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

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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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“The TGF-β family comprises three isoforms, namely TGF-β1, TGF-β2, and TGF-β3, existing as homodimers within the biological system [39].”
Mechanistic insights curcumin’s anti-inflammatory in pancreatic cancer: experimental and computational evidence implicating IL1B interference via IL10RA upregulation and NLRP3/TLR3 downregulation
Cao, J., Hang, K., Zhang, H., Xia, Q., Zhang, X., Men, J., Tian, J., Xia, Z.-L., Liao, D.-S., & Li, K.-Z. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1601908 · Cited by 15
Role of inhibitor of differentiation 3 gene in cellular differentiation of human corneal stromal fibroblasts.
Gupta, S., Martin, L. M., Sinha, N. R., Smith, K. E., Sinha, P. R., Dailey, E. M., Hesemann, N. P., & Mohan, R. R. (2020) · PubMed Central · Cited by 13
Anti-TGF-β1 aptamer enhances therapeutic effect of tyrosine kinase inhibitor, gefitinib, on non-small cell lung cancer in xenograft model
Takahashi, M., Hashimoto, Y., & Nakamura, Y. (2022) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2022.06.001 · Cited by 13
“INTRODUCTION Transforming growth factor b (TGF-b) is a pleiotropic cytokine involved in diverse cellular events, including cell proliferation, differentiation, immune response, and apoptosis.(1,2) In mammals, there are three isoforms of TGF-b—TGF-b1, -b2, and -b3—encoded at distinct genomic loci,(3) and TGF-b1 is the…”
Background
Potential role of TGFΒ and autophagy in early cerebellum development
Dalvand, A., Rosa, S. C. D. S., Ghavami, S., & Marzban, H. (2022) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2022.101358 · Cited by 13
Effects of epidermal growth factor on transforming growth factor-beta1-induced epithelial-mesenchymal transition and potential mechanism in human corneal epithelial cells
Chen, S.-Y. (2019) · International Journal of Ophthalmology · doi:10.18240/ijo.2020.01.03 · Cited by 14
A TGF-β– and p63-Responsive Enhancer Regulates IFN-κ Expression in Human Keratinocytes
Klein, K., Habiger, C., Iftner, T., & Stubenrauch, F. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1901178 · Cited by 13
Mechanisms of TGFβ3 Action as a Therapeutic Agent for Promoting the Synthesis of Extracellular Matrix Proteins in Hyaline Cartilage
Bozhokin, M. S., Sopova, J. V., Kachkin, D. V., Rubel, A. A., & Георгиевич, Х. М. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920040045 · Cited by 13
Effects of TG interaction factor 1 on synthesis of estradiol and progesterone in granulosa cells of goats through SMAD2/3-SP1 signaling pathway
An, X., Cao, H., Liu, S., & Cao, B. (2021) · Animal Reproduction Science · doi:10.1016/j.anireprosci.2021.106750 · Cited by 13
Beta-hydroxybutyrate dampens adipose progenitors’ profibrotic activation through canonical Tgfβ signaling and non-canonical ZFP36-dependent mechanisms
Lecoutre, S., Merabtene, F., HACHEM, E.-K., Gamblin, C., Rouault, C., Sokolovska, N., Soula, H., Lai, W., Blackshear, P., Clément, K., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101512 · Cited by 11
“Tgfb regulates the expression of ECM genes by activation of SMAD-2/3 downstream of Tgfb receptors [28].”
Background
Montelukast prevents mice against carbon tetrachloride- and methionine-choline deficient diet-induced liver fibrosis: Reducing hepatic stellate cell activation and inflammation
Pu, S., Zhang, J., Ren, C., Zhou, H., Wang, Y., Wu, Y., Yang, S., Cao, F., & Zhou, H. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121772 · Cited by 11
Potential therapeutic and diagnostic approaches of exosomes in multiple sclerosis pathophysiology
Hasaniani, N., Nouri, S., Shirzad, M., & Rostami-Mansoor, S. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122668 · Cited by 13
VCAM-1 targeted nanocarriers of shRNA-Smad3 mitigate endothelial-to-mesenchymal transition triggered by high glucose concentrations and osteogenic factors in valvular endothelial cells
Voicu, G., Mocanu, C. A., Safciuc, F., Rebleanu, D., Anghelache, M., Cecoltan, S., Droc, I., Simionescu, M., Mânduțeanu, I., & Călin, M. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136355 · Cited by 12
Direct and indirect effects of transforming growth factor-beta on osteoclast-mediated bone remodeling using a new in vitro bone matrix model
Chiba-Ohkuma, R., Karakida, T., Yamamoto, R., & Yamakoshi, Y. (2025) · JBMR Plus · doi:10.1093/jbmrpl/ziaf104 · Cited by 12
“30 We confirmed that RANKL-induced osteo-clasts release TGF-β and that resorption pits on the β ( + )-”
SMAD-oncoprotein interplay: Potential determining factors in targeted therapies
Li, X., & Feng, X. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114155 · Cited by 13
A new glioma grading model based on histopathology and Bone Morphogenetic Protein 2 mRNA expression
Zhou, K., Zhao, Z., Li, S., Liu, Y., Li, G., & Jiang, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-75574-9 · Cited by 12
Nucleocytoplasmic Shuttling of the Mechanosensitive Transcription Factors MRTF and YAP/TAZ
Kofler, M., & Kapùs, A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_15 · Cited by 12
Advances in biological and targeted therapies for systemic sclerosis
Mulcaire-Jones, E., Low, A. H. L., Domsic, R. T., Whitfield, M. L., & Khanna, D. (2023) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2023.2196009 · Cited by 13
“TGF-β1 must be activated by proteases or integrins and has an anti-inflammatory function [51].”
Background
TRAF4/6 Is Needed for CD44 Cleavage and Migration via RAC1 Activation
Kolliopoulos, C., Chatzopoulos, A., Skandalis, S. S., Heldin, C., & Heldin, P. (2021) · Cancers · doi:10.3390/cancers13051021 · Cited by 11
Tea domain transcription factor TEAD4 mitigates TGF-β signaling and hepatocellular carcinoma progression independently of YAP
Luo, W., Li, Y., Zeng, Y. A., Li, Y., Cheng, M., Zhang, C., Li, F., Wu, Y., Huang, C., Yang, X., et al. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad010 · Cited by 13
Exploration the role of INHBA in Hu sheep granulosa cells using RNA-Seq
Bao, Y., Li, X., El-Samahy, M. A., Yang, H., Wang, Z., Yang, F., Yao, X., & Wang, F. (2022) · Theriogenology · doi:10.1016/j.theriogenology.2022.12.006 · Cited by 12
Receptor-Mediated Redox Imbalance: An Emerging Clinical Avenue against Aggressive Cancers
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“While TβRI and TβRII form a hetero-tetramer that harbors serine/threonine protein kinases in the cytoplasmic domain that are activated after binding of the ligand TGFβ, TβRIII functions as a co-receptor to increase the ligand-receptor interaction affinity without catalytic activity [23,24].”
Background
Transcriptional network governing extraembryonic endoderm cell fate choice
Pham, P. D., Lu, H., Han, H., Zhou, J. J., Madan, A., Wang, W., Murre, C., & Cho, K. W. Y. (2023) · Developmental Biology · doi:10.1016/j.ydbio.2023.07.002 · Cited by 11
“We propose that it will be crucial to distinguish the respective contributions of canonical and noncanonical BMP signaling pathways (Derynck and Budi, 2019) to the VE gene program.”
Background
The crosstalk between miRNAs and signaling pathways in human cancers: Potential therapeutic implications
Shekhar, R., Kumari, S., Vergish, S., & Tripathi, P. (2024) · International review of cytology · doi:10.1016/bs.ircmb.2023.12.001 · Cited by 11
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“21 44 Our study suggests that circWNK1 regulates SMAD7 expression via a ceRNA mechanism, subsequently influencing TGF-β signaling and tumor progression in GC.”
Notoginsenoside R1-Protocatechuic aldehyde reduces vascular inflammation and calcification through increasing the release of nitric oxide to inhibit TGFβR1-YAP/TAZ pathway in vascular smooth muscle cells
Cui, X., Zhang, L., Lin, L., Hu, Y., Zhang, M., Sun, B., Zhang, Z., Lu, M., Guan, X., Hao, J., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113574 · Cited by 11
Zero valent zinc regulates adipocyte differentiation through calpain family protein and peroxisome proliferator-activated receptor gamma signaling in mouse 3T3-L1 cells
Ramalingam, V., & Hwang, I. (2020) · Process Biochemistry · doi:10.1016/j.procbio.2020.11.022 · Cited by 11
Emerging Role of EGFR Mutations in Creating an Immune Suppressive Tumour Microenvironment
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“TGFβ is secreted and stored in a latent form and has to be activated locally [58,59].”
Background
Mechanisms involved in suppression of osteoclast supportive activity by transforming growth factor-β1 via the ubiquitin-proteasome system
Inoue, M., Nagai‐Yoshioka, Y., Yamasaki, R., Kawamoto, T., Nishihara, T., & Ariyoshi, W. (2022) · PLoS ONE · doi:10.1371/journal.pone.0262612 · Cited by 11
“TGF-β 1 binds to serine-threonine kinase receptors type I (T β RI, ALK5) and type II receptor (T β RII), which form a hetero-tetramer that specifically induces phosphorylation of the receptor activate (R) smads such as smad2 and smad3 [30].”
Expression, Polymorphism, and Potential Functional Sites of the BMPR1A Gene in the Sheep Horn
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Mechanism of TGF‑β1 inhibiting Kupffer cell immune responses in cholestatic cirrhosis
Qian, J., Jiao, Y., Wang, G., Liu, H., Cao, X., & Yang, H. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8826 · Cited by 11
“TGF-β1 is associated with polydysplasia and various human diseases, including cancer, fibrosis and autoimmune diseases (21,22).”
Background
Tetratricopeptide repeat domain 36 deficiency mitigates renal tubular injury by inhibiting TGF-β1-induced epithelial–mesenchymal transition in a mouse model of chronic kidney disease
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SMAD4 and TGFβ are architects of inverse genetic programs during fate determination of antiviral CTLs
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“Members of the TGF cytokine family elicit cellular responses via both canonical and noncanonical signaling pathways (Derynck and Budi, 2019).”
Background
Platelet-Derived Extracellular Vesicles Promote Tenogenic Differentiation of Stem Cells on Bioengineered Living Fibers
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“These results might also be related to an upregulation by EVs-derived TGF-β, a potent stimulator of ECM synthesis [58].”
BackgroundInfluential
Defining the Role of Mitochondrial Fission in Corneal Myofibroblast Differentiation
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Bifidobacterium breve CCFM1310 enhances immunity in immunosuppressed mice via modulating immune response and gut microbiota
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“The TGF-β latent complex binds to TGF-β receptors on the cell membrane, leading to phosphorylation and activation of SMAD2 and SMAD3 (Derynck and Budi 2019).”
Background
Role of Protein Phosphatases in Tumor Angiogenesis: Assessing PP1, PP2A, PP2B and PTPs Activity
Fonódi, M., Nagy, L., & Boratkó, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136868 · Cited by 10
“Reversible protein phosphorylation is one of the most common modifications of proteins to regulate their activity, conformation, interacting partners, or cellular fate.”
Background
CD4+ anti-TGF-β CAR T cells and CD8+ conventional CAR T cells exhibit synergistic antitumor effects
Zheng, D., Qin, L., Lv, J., Che, M., He, B., Zheng, Y., Lin, S., Qi, Y., Li, M., Tang, Z., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102020 · Cited by 11
A Novel Splice Variant of Human TGF-β Type II Receptor Encodes a Soluble Protein and Its Fc-Tagged Version Prevents Liver Fibrosis in vivo
Bertolio, M., la Colla, A. B., Carrea, A., Romo, A., Canziani, G., Echarte, S. M., Campisano, S., Barletta, G. P., Monzón, A. M., Rodríguez, T. M., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.690397 · Cited by 11
BMP2 suppresses the production of pentraxin 3 in human endometrial stromal and decidual stromal cells
Zhang, Y., Chang, H., Zhu, H., & Leung, P. C. K. (2022) · The FASEB Journal · doi:10.1096/fj.202200081rr · Cited by 10
Activation of TRPA1 in Bladder Suburothelial Myofibroblasts Counteracts TGF-β1-Induced Fibrotic Changes
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“The canonical downstream signal pathway of TGF-β 1 involves the phosphorylation of Smad2/3 [28].”
BackgroundInfluential

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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