoh, F.6    Satoh, K.7    Wiercinska, E.8    Yang, W.9    Shi, L.10
  • 247
    • 79751469547 scopus 로고    scopus 로고
    • NEDD8 pathways in cancer, Sine Quibus Non
    • Watson IR, Irwin MS, Ohh M. 2011. NEDD8 pathways in cancer, Sine Quibus Non. Cancer Cell 19: 168–176.
    • (2011) Cancer Cell , vol.19 , pp. 168-176
    • Watson, I.R.1    Irwin, M.S.2    Ohh, M.3
  • 249
    • 27944498719 scopus 로고    scopus 로고
    • The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signalling
    • Wicks SJ, Haros K, Maillard M, Song L, Cohen RE, Dijke PT, Chantry A. 2005. The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signalling. Oncogene 24: 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
  • 250
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex
    • Wieser R, Wrana JL, Massagué J. 1995. GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex. EMBO J 14: 2199–2208.
    • (1995) EMBO J , vol.14 , pp. 2199-2208
    • Wieser, R.1    Wrana, J.L.2    Massagué, J.3
  • 251
    • 0029985652 scopus 로고    scopus 로고
    • Formation and activation by phosphorylation of activin receptor complexes
    • Willis SA, Zimmerman CM, Li LI, Mathews LS. 1996. Formation and activation by phosphorylation of activin receptor complexes. Mol Endocrinol 10: 367–379.
    • (1996) Mol Endocrinol , vol.10 , pp. 367-379
    • Willis, S.A.1    Zimmerman, C.M.2    Li, L.I.3    Mathews, L.S.4
  • 254
    • 48249099342 scopus 로고    scopus 로고
    • Critical regulation of TGF-β signaling by Hsp90
    • Wrighton KH, Lin X, Feng XH. 2008. Critical regulation of TGF-β signaling by Hsp90. Proc Natl Acad Sci 105: 9244–9249.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 9244-9249
    • Wrighton, K.H.1    Lin, X.2    Feng, X.H.3
  • 256
    • 84863263055 scopus 로고    scopus 로고
    • Huang H. 2012. miR-30 family members negatively regulate osteoblast differentiation
    • Wu T, Zhou H, Hong Y, Li J, Jiang X, Huang H. 2012. miR-30 family members negatively regulate osteoblast differentiation. J Biol Chem 287: 7503–7511.
    • J Biol Chem , vol.287 , pp. 7503-7511
    • Wu, T.1    Zhou, H.2    Hong, Y.3    Li, J.4    Jiang, X.5
  • 258
    • 0034604343 scopus 로고    scopus 로고
    • Importin β mediates nuclear translocation of Smad 3
    • Xiao Z, Liu X, Lodish HF. 2000. Importin β mediates nuclear translocation of Smad 3. J Biol Chem 275: 23425– 23428.
    • (2000) J Biol Chem , vol.275
    • Xiao, Z.1    Liu, X.2    Lodish, H.F.3
  • 259
    • 0347664883 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of Smad1 conferred by its nuclear localization and nuclear export signals
    • Xiao Z, Watson N, Rodriguez C, Lodish HF. 2001. Nucleocytoplasmic shuttling of Smad1 conferred by its nuclear localization and nuclear export signals. J Biol Chem 276: 39404–39410.
    • (2001) J Biol Chem , vol.276 , pp. 39404-39410
    • Xiao, Z.1    Watson, N.2    Rodriguez, C.3    Lodish, H.F.4
  • 260
    • 0141706697 scopus 로고    scopus 로고
    • A novel nuclear export signal in Smad1 is essential for its signaling activity
    • Xiao Z, Brownawell AM, Macara IG, Lodish HF. 2003a. A novel nuclear export signal in Smad1 is essential for its signaling activity. J Biol Chem 278: 34245–34252.
    • (2003) J Biol Chem , vol.278 , pp. 34245-34252
    • Xiao, Z.1    Brownawell, A.M.2    Macara, I.G.3    Lodish, H.F.4
  • 261
    • 0037455715 scopus 로고    scopus 로고
    • An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity
    • Xiao Z, Latek R, Lodish HF. 2003b. An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity. Oncogene 22: 1057–1069.
    • (2003) Oncogene , vol.22 , pp. 1057-1069
    • Xiao, Z.1    Latek, R.2    Lodish, H.F.3
  • 262
    • 70349436102 scopus 로고    scopus 로고
    • Induction of microRNA-155 during Helicobacter pylori infection and its negative regulatory role in the inflammatory response
    • Xiao B, Liu Z, Li BS, Tang B, Li W, Guo G, Shi Y, Wang F, Wu Y, Tong WD, et al. 2009. Induction of microRNA-155 during Helicobacter pylori infection and its negative regulatory role in the inflammatory response. J Infect Dis 200: 916–925.
    • (2009) J Infect Dis , vol.200 , pp. 916-925
    • Xiao, B.1    Liu, Z.2    Li, B.S.3    Tang, B.4    Li, W.5    Guo, G.6    Shi, Y.7    Wang, F.8    Wu, Y.9    Tong, W.D.10
  • 263
    • 1542284152 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of signal transducers
    • Xu L, Massagué J. 2004. Nucleocytoplasmic shuttling of signal transducers. Nat Rev Mol Cell Biol 5: 209–219.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 209-219
    • Xu, L.1    Massagué, J.2
  • 264
    • 0034253480 scopus 로고    scopus 로고
    • The nuclear import function of Smad2 is masked by SARA and unmasked by TGF-β-dependent phosphorylation
    • Xu L, Chen YG, Massagué J. 2000. The nuclear import function of Smad2 is masked by SARA and unmasked by TGF-β-dependent phosphorylation. Nat Cell Biol 2: 559–562.
    • (2000) Nat Cell Biol , vol.2 , pp. 559-562
    • Xu, L.1    Chen, Y.G.2    Massagué, J.3
  • 265
    • 0036670359 scopus 로고    scopus 로고
    • Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGF-β signaling complexes in the cytoplasm and nucleus
    • Xu L, Kang Y, Col S, Massagué J. 2002. Smad2 nucleocytoplasmic shuttling by nucleoporins CAN/Nup214 and Nup153 feeds TGF-β 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    Massagué, J.4
  • 266
    • 0142211206 scopus 로고    scopus 로고
    • Distinct domain utilization by Smad3 and Smad4 for nucleoporin interaction and nuclear import
    • Xu L, Alarcon C, Col S, Massagué J. 2003. Distinct domain utilization by Smad3 and Smad4 for nucleoporin interaction and nuclear import. J Biol Chem 278: 42569–42577.
    • (2003) J Biol Chem , vol.278 , pp. 42569-42577
    • Xu, L.1    Alarcon, C.2    Col, S.3    Massagué, J.4
  • 267
    • 34548842261 scopus 로고    scopus 로고
    • Msk is required for nuclear import of TGF-β/BMP-activated Smads
    • Xu L, Yao X, Chen X, Lu P, Zhang B, Ip YT. 2007. Msk is required for nuclear import of TGF-β/BMP-activated Smads. J Cell Biol 178: 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
  • 268
    • 84862765059 scopus 로고    scopus 로고
    • Post-translational regulation of TGF-β receptor and Smad signaling
    • Xu P, Liu J, Derynck R. 2012. Post-translational regulation of TGF-β receptor and Smad signaling. FEBS Lett 586: 1871–1884.
    • (2012) FEBS Lett , vol.586 , pp. 1871-1884
    • Xu, P.1    Liu, J.2    Derynck, R.3
  • 269
    • 33745197796 scopus 로고    scopus 로고
    • FKBP12 functions as an adaptor of the Smad7–Smurf1 complex on activin type I receptor
    • Yamaguchi T, Kurisaki A, Yamakawa N, Minakuchi K, Sugino H. 2006. FKBP12 functions as an adaptor of the Smad7–Smurf1 complex on activin type I receptor. J Mol Endocrinol 36: 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
  • 270
    • 0037007204 scopus 로고    scopus 로고
    • The rasGAP-binding protein, Dok-1, mediates activin signaling via serine/threonine kinase receptors
    • Yamakawa N, Tsuchida K, Sugino H. 2002. The rasGAP-binding protein, Dok-1, mediates activin signaling via serine/threonine kinase receptors. EMBO J 21: 1684–1694.
    • (2002) EMBO J , vol.21 , pp. 1684-1694
    • Yamakawa, N.1    Tsuchida, K.2    Sugino, H.3
  • 271
    • 0027930903 scopus 로고
    • Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-β
    • Yamashita H, ten Dijke P, Franzen P, Miyazono K, Heldin CH. 1994. Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-β. J Biol Chem 269: 20172–20178.
    • (1994) J Biol Chem , vol.269 , pp. 20172-20178
    • Yamashita, H.1    Ten Dijke, P.2    Franzen, P.3    Miyazono, K.4    Heldin, C.H.5
  • 273
    • 79251556820 scopus 로고    scopus 로고
    • Smad7: Not only a regulator, but also a cross-talk mediator of TGF-β signalling
    • Yan X, Chen YG. 2011. Smad7: Not only a regulator, but also a cross-talk mediator of TGF-β signalling. Biochem J 434: 1–10.
    • (2011) Biochem J , vol.434 , pp. 1-10
    • Yan, X.1    Chen, Y.G.2
  • 274
    • 71049139747 scopus 로고    scopus 로고
    • Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-β signaling
    • Yan X, Lin Z, Chen F, Zhao X, Chen H, Ning Y, Chen YG. 2009. Human BAMBI cooperates with Smad7 to inhibit transforming growth factor-β signaling. J Biol Chem 284: 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
  • 275
    • 80052572648 scopus 로고    scopus 로고
    • TSC-22 promotes transforming growth factor β-mediated cardiac myofibroblast differentiation by antagonizing Smad7 activity
    • Yan X, Zhang J, Pan L, Wang P, Xue H, Zhang L, Gao X, Zhao X, Ning Y, Chen YG. 2011. TSC-22 promotes transforming growth factor β-mediated cardiac myofibroblast differentiation by antagonizing Smad7 activity. Mol Cell Biol 31: 3700–3709.
    • (2011) Mol Cell Biol , vol.31 , pp. 3700-3709
    • Yan, X.1    Zhang, J.2    Pan, L.3    Wang, P.4    Xue, H.5    Zhang, L.6    Gao, X.7    Zhao, X.8    Ning, Y.9    Chen, Y.G.10
  • 276
    • 84866627838 scopus 로고    scopus 로고
    • MicroRNA-145 suppresses mouse granulosa cell proliferation by targeting activin receptor IB
    • Yan G, Zhang L, Fang T, Zhang Q, Wu S, Jiang Y, Sun H, Hu Y. 2012. MicroRNA-145 suppresses mouse granulosa cell proliferation by targeting activin receptor IB. FEBS Lett 586: 3263–3270.
    • (2012) FEBS Lett , vol.586 , pp. 3263-3270
    • Yan, G.1    Zhang, L.2    Fang, T.3    Zhang, Q.4    Wu, S.5    Jiang, Y.6    Sun, H.7    Hu, Y.8
  • 277
    • 84870473950 scopus 로고    scopus 로고
    • DRAK2 participates in a negative feedback loop to control TGF-β/Smads signaling by binding to type I TGF-β receptor
    • Yang KM, Kim W, Bae E, Gim J, Weist BM, Jung Y, Hyun JS, Hernandez JB, Leem SH, Park T, et al. 2012. DRAK2 participates in a negative feedback loop to control TGF-β/Smads signaling by binding to type I TGF-β receptor. Cell Rep 2: 1286–1299.
    • (2012) Cell Rep , vol.2 , pp. 1286-1299
    • Yang, K.M.1    Kim, W.2    Bae, E.3    Gim, J.4    Weist, B.M.5    Jung, Y.6    Hyun, J.S.7    Hernandez, J.B.8    Leem, S.H.9    Park, T.10
  • 278
    • 84879607251 scopus 로고    scopus 로고
    • MicroRNA-140-5p suppresses tumor growth and metastasis by targeting transforming growth factor β receptor 1 and fibroblast growth factor 9 in hepatocellular carcinoma
    • Yang H, Fang F, Chang R, Yang L. 2013. MicroRNA-140-5p suppresses tumor growth and metastasis by targeting transforming growth factor β receptor 1 and fibroblast growth factor 9 in hepatocellular carcinoma. Hepatology 58: 205–217.
    • (2013) Hepatology , vol.58 , pp. 205-217
    • Yang, H.1    Fang, F.2    Chang, R.3    Yang, L.4
  • 279
    • 0034725060 scopus 로고    scopus 로고
    • FKBP12 is a negative regulator of transforming growth factor-β receptor internalization
    • Yao D, Dore JJ Jr, Leof EB. 2000. FKBP12 is a negative regulator of transforming growth factor-β receptor internalization. J Biol Chem 275: 13149–13154.
    • (2000) J Biol Chem , vol.275 , pp. 13149-13154
    • Yao, D.1    Dore, J.J.2    Leof, E.B.3
  • 280
    • 77249164641 scopus 로고    scopus 로고
    • MicroRNA-224 is involved in transforming growth fac-tor-β-mediated mouse granulosa cell proliferation and granulosa cell function by targeting Smad4
    • Yao G, Yin M, Lian J, Tian H, Liu L, Li X, Sun F. 2010. MicroRNA-224 is involved in transforming growth fac-tor-β-mediated mouse granulosa cell proliferation and granulosa cell function by targeting Smad4. Mol Endocrinol 24: 540–551.
    • (2010) Mol Endocrinol , vol.24 , pp. 540-551
    • Yao, G.1    Yin, M.2    Lian, J.3    Tian, H.4    Liu, L.5    Li, X.6    Sun, F.7
  • 281
    • 77953308345 scopus 로고    scopus 로고
    • MicroRNA miR-155 inhibits bone morphogenetic protein (BMP) signaling and BMP-mediated Epstein–Barr virus reactivation
    • Yin Q, Wang X, Fewell C, Cameron J, Zhu H, Baddoo M, Lin Z, Flemington EK. 2010. MicroRNA miR-155 inhibits bone morphogenetic protein (BMP) signaling and BMP-mediated Epstein–Barr virus reactivation. J Virol 84: 6318–6327.
    • (2010) J Virol , vol.84 , pp. 6318-6327
    • Yin, Q.1    Wang, X.2    Fewell, C.3    Cameron, J.4    Zhu, H.5    Baddoo, M.6    Lin, Z.7    Flemington, E.K.8
  • 282
    • 0037099745 scopus 로고    scopus 로고
    • TGF-β receptor-activated p38 MAP kinase mediates Smad-independent TGF-β responses
    • Yu L, Hebert MC, Zhang YE. 2002. TGF-β receptor-activated p38 MAP kinase mediates Smad-independent TGF-β responses. EMBO J 21: 3749–3759.
    • (2002) EMBO J , vol.21 , pp. 3749-3759
    • Yu, L.1    Hebert, M.C.2    Zhang, Y.E.3
  • 283
    • 77950874802 scopus 로고    scopus 로고
    • MTMR4 attenuates transforming growth factor β (TGF-β) signaling by dephosphorylating R-Smads in endosomes
    • Yu J, Pan L, Qin X, Chen H, Xu Y, Chen Y, Tang H. 2010. MTMR4 attenuates transforming growth factor β (TGF-β) 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
  • 284
    • 84872053875 scopus 로고    scopus 로고
    • Myotubularin-related protein 4 (MTMR4) attenuates BMP/Dpp signaling by dephosphorylation of Smad proteins
    • Yu J, He X, Chen YG, Hao Y, Yang S, Wang L, Pan L, Tang H. 2013. Myotubularin-related protein 4 (MTMR4) attenuates BMP/Dpp signaling by dephosphorylation of Smad proteins. J Biol Chem 288: 79–88.
    • (2013) J Biol Chem , vol.288 , pp. 79-88
    • Yu, J.1    He, X.2    Chen, Y.G.3    Hao, Y.4    Yang, S.5    Wang, L.6    Pan, L.7    Tang, H.8
  • 285
    • 84857940642 scopus 로고    scopus 로고
    • Ubc9 negatively regulates BMP-mediated osteoblastic differentiation in cultured cells
    • Yukita A, Hosoya A, Ito Y, Katagiri T, Asashima M, Nakamura H. 2012. Ubc9 negatively regulates BMP-mediated osteoblastic differentiation in cultured cells. Bone 50: 1092–1099.
    • (2012) Bone , vol.50 , pp. 1092-1099
    • Yukita, A.1    Hosoya, A.2    Ito, Y.3    Katagiri, T.4    Asashima, M.5    Nakamura, H.6
  • 288
    • 6044272725 scopus 로고    scopus 로고
    • Zebrafish Dpr2 inhibits mesoderm induction by promoting degradation of nodal receptors
    • Zhang L, Zhou H, Su Y, Sun Z, Zhang H, Zhang Y, Ning Y, Chen YG, Meng A. 2004. Zebrafish Dpr2 inhibits mesoderm induction by promoting degradation of nodal receptors. Science 306: 114–117.
    • (2004) Science , vol.306 , pp. 114-117
    • Zhang, L.1    Zhou, H.2    Su, Y.3    Sun, Z.4    Zhang, H.5    Zhang, Y.6    Ning, Y.7    Chen, Y.G.8    Meng, A.9
  • 289
    • 70349443042 scopus 로고    scopus 로고
    • Single-molecule imaging reveals transforming growth factor-β-induced type II receptor dimerization
    • Zhang W, Jiang Y, Wang Q, Ma X, Xiao Z, Zuo W, Fang X, Chen YG. 2009. Single-molecule imaging reveals transforming growth factor-β-induced type II receptor dimerization. Proc Natl Acad Sci 106: 15679–15683.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 15679-15683
    • Zhang, W.1    Jiang, Y.2    Wang, Q.3    Ma, X.4    Xiao, Z.5    Zuo, W.6    Fang, X.7    Chen, Y.G.8
  • 290
    • 78049467243 scopus 로고    scopus 로고
    • Monomeric type I and type III transforming growth factor-β receptors and their dimerization revealed by single-molecule imaging
    • Zhang W, Yuan J, Yang Y, Xu L, Wang Q, Zuo W, Fang X, Chen YG. 2010. Monomeric type I and type III transforming growth factor-β receptors and their dimerization revealed by single-molecule imaging. Cell Res 20: 1216–1223.
    • (2010) Cell Res , vol.20 , pp. 1216-1223
    • Zhang, W.1    Yuan, J.2    Yang, Y.3    Xu, L.4    Wang, Q.5    Zuo, W.6    Fang, X.7    Chen, Y.G.8
  • 293
    • 84875170985 scopus 로고    scopus 로고
    • MicroRNA-181a suppresses mouse granulosa cell proliferation by targeting activin receptor IIA
    • Zhang Q, Sun H, Jiang Y, Ding L, Wu S, Fang T, Yan G, Hu Y. 2013b. MicroRNA-181a suppresses mouse granulosa cell proliferation by targeting activin receptor IIA. PLoS ONE 8: e59667.
    • (2013) Plos ONE , vol.8
    • Zhang, Q.1    Sun, H.2    Jiang, Y.3    Ding, L.4    Wu, S.5    Fang, T.6    Yan, G.7    Hu, Y.8
  • 294
  • 295
    • 84867054072 scopus 로고    scopus 로고
    • PICK1 promotes caveolin-dependent degradation of TGF-β type I receptor
    • Zhao B, Wang Q, Du J, Luo S, Xia J, Chen YG. 2012. PICK1 promotes caveolin-dependent degradation of TGF-β type I receptor. Cell Res 22: 1467–1478.
    • (2012) Cell Res , vol.22 , pp. 1467-1478
    • Zhao, B.1    Wang, Q.2    Du, J.3    Luo, S.4    Xia, J.5    Chen, Y.G.6
  • 296
    • 84907210862 scopus 로고    scopus 로고
    • C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via Smad dephosphorylation
    • Zhao Y, Xiao M, Sun B, Zhang Z, Shen T, Duan X, Yu PB, Feng XH, Lin X. 2014. C-terminal domain (CTD) small phosphatase-like 2 modulates the canonical bone morphogenetic protein (BMP) signaling and mesenchymal differentiation via Smad dephosphorylation. J Biol Chem 289: 26441–26450.
    • (2014) J Biol Chem , vol.289 , pp. 26441-26450
    • Zhao, Y.1    Xiao, M.2    Sun, B.3    Zhang, Z.4    Shen, T.5    Duan, X.6    Yu, P.B.7    Feng, X.H.8    Lin, X.9
  • 297
  • 298
    • 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 JL, Thomsen GH. 1999. A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400: 687– 693.
    • (1999) Nature , vol.400
    • Zhu, H.1    Kavsak, P.2    Abdollah, S.3    Wrana, J.L.4    Thomsen, G.H.5
  • 299
    • 84873966593 scopus 로고    scopus 로고
    • Tollip, an intracellular trafficking protein, is a novel modulator of the transforming growth factor-β signaling pathway
    • Zhu L, Wang L, Luo X, Zhang Y, Ding Q, Jiang X, Wang X, Pan Y, Chen Y. 2012. Tollip, an intracellular trafficking protein, is a novel modulator of the transforming growth factor-β signaling pathway. J Biol Chem 287: 39653– 39663.
    • (2012) J Biol Chem , vol.287
    • Zhu, L.1    Wang, L.2    Luo, X.3    Zhang, Y.4    Ding, Q.5    Jiang, X.6    Wang, X.7    Pan, Y.8    Chen, Y.9
  • 300
    • 84906545323 scopus 로고    scopus 로고
    • MicroRNA-130a is up-regulated in mouse liver by iron deficiency and targets the bone morphogenetic protein (BMP) receptor ALK2 to attenuate BMP signaling and hepcidin transcription
    • Zumbrennen-Bullough KB, Wu Q, Core AB, Canali S, Chen W, Theurl I, Meynard D, Babitt JL. 2014. MicroRNA-130a is up-regulated in mouse liver by iron deficiency and targets the bone morphogenetic protein (BMP) receptor ALK2 to attenuate BMP signaling and hepcidin transcription. J Biol Chem 289: 23796–23808.
    • (2014) J Biol Chem , vol.289 , pp. 23796-23808
    • Zumbrennen-Bullough, K.B.1    Wu, Q.2    Core, A.B.3    Canali, S.4    Chen, W.5    Theurl, I.6    Meynard, D.7    Babitt, J.L.8
  • 301
    • 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
    • Zuo W, Chen YG. 2009. 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: 1020–1029.
    • (2009) Mol Biol Cell , vol.20 , pp. 1020-1029
    • Zuo, W.1    Chen, Y.G.2
  • 302
    • 84873438391 scopus 로고    scopus 로고
    • c-Cbl-mediated neddylation antagonizes ubiquitination and degradation of the TGF-β type II receptor
    • Zuo W, Huang F, Chiang YJ, Li M, Du J, Ding Y, Zhang T, Lee HW, Jeong LS, Chen Y, et al. 2013. c-Cbl-mediated neddylation antagonizes ubiquitination and degradation of the TGF-β type II receptor. Mol Cell 49: 499–510.
    • (2013) Mol Cell , vol.49 , pp. 499-510
    • Zuo, W.1    Huang, F.2    Chiang, Y.J.3    Li, M.4    Du, J.5    Ding, Y.6    Zhang, T.7    Lee, H.W.8    Jeong, L.S.9    Chen, Y.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.