Cited by 797TGF-β signaling in diseasesDevelopmental Biology and Gene RegulationSignaling Pathways in Disease

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Specificity, versatility, and control of TGF-β family signaling

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Derynck, Rik, Budi, Erine H.·2019·Science Signaling

DOI 10.1126/scisignal.aav5183PMC PMC6800142

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Abstract

Molecular function and pathway cross-talk in TGF-β signaling reveal its complexity and open questions.

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Items 201–346 of 346

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Agricola, E., Randall, R. A., Gaarenstroom, T., Dupont, S., & Hill, C. S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.020 · Cited by 158
GDF11 Forms a Bone Morphogenetic Protein 1-Activated Latent Complex That Can Modulate Nerve Growth Factor-Induced Differentiation of PC12 Cells
Ge, G., Hopkins, D. R., Ho, W., & Greenspan, D. S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5846-5858.2005 · Cited by 158 · cited 1×
“Rather, the release of myostatin and GDF11 from latency depends on cleavage of the prodomain by BMP1 and mTolloid metalloproteases (50, 51).”
Background
VE‐cadherin is a critical endothelial regulator of TGF‐β signalling
Rudini, N., Felici, A., Giampietro, C., Lampugnani, M. G., Corada, M., Swirsding, K., Garrè, M., Liebner, S., Letarte, M., ten Dijke, P., et al. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.46 · Cited by 157
Topological similarities in TGF-β2, PDGF-BB and NGF define a superfamily of polypeptide growth factors
Murray‐Rust, J., McDonald, N. Q., Blundell, T. L., Hosang, M., Oefner, C., Winkler, F. K., & Bradshaw, R. A. (1993) · Structure · doi:10.1016/0969-2126(93)90029-g · Cited by 155
Two different signal transduction pathways can be activated by transforming growth factor beta 1 in epithelial cells.
Yan, Z., Winawer, S. J., & Friedman, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36823-0 · Cited by 153
TACE Activation by MAPK-Mediated Regulation of Cell Surface Dimerization and TIMP3 Association
Xu, P., Liu, J., Sakaki‐Yumoto, M., & Derynck, R. (2012) · Science Signaling · doi:10.1126/scisignal.2002689 · Cited by 151
Self-citation
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Mullen, A. C., & Wrana, J. L. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022186 · Cited by 149
The type I TGF-β receptor is covalently modified and regulated by sumoylation
Kang, J. S., Saunier, E. F., Akhurst, R. J., & Derynck, R. (2008) · Nature Cell Biology · doi:10.1038/ncb1728 · Cited by 148
Self-citation
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Mittl, P. R. E., Priestle, J. P., Cox, D., McMaster, G., Cerletti, N., & Grütter, M. G. (1996) · Protein Science · doi:10.1002/pro.5560050705 · Cited by 147
JAK‐2 as a novel mediator of the profibrotic effects of transforming growth factor β in systemic sclerosis
Dees, C., Tomčík, M., Palumbo‐Zerr, K., Distler, A., Beyer, C., Lang, V. R., Horn, A., Zerr, P., Zwerina, J., Gelse, K., et al. (2012) · Arthritis & Rheumatism · doi:10.1002/art.34500 · Cited by 147
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Liu, C., Xu, P., Lamouille, S., Xu, J., & Derynck, R. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.018 · Cited by 145
Self-citation
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Yang, Y., Park, J. W., Bebee, T. W., Warzecha, C. C., Guo, Y., Shang, X., Xing, Y., & Carstens, R. P. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00019-16 · Cited by 142
TGF‐β‐activated Smad3 represses MEF2‐dependent transcription in myogenic differentiation
Liu, D., Kang, J. S., & Derynck, R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600179 · Cited by 140
Self-citation
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Wilkes, M. C., Murphy, S. J., Garamszegi, N., & Leof, E. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8878-8889.2003 · Cited by 139
PARP-1 Attenuates Smad-Mediated Transcription
Lönn, P., van der Heide, L. P., Dahl, M., Hellman, U., Heldin, C., & Moustakas, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.029 · Cited by 138
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, R. G., Lodish, H. F., & Henis, Y. I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.4.767 · Cited by 138
Ablation of Smurf2 reveals an inhibition in TGF‐β signalling through multiple mono‐ubiquitination of Smad3
Tang, L.-Y., Yamashita, M., Coussens, N. P., Tang, Y., Wang, X., Li, C., Deng, C., Cheng, S. Y., & Zhang, Y. E. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.393 · Cited by 137
Regulation of transcription factors by sumoylation
Rosonina, E., Akhter, A., Dou, Y., Babu, J., & Theivakadadcham, V. S. S. (2017) · Transcription · doi:10.1080/21541264.2017.1311829 · Cited by 137
Heterodimeric transforming growth factor beta. Biological properties and interaction with three types of cell surface receptors.
Cheifetz, S., Bassols, A., Stanley, K., Ohta, M., Greenberger, J. S., & Massagué, J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38039-6 · Cited by 134
Genome-wide mechanisms of Smad binding
Morikawa, M., Koinuma, D., Miyazono, K., & Ch, H. (2012) · Oncogene · doi:10.1038/onc.2012.191 · Cited by 134
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, Y. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-09-0898 · Cited by 132
The Type II Transforming Growth Factor-β Receptor Autophosphorylates Not Only on Serine and Threonine but Also on Tyrosine Residues
Lawler, S. E., Feng, X., Chen, R., Maruoka, E. M., Turck, C. W., Griswold‐Prenner, I., & Derynck, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14850 · Cited by 131
Self-citation
Distinct Domain Utilization by Smad3 and Smad4 for Nucleoporin Interaction and Nuclear Import
Xu, L., Alarcón, C. R., Çöl, S., & Massagué, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307601200 · Cited by 127
Physical and Functional Interactions between Type I Transforming Growth Factor β Receptors and Bα, a WD-40 Repeat Subunit of Phosphatase 2A
Griswold‐Prenner, I., Kamibayashi, C., Maruoka, E. M., Mumby, M. C., & Derynck, R. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6595 · Cited by 127
Self-citation
Positive and negative regulation of type II TGF‐β receptor signal transduction by autophosphorylation on multiple serine residues
Luo, K., & Lodish, H. F. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1970 · Cited by 126
BMP2 induction of actin cytoskeleton reorganization and cell migration requires PI3-kinase and Cdc42 activity
Gamell, C., Osses, N., Bartrons, R., Rückle, T., Camps, M., Rosa, J. L., & Ventura, F. (2008) · Journal of Cell Science · doi:10.1242/jcs.031286 · Cited by 125 · cited 1×
“TGF-bs and BMPs rapidly induce AKT and mTOR activation, often followed by delayed, indirect activation, as seen with other non-Smad signaling pathways (283, 313, 314).”
Background
TGF-β Family Signaling in Connective Tissue and Skeletal DiseasesPreprint
MacFarlane, E. G., Haupt, J., Dietz, H. C., & Shore, E. M. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022269 · Cited by 125
Itch E3 Ligase-Mediated Regulation of TGF-β Signaling by Modulating Smad2 Phosphorylation
Bai, Y., Yang, C., Hu, K., Elly, C., & Liu, Y. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.07.021 · Cited by 123
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, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908279106 · Cited by 122
Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors
Martín-Malpartida, P., Palau, M. B., Kaczmarska, Z., Freier, R., Gomes, T., Aragón, E., Zou, Y., Wang, Q., Xi, Q., Ruiz, L., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02054-6 · Cited by 121
Lipid Rafts and Caveolin-1 Coordinate Interleukin-1β (IL-1β)-dependent Activation of NFκB by Controlling Endocytosis of Nox2 and IL-1β Receptor 1 from the Plasma Membrane
Oakley, F. D., Smith, R. L., & Engelhardt, J. F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.042127 · Cited by 120
L- and S-endoglin differentially modulate TGFβ1 signaling mediated by ALK1 and ALK5 in L6E9 myoblasts
Velasco, S., Álvarez-Muñoz, P., Pericacho, M., ten Dijke, P., Bernabéu, C., López-Novoa, J. M., & Rodríguez‐Barbero, A. (2008) · Journal of Cell Science · doi:10.1242/jcs.023283 · Cited by 119
RGMs: Structural Insights, Molecular Regulation, and Downstream Signaling
Siebold, C., Yamashita, T., Monnier, P. P., Mueller, B. K., & Pasterkamp, R. J. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.11.009 · Cited by 118
Structure of bone morphogenetic protein 9 procomplex
Mi, L.-Z., Brown, C. T., Gao, Y., Tian, Y., Le, V. Q., Walz, T., & Springer, T. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501303112 · Cited by 117
An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity
Xiao, Z., Latek, R. R., & Lodish, H. F. (2003) · Oncogene · doi:10.1038/sj.onc.1206212 · Cited by 117
The Activity of Guanine Exchange Factor NET1 Is Essential for Transforming Growth Factor-β-mediated Stress Fiber Formation
Shen, X., Li, J., Hu, P. P.-C., Waddell, D. S., Zhang, J., & Wang, X. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009534200 · Cited by 116
Betaglycan: A multifunctional accessory
Bilandzic, M., & Stenvers, K. L. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.04.014 · Cited by 115
The regulation of TGF-β/SMAD signaling by protein deubiquitination
Zhang, J., Zhang, X., Xie, F., Zhang, Z., van Dam, H., Zhang, L., & Zhou, F. (2014) · Protein & Cell · doi:10.1007/s13238-014-0058-8 · Cited by 114
The transcriptional co-activator P/CAF potentiates TGF-beta/Smad signaling
Itoh, S. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.21.4291 · Cited by 114
Smad6 Recruits Transcription Corepressor CtBP To Repress Bone Morphogenetic Protein-Induced Transcription
Lin, X., Liang, Y.-Y., Sun, B., Liang, M., Shi, Y. G., Brunicardi, F. C., Shi, Y., & Feng, X. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.24.9081-9093.2003 · Cited by 114
TGF-β sensitivity is determined by N-linked glycosylation of the type II TGF-β receptor
Kim, Y.-W., Park, J., Lee, H., Lee, S., & Kim, S. (2012) · Biochemical Journal · doi:10.1042/bj20111923 · Cited by 110
Arginine Methylation Initiates BMP-Induced Smad Signaling
Xu, J., Wang, A. H., Osés-Prieto, J. A., Makhijani, K., Katsuno, Y., Pei, M., Yan, L., Zheng, Y. G., Burlingame, A. L., Brückner, K., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.004 · Cited by 108
Self-citation
STAT3 selectively interacts with Smad3 to antagonize TGF-β
Wang, G., Yu, Y., Sun, C., Liu, T., Liang, T., Zhan, L., Lin, X., & Feng, X.-H. (2015) · Oncogene · doi:10.1038/onc.2015.446 · Cited by 107
A Nuclear Antagonistic Mechanism of Inhibitory Smads in Transforming Growth Factor-β Signaling
Bai, S., & Cao, X. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105105200 · Cited by 106
Nuclear Export of Smad2 and Smad3 by RanBP3 Facilitates Termination of TGF-β Signaling
Dai, F., Lin, X., Chang, C., & Feng, X. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.01.022 · Cited by 105
Modulation of GDF5/BRI‐b signalling through interaction with the tyrosine kinase receptor Ror2
Sammar, M., Stricker, S., Schwabe, G. C., Sieber, C., Hartung, A., Hanke, M., Oishi, I., Pohl, J., Minami, Y., Sebald, W., et al. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00799.x · Cited by 104
Smad6 inhibits non-canonical TGF-β1 signalling by recruiting the deubiquitinase A20 to TRAF6
Jung, S. M., Lee, J.-H., Park, J., Oh, Y. S., Lee, S. K., Park, J. S., Lee, J. Y., Kim, J. H., Lee, J. Y., Bae, Y., et al. (2013) · Nature Communications · doi:10.1038/ncomms3562 · Cited by 104
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) · Journal of Cell Science · doi:10.1242/jcs.03400 · Cited by 104
Direct Regulation of Alternative Splicing by SMAD3 through PCBP1 Is Essential to the Tumor-Promoting Role of TGF-β
Tripathi, V., Sixt, K. M., Gao, S., Xu, X., Huang, J. L., Weigert, R., Zhou, M., & Zhang, Y. E. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.013 · Cited by 104
CHIP Controls the Sensitivity of Transforming Growth Factor-β Signaling by Modulating the Basal Level of Smad3 through Ubiquitin-mediated Degradation
Xin, H., Xu, X., Li, L., Ning, H., Rong, Y., Shang, Y., Wang, Y., Fu, X.-Y., & Chang, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412275200 · Cited by 103
Protein Serine/Threonine Phosphatase PPM1A Dephosphorylates Smad1 in the Bone Morphogenetic Protein Signaling Pathway
Duan, X., Liang, Y.-Y., Feng, X., & Lin, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605169200 · Cited by 103
Agonists and Antagonists of TGF-β Family LigandsPreprint
Chang, C. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021923 · Cited by 101
Small C-terminal Domain Phosphatases Dephosphorylate the Regulatory Linker Regions of Smad2 and Smad3 to Enhance Transforming Growth Factor-β Signaling
Wrighton, K. H., Willis, D., Long, J., Liu, F., Lin, X., & Feng, X. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607246200 · Cited by 100
The Mechanism of Nuclear Export of Smad3 Involves Exportin 4 and Ran
Kurisaki, A., Kurisaki, K., Kowanetz, M., Sugino, H., Yoneda, Y., Heldin, C., & Moustakas, A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1318-1332.2006 · Cited by 100
Differential Ubiquitination Defines the Functional Status of the Tumor Suppressor Smad4
Morén, A., Hellman, U., Inada, Y., Imamura, T., Heldin, C., & Moustakas, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300159200 · Cited by 99
Smad3 regulates E-cadherin via miRNA-200 pathway
Ahn, S.-M., Cha, J.-Y., Kim, J., Kim, D., Trang, H. T. H., Kim, Y.-M., Yh, C., Park, D., & Hong, S. (2011) · Oncogene · doi:10.1038/onc.2011.484 · Cited by 98
TGFβ and Wnt pathway cross-talk
Attisano, L., & Labbé, E. (2004) · Cancer and Metastasis Reviews · doi:10.1023/a:1025811012690 · Cited by 98
Fine‐tuning BMP7 signalling in adipogenesis by UBE2O/E2‐230K‐mediated monoubiquitination of SMAD6
Zhang, X., Zhang, J., Bauer, A., Zhang, L., Selinger, D. W., Lu, C., & ten Dijke, P. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.38 · Cited by 97
Posttranslational Regulation of SmadsPreprint
Xu, P., Lin, X., & Feng, X. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022087 · Cited by 97 · cited 10×
“6, II and III) that thus define the behavior and activities of the Smads (154, 197).”
BackgroundInfluential
Repression of Bone Morphogenetic Protein and Activin-inducible Transcription by Evi-1
Alliston, T. N., Ko, T. C., Cao, Y., Liang, Y. Y., Feng, X.-H., Chang, C., & Derynck, R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414305200 · Cited by 96
Self-citation
Smad2 and Smad3 have differential sensitivity in relaying TGFβ signaling and inversely regulate early lineage specification
Liu, L., Liu, X., Ren, X., Tian, Y., Chen, Z., Xu, X., Du, Y., Jiang, C., Fang, Y., Liu, Z., et al. (2016) · Scientific Reports · doi:10.1038/srep21602 · Cited by 95
Structural Basis of Intracellular TGF-β Signaling: Receptors and SmadsPreprint
Chaikuad, A., & Bullock, A. N. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022111 · Cited by 95
Evolution of the GDNF Family Ligands and Receptors
Airaksinen, M. S., Holm, L., & Hätinen, T. (2006) · Brain Behavior and Evolution · doi:10.1159/000094087 · Cited by 94
Arkadia Enhances Nodal/TGF-β Signaling by Coupling Phospho-Smad2/3 Activity and Turnover
Mavrakis, K. J., Andrew, R. L., Lee, K. L., Petropoulou, C., Dixon, J. E., Navaratnam, N., Norris, D. P., & Episkopou, V. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050067 · Cited by 94
Cripto Binds Transforming Growth Factor β (TGF-β) and Inhibits TGF-β Signaling
Gray, P. C., Shani, G., Aung, K., Kelber, J. A., & Vale, W. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01168-06 · Cited by 93
Membrane Rafts Play a Crucial Role in Receptor Activator of Nuclear Factor κB Signaling and Osteoclast Function
Ha, H., Kwak, H. B., Lee, S. K., Na, D. S., Rudd, C. E., Lee, Z. H., & Kim, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212626200 · Cited by 91
Ubiquitination and Proteolysis of Cancer-Derived Smad4 Mutants by SCFSkp2
Liang, M., Liang, Y.-Y., Wrighton, K. H., Ungermannova, D., Wang, X., Brunicardi, F. C., Liu, X., Feng, X., & Lin, X. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7524-7537.2004 · Cited by 89
Erratum: STAT3 selectively interacts with Smad3 to antagonize TGF-β signalling
Wang, G., Yu, Y., Sun, C., Liu, T., Liang, T., Zhan, L., Lin, X., & Feng, X.-H. (2016) · Oncogene · doi:10.1038/onc.2016.145 · Cited by 88
Dullard Promotes Degradation and Dephosphorylation of BMP Receptors and Is Required for Neural Induction
Satow, R., Kurisaki, A., Chan, T.-C., Hamazaki, T. S., & Asashima, M. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.10.001 · Cited by 87
Biosynthesis of the Type I and Type II TGF-β Receptors
Wells, R. G., Yankelev, H., Lin, H. Y.-F., & Lodish, H. F. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11444 · Cited by 86
Regulation of Transforming Growth Factor-β Signaling by Protein Inhibitor of Activated STAT, PIASy through Smad3
Imoto, S., Sugiyama, K., Muromoto, R., Sato, N., Yamamoto, T., & Matsuda, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304961200 · Cited by 85
Regulation of Smad4 Sumoylation and Transforming Growth Factor-β Signaling by Protein Inhibitor of Activated STAT1
Liang, M., Melchior, F., Feng, X., & Lin, X. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401554200 · Cited by 85
Innate Antiviral Host Defense Attenuates TGF-β Function through IRF3-Mediated Suppression of Smad Signaling
Xu, P., Bailey-Bucktrout, S. L., Xi, Y., Xu, D., Du, D., Zhang, Q., Xiang, W., Liu, J., Melton, A. C., Sheppard, D., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.027 · Cited by 85
Self-citation
Kinesin-Mediated Transport of Smad2 Is Required for Signaling in Response to TGF-β Ligands
Batut, J., Howell, M. T., & Hill, C. S. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.01.010 · Cited by 84
Two highly related regulatory subunits of PP2A exert opposite effects on TGF-β/Activin/Nodal signalling
Batut, J., Schmierer, B., Cao, J., Raftery, L. A., Hill, C. S., & Howell, M. T. (2008) · Development · doi:10.1242/dev.020842 · Cited by 84
Transforming Growth Factor-beta (TGF-β) Binding to the Extracellular Domain of the Type II TGF-β Receptor: Receptor Capture on a Biosensor Surface Using a New Coiled-coil Capture System Demonstrates that Avidity Contributes Significantly to High Affinity Binding
Crescenzo, G. D., Pham, P. L., Durocher, Y., & O'Connor‐McCourt, M. D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00360-7 · Cited by 83
Transforming Growth Factor-β1 Stimulates Protein Kinase A in Mesangial Cells
Wang, L., Zhu, Y., & Sharma, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.14.8522 · Cited by 82
Arginine methylation of SMAD7 by PRMT1 in TGF-β–induced epithelial–mesenchymal transition and epithelial stem-cell generation
Katsuno, Y., Qin, J., Osés-Prieto, J. A., Wang, H., Jackson‐Weaver, O., Zhang, T., Lamouille, S., Wu, J., Burlingame, A. L., Xu, J., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002027 · Cited by 82
Self-citation
Extracellular Regulation of Bone Morphogenetic Protein Activity by the Microfibril Component Fibrillin-1
Wohl, A. P., Troilo, H., Collins, R. F., Baldock, C., & Sengle, G. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.704734 · Cited by 79
Oligomeric interactions of TGF‐β and BMP receptors
Ehrlich, M., Gutman, O., Knaus, P. I., & Henis, Y. I. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.01.040 · Cited by 78
Increase of O-Glycosylated Oncofetal Fibronectin in High Glucose-Induced Epithelial-Mesenchymal Transition of Cultured Human Epithelial Cells
Alisson‐Silva, F., Freire‐de‐Lima, L., Donadio, J. L., Lucena, M. C., Penha, L., Sá-Diniz, J. N., Dias, W. B., & Todeschini, A. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060471 · Cited by 77 · cited 1×
“High glucose (meaning 25 mM, the amount associated with hyperglycemia) promotes N- and O-glycosylation of proteins (105, 106), raising the possibility that it might also promote TGF-b or BMP receptor glycosylation and thus increase ligand binding.”
Background
Integrin-mediated type II TGF-β receptor tyrosine dephosphorylation controls SMAD-dependent profibrotic signaling
Chen, X., Wang, H., Liao, H., Hu, W., Gewin, L. S., Mernaugh, G., Zhang, S., Zhang, Z., Vega‐Montoto, L., Vanacore, R., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci71668 · Cited by 76
Distinct role of endocytosis for Smad and non-Smad TGF-β signaling regulation in hepatocytes
Meyer, C., Godoy, P., Bachmann, A., Liu, Y., Barzan, D., Ilkavets, I., Maier, P. J., Herskind, C., Hengstler, J. G., & Dooley, S. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.11.027 · Cited by 75
TRAF6 Stimulates the Tumor-Promoting Effects of TGFβ Type I Receptor Through Polyubiquitination and Activation of Presenilin 1
Gudey, S. K., Sundar, R., Mu, Y., Wallenius, A., Zang, G., Bergh, A. R. J., Heldin, C., & Landström, M. (2014) · Science Signaling · doi:10.1126/scisignal.2004207 · Cited by 75
SET9-Mediated Regulation of TGF-β Signaling Links Protein Methylation to Pulmonary Fibrosis
Elkouris, M., Kontaki, H., Stavropoulos, A., Antonoglou, A., Nikolaou, K. C., Samiotaki, M. K., Szántai, E., Saviolaki, D., Brown, P. J., Sideras, P., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.051 · Cited by 75
The Long (lncRNA) and Short (miRNA) of It: TGFβ-Mediated Control of RNA-Binding Proteins and Noncoding RNAs
Janakiraman, H., House, R. P., Gangaraju, V. K., Diehl, J. A., Howe, P. H., & Palanisamy, V. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0547 · Cited by 74
Stabilization of Snail through AKT/GSK-3β signaling pathway is required for TNF-α-induced epithelial–mesenchymal transition in prostate cancer PC3 cells
Wang, H., Fang, R., Wang, X., Zhang, F., Chen, D., Zhou, B., Wang, H., Cai, S., & Du, J. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.05.046 · Cited by 73
Smad3‐mediated recruitment of the methyltransferase SETDB1/ESET controls Snail1 expression and epithelial–mesenchymal transition
Du, D., Katsuno, Y., Meyer, D. S., Budi, E. H., Chen, S., Koeppen, H., Wang, H., Akhurst, R. J., & Derynck, R. (2017) · EMBO Reports · doi:10.15252/embr.201744250 · Cited by 73
Self-citation
Platelet-derived Growth Factor β-Receptor, Transforming Growth Factor β Type I Receptor, and CD44 Protein Modulate Each Other's Signaling and Stability
Porsch, H., Mehić, M., Olofsson, B., Heldin, P., & Heldin, C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.547273 · Cited by 71
Roles for the MH2 Domain of Smad7 in the Specific Inhibition of Transforming Growth Factor-β Superfamily Signaling
Mochizuki, T., Miyazaki, H., Hara, T., Furuya, T., Imamura, T., Watabe, T., & Miyazono, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313977200 · Cited by 70
BMP-4 Induction of Arrest and Differentiation of Osteoblast-Like Cells via p21 CIP1 and p27 KIP1 Regulation
Chang, S., Chang, T., Peng, H., Yeh, Y. T., Lee, D. Y., Yeh, C. R., Zhou, J., Cheng, C. K., Chang, C. A., & Chiu, J. (2009) · Molecular Endocrinology · doi:10.1210/me.2009-0143 · Cited by 69
The insulin response integrates increased TGF-β signaling through Akt-induced enhancement of cell surface delivery of TGF-β receptors
Budi, E. H., Muthusamy, B.-P., & Derynck, R. (2015) · Science Signaling · doi:10.1126/scisignal.aaa9432 · Cited by 69
Self-citation
Distributing signaling proteins in space and time: the province of cytonemes
Kornberg, T. B. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.02.010 · Cited by 69
Cripto Binds Transforming Growth Factor β (TGF-β) and Inhibits TGF-β Signaling
Gray, P. C., Shani, G., Aung, K., Kelber, J. A., & Vale, W. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01609-08 · Cited by 68
Polyubiquitination of Transforming Growth Factor β (TGFβ)-associated Kinase 1 Mediates Nuclear Factor-κB Activation in Response to Different Inflammatory Stimuli
Hamidi, A., von Bülow, V., Hamidi, R., Winssinger, N., Barluenga, S., Heldin, C., & Landström, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.285122 · Cited by 67
Cross‐talk between IL‐6 and TGF‐β signaling in hepatoma cells
Yamamoto, T., Matsuda, T., Muraguchi, A., Miyazono, K., & Kawabata, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02258-x · Cited by 65
Zebrafishnma is involved in TGF? family signaling
Tsang, M., Kim, R., de Caestecker, M. P., Kudoh, T., Roberts, A. B., & Dawid, I. B. (2000) · genesis · doi:10.1002/1526-968x(200010)28:2 · Cited by 64
Smad7 Inhibits Transforming Growth Factor-β Family Type I Receptors through Two Distinct Modes of Interaction
Kamiya, Y., Miyazono, K., & Miyazawa, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166140 · Cited by 63
A Large Bioactive BMP Ligand with Distinct Signaling Properties Is Produced by Alternative Proconvertase Processing
Akiyama, T., Marqués, G., & Wharton, K. A. (2012) · Science Signaling · doi:10.1126/scisignal.2002549 · Cited by 63
Role of GARP in the activation of latent TGF-β1
Stockis, J., Dedobbeleer, O., & Lucas, S. (2017) · Molecular BioSystems · doi:10.1039/c7mb00251c · Cited by 62
Regulation of transforming growth factor‐β and bone morphogenetic protein signalling by transcriptional coactivator GCN5
Kahata, K., Hayashi, M., Asaka, M., Hellman, U., Kitagawa, H., Yanagisawa, J., Kato, S., Imamura, T., & Miyazono, K. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00706.x · Cited by 60
Resolving the Combinatorial Complexity of Smad Protein Complex Formation and Its Link to Gene Expression
Lucarelli, P., Schilling, M., Kreutz, C., Vlasov, A., Boehm, M. E., Iwamoto, N., Steiert, B., Lattermann, S., Wäsch, M., Stepath, M., et al. (2017) · Cell Systems · doi:10.1016/j.cels.2017.11.010 · Cited by 60
Smad Signaling Antagonizes STAT5-mediated Gene Transcription and Mammary Epithelial Cell Differentiation
Cocolakis, E., Dai, M., Drevet, L., Ho, J., Haines, E., Ali, S., & Lebrun, J. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707492200 · Cited by 59
Vg1-Nodal heterodimers are the endogenous inducers of mesendoderm
Montague, T. G., & Schier, A. F. (2017) · eLife · doi:10.7554/elife.28183 · Cited by 59 · cited 7×
“P. S. Kunwar, S. Zimmerman, J. T. Bennett, Y. Chen, M. Whitman, A. F. Schier, Mixer/Bon and FoxH1/Sur have overlapping and divergent roles in Nodal signaling and mesendoderm induction.”
BackgroundInfluential
Mixer/Bon and FoxH1/Sur have overlapping and divergent roles in Nodal signaling and mesendoderm induction
Kunwar, P. S., Zimmerman, S., Bennett, J. T., Chen, Y., Whitman, M., & Schier, A. F. (2003) · Development · doi:10.1242/dev.00803 · Cited by 58
c-Abl promotes osteoblast expansion by differentially regulating canonical and non-canonical BMP pathways and p16INK4a expression
Kua, H. Y., Liu, H., Leong, W. F., Li, L., Jia, D., Ma, G., Hu, Y., Wang, X., Chau, J. F. L., Chen, Y., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2528 · Cited by 57 · cited 1×
“In addition, TGF-b can induce activation of the c-Abl tyrosine kinase (341), whereas c-Abl was seen to associate with and phosphorylate the BMP-RIA receptor (342).”
Background
The Transcription Factor GLI1 Interacts with SMAD Proteins to Modulate Transforming Growth Factor β-Induced Gene Expression in a p300/CREB-binding Protein-associated Factor (PCAF)-dependent Manner
Nye, M. D., Almada, L. L., Fernández‐Barrena, M. G., Marks, D. L., Elsawa, S. F., Vrabel, A. M., Tolosa, E. J., Ellenrieder, V., & Fernández-Zapico, M. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545194 · Cited by 57
MTMR4 Attenuates Transforming Growth Factor β (TGFβ) Signaling by Dephosphorylating R-Smads in Endosomes
Yu, J., Pan, L., Qin, X., Chen, H., Xu, Y., Chen, Y., & Tang, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.075036 · Cited by 57
Histone 3 Lysine 9 (H3K9) Methyltransferase Recruitment to the Interleukin-2 (IL-2) Promoter Is a Mechanism of Suppression of IL-2 Transcription by the Transforming Growth Factor-β-Smad Pathway
Wakabayashi, Y., Tamiya, T., Takada, I., Fukaya, T., Sugiyama, Y., Inoue, N., Kimura, A., Morita, R., Kashiwagi, I., Takimoto, T., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.236794 · Cited by 55
Mechanisms of Transforming Growth Factor-β Receptor Endocytosis and Intracellular Sorting Differ between Fibroblasts and Epithelial Cells
Doré, J. J. E., Yao, D., Edens, M., Garamszegi, N., Sholl, E. L., & Leof, E. B. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.3.675 · Cited by 55
An evolving web of signaling networks regulated by Cripto-1
Nagaoka, T., Karasawa, H., de Castro, N. P., Rangel, M. C., Salomon, D. S., & Bianco, C. (2011) · Growth Factors · doi:10.3109/08977194.2011.641962 · Cited by 54 · cited 1×
“Cripto may have additional roles in integrating signaling pathways, including EGF receptor and Wnt signaling (92).”
Background
Regulation of Bone Morphogenetic Protein 9 (BMP9) by Redox-dependent Proteolysis
Wei, Z., Salmon, R. M., Upton, P. D., Morrell, N. W., & Li, W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.579771 · Cited by 53 · cited 2×
“nonlinked dimer showing increased susceptibility to proteolytic degradation (35).”
Background
Signaling-Mediated Regulation of MicroRNA Processing
Shen, J., & Hung, M. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2568 · Cited by 53 · cited 1×
“miRNA genes are transcribed by RNApolymerase II into pri-miRNAs that are then processed through cleavage into pre-miRNAs and give rise to mature miRNAs (229).”
Background
Endocytosis and trafficking of BMP receptors: Regulatory mechanisms for fine-tuning the signaling response in different cellular contexts
Ehrlich, M. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2015.12.008 · Cited by 53
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, X. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00121-15 · Cited by 49
ShcA Protects against Epithelial–Mesenchymal Transition through Compartmentalized Inhibition of TGF-β-Induced Smad Activation
Muthusamy, B.-P., Budi, E. H., Katsuno, Y., Lee, M., Smith, S. M., Mirza, A. M., Akhurst, R. J., & Derynck, R. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002325 · Cited by 47
Self-citation
Nodal·Gdf1 Heterodimers with Bound Prodomains Enable Serum-independent Nodal Signaling and Endoderm Differentiation
Fuerer, C., Nostro, M. C., & Constam, D. B. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.550301 · Cited by 46
Time-resolved dissection of early phosphoproteome and ensuing proteome changes in response to TGF-β
D’Souza, R. C. J., Knittle, A. M., Nagaraj, N., van Dinther, M., Choudhary, C., ten Dijke, P., Mann, M., & Sharma, K. (2014) · Science Signaling · doi:10.1126/scisignal.2004856 · Cited by 46
Differential Trafficking of Transforming Growth Factor-β Receptors and Ligand in Polarized Epithelial Cells
Murphy, S. J., Doré, J. J. E., Edens, M., Coffey, R. J., Barnard, J. A., Mitchell, H. D., Wilkes, M. C., & Leof, E. B. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-02-0097 · Cited by 45
TRAF6 promotes TGFβ-induced invasion and cell-cycle regulation via Lys63-linked polyubiquitination of Lys178 in TGFβ type I receptor
Sundar, R., Gudey, S. K., Heldin, C., & Landström, M. (2015) · Cell Cycle · doi:10.4161/15384101.2014.990302 · Cited by 45
Twisted gastrulation loss-of-function analyses support its role as a BMP inhibitor during earlyXenopusembryogenesis
Blitz, I. L., Cho, K. W. Y., & Chang, C. (2003) · Development · doi:10.1242/dev.00709 · Cited by 44
A Novel Nuclear Export Signal in Smad1 Is Essential for Its Signaling Activity
Xiao, Z., Brownawell, A. M., Macara, I. G., & Lodish, H. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301596200 · Cited by 41
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, P. B., Feng, X., & Lin, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.568964 · Cited by 40 · cited 8×
“MTMR4 also C-terminally dephosphorylates, and thus deactivates Smad2 and Smad3 (248), and SCP4 dephosphorylates BMP-activated Smad1 and Smad5 (249).”
BackgroundInfluential
Zinc Finger Protein 451 Is a Novel Smad Corepressor in Transforming Growth Factor-β Signaling
Feng, Y.-L., Wu, H., Xu, Y., Zhang, Z., Liu, T., Lin, X., & Feng, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526905 · Cited by 39
Regulation of RabGAPs involved in insulin action
Mafakheri, S., Chadt, A., & Al‐Hasani, H. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170479 · Cited by 39
TrkC Binds to the Bone Morphogenetic Protein Type II Receptor to Suppress Bone Morphogenetic Protein Signaling
Jin, W., Yun, C., Kim, H.-S., & Kim, S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0436 · Cited by 37
Retromer maintains basolateral distribution of the type II TGF-β receptor via the recycling endosome
Yin, X., Murphy, S. J., Wilkes, M. C., Ji, Y., & Leof, E. B. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-02-0093 · Cited by 37
Elucidation of Epigenetic Inactivation of SMAD8 in Cancer Using Targeted Expressed Gene Display
Cheng, K., Ponte, J. F., & Thiagalingam, S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2688 · Cited by 36
Repulsive guidance molecules (RGMs) and neogenin in bone morphogenetic protein (BMP) signaling
Tian, C., & Liu, J. (2013) · Molecular Reproduction and Development · doi:10.1002/mrd.22199 · Cited by 35 · cited 1×
“How RGMs promote BMP binding to receptor complexes and enhance BMP signaling remains to be clarified, although they are thought to control endocytosis of the ligand-receptor complexes in a clathrin-dependent manner, thus promoting BMP-induced Smad activation (13, 85, 86).”
Background
Requirement of a dynein light chain in TGFβ/Smad3 signaling
Jin, Q., Gao, G., & Mulder, K. M. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21910 · Cited by 35
Alternative splicing of SMADs in differentiation and tissue homeostasis
Tao, S., & Sampath, K. (2010) · Development Growth & Differentiation · doi:10.1111/j.1440-169x.2009.01163.x · Cited by 34 · cited 1×
“Adding to this complexity, several Smads are expressed as differently spliced isoforms (155).”
Background
Tolloid cleavage activates latent GDF8 by priming the pro‐complex for dissociation
Le, V. Q., Iacob, R. E., Tian, Y., McConaughy, W., Jackson, J., Su, Y., Zhao, B., Engen, J. R., Pirruccello, M., & Springer, T. A. (2018) · The EMBO Journal · doi:10.15252/embj.201797931 · Cited by 33
Regulation of the TGF-β pathway by deubiquitinases in cancer
Liu, S., de Boeck, M., van Dam, H., & ten Dijke, P. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.05.001 · Cited by 32
Endofin, a novel BMP-SMAD regulator of the iron-regulatory hormone, hepcidin
Goh, J. B., Wallace, D. F., Hong, W., & Subramaniam, V. N. (2015) · Scientific Reports · doi:10.1038/srep13986 · Cited by 29
Endothelial cell biology of Endoglin in hereditary hemorrhagic telangiectasia
Sugden, W. W., & Siekmann, A. F. (2018) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000419 · Cited by 29 · cited 3×
“In contrast to these ligands, endoglin binds BMP-9 and BMP-10 with high affinity, suggesting a natural physiological role in the presentation of these ligands to their receptors and in the vascular roles of these ligands (77, 82, 83).”
Background
Dab2 inhibits the cholesterol-dependent activation of JNK by TGF-β
Shapira, K. E., Hirschhorn, T., Barzilay, L., Smorodinsky, N. I., Henis, Y. I., & Ehrlich, M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0537 · Cited by 27
Different Requirements for Proteolytic Processing of Bone Morphogenetic Protein 5/6/7/8 Ligands in Drosophila melanogaster
Fritsch, C., Sawala, A., Harris, R. E., Maartens, A. P., Sutcliffe, C., Ashe, H. L., & Ray, R. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.316745 · Cited by 24
The Unglycosylated Extracellular Domain of Type‐II Receptor for Transforming Growth Factor‐β
Goetschy, J., Letourneur, O., Cerletti, N., & Horisberger, M. A. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00355.x · Cited by 23
The methyltransferase SET9 regulates TGFB1 activation of renal fibroblasts via interaction with SMAD3
Shuttleworth, V. G., Gaughan, L., Nawafa, L. S. O., Mooney, C. A., Cobb, S. L., Sheerin, N., & Logan, I. R. (2017) · Journal of Cell Science · doi:10.1242/jcs.207761 · Cited by 23 · cited 1×
“Recruitment of Suv39h1 (213) or SETDB1 (214) confer TGF-b–induced H3K9 methylation and transcription repression at promoter sequences of the Il2 and Snai1 genes, respectively (187, 188), whereas Smad3-mediated recruitment of the H3K4 methyltransferase SET9 targets the ACTA2 gene (215).”
Background
Yin Yang 1 (YY1) synergizes with Smad7 to inhibit TGF-β signaling in the nucleus
Yan, X., Pan, J., Xiong, W., Cheng, M., Sun, Y., Zhang, S., & Chen, Y. (2013) · Science China Life Sciences · doi:10.1007/s11427-013-4581-2 · Cited by 22
N-linked glycosylation of the bone morphogenetic protein receptor type 2 (BMPR2) enhances ligand binding
Lowery, J. W., Amich, J. M., Andonian, A., & Rosen, V. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1541-8 · Cited by 20 · cited 2×
“In addition, ectodomain N-glycosylation enhances the binding of BMP-2 to the BMP-RII but not to the ActRII or ActRIIB type II receptors (103).”
Background
Alternative cleavage of the bone morphogenetic protein (BMP), Gbb, produces ligands with distinct developmental functions and receptor preferences
Anderson, E. N., & Wharton, K. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.793513 · Cited by 20
Analysis of the mRNA expression of the TGF‐Beta family in testicular cells and localization of the splice variant TGF‐β2B in testis
Konrad, L., Lüers, G. H., Völck‐Badouin, E., Keilani, M. M., Laible, L., Aumüller, G., & Hofmann, R. W. (2006) · Molecular Reproduction and Development · doi:10.1002/mrd.20399 · Cited by 17
High glucose induces N-linked glycosylation-mediated functional upregulation and overexpression of Cav3.2 T-type calcium channels in neuroendocrine-like differentiated human prostate cancer cells
Fukami, K., Asano, E., Ueda, M., Sekiguchi, F., Yoshida, S., & Kawabata, A. (2017) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2016.12.004 · Cited by 12 · cited 1×
“High glucose (meaning 25 mM, the amount associated with hyperglycemia) promotes N- and O-glycosylation of proteins (105, 106), raising the possibility that it might also promote TGF-b or BMP receptor glycosylation and thus increase ligand binding.”
Background
Identification and characterization of a human smad3 splicing variant lacking part of the linker region
Kjellman, C., Honeth, G., Järnum, S., Lindvall, M. L., Darabi, A., Nilsson, I., Edvardsen, K., Salford, L. G., & Widegren, B. (2004) · Gene · doi:10.1016/j.gene.2003.11.026 · Cited by 11
Novel Signaling Interface Constituted with Membrane Receptor-Like Kinases Emerged from the Study of Interaction and Transphosphorylation of BRI1 and BAK1
Li, C., Zhang, S., & Wang, X. (2017) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026617666170414144145 · Cited by 6

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R. Derynck K. Miyazono The Biology of the TGF-β Family (Cold Spring Harbor Laboratory Press 2017) pp. 1164.

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Authors: Derynck, R., & Budi, E. H.
Affiliations: University of California, San Francisco (US)
Corresponding author: Derynck, Rik
ORCID: Derynck, Rik
Budi, Erine H.
Venue: Science Signaling
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2019-02-26
Volume: 12
Issue: 570
ISSN: 1937-9145 (ISSN-L)
1945-0877
DOI: 10.1126/scisignal.aav5183
PMC: PMC6800142
OpenAlex: W2917714624
Cited by: 785
References: 347
Citations by year: 2026: 83 · 2025: 85 · 2024: 129 · 2023: 118 · 2022: 102 · 2021: 152 · 2020: 77 · 2019: 35
FWCI: 8.08
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Science Signaling (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Cancer Institute (RO1-CA63101, RO1-CA136690)
JDRF (3-APF-2017-392-A-N)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: Smad proteins, TGF-beta receptor, dual-specificity kinase, signaling crosstalk, non-Smad signaling, cancer, fibrosis, developmental anomalies
MeSH terms: Animals, Cell Differentiation, Gene Expression Regulation, Humans, Ligands, Neoplasms, Protein Binding, Signal Transduction, Transforming Growth Factor beta, Receptors, Transforming Growth Factor beta

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Specificity, versatility, and control of TGF-β family signaling

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