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Specificity, versatility, and control of TGF-β family signaling
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Molecular function and pathway cross-talk in TGF-β signaling reveal its complexity and open questions.
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“they need to effectively interfere with the very high binding affinity (10−11 M range) of TGF-β to cell surface receptor complexes65.”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [65]
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“By design, these chimeras, based on the TβRII ligand trap, should sequester TGF-β1 and -β3 only, similarly to dimerized TβRII receptor65.”
From TGFβ biology in cancer progression and immunotherapy (2021) · cites this paper as [65]
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“TGF 1 signaling activates nucleocytoplasmic shuttling of the SMADs and SMAD3 phosphorylation (53).”
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“Another potential target for the treatment of SSc is transforming growth factor-β (TGF β ), which consists of three isoforms and has been shown to have profibrotic activity and promote collagen synthesis [89].”
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“They include branches of ERK, JNK, p38 MAPK, NF-kB, PI3K-AKT, JAKSTAT and small GTPase pathways (10, 26, 27).”
BackgroundInfluentialTransforming Growth Factor-β1 in Cancer Immunology: Opportunities for Immunotherapy
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“…is regulated by various mechanisms, including positive feedback through auto-and cross-induced TGF-β isoforms and target transcription factors (55), negative feedback through inhibitory SMADs, SMAD6 and SMAD7 ( 56), recycling of activated SMADs by dephosphorylation and poly(ADP)-ribosylation…”
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“It has been proposed that TGF‐β induces EMT of RPE cells via classical, Smad‐dependent and non‐classical, Smad‐independent, signaling (2,52).”
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“TGF β -TGF β R2/1 can also signal via noncanonical non-SMAD pathways, including TRAF6, PI3K, ERK, Akt, and mTOR, some of which are activated by TGF β receptors within caveolae (Derynck & Budi 2019).”
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“The action of TGFβ is highly context dependent and is subject to positive and negative regulation in each step of the signaling pathway [6,20].”
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“Smads are latent cytoplasmic transcription factors and major TGF-β signal transducers [50,52,53].”
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“The complex then translocates to the nucleus to regulate the target gene expression [94, 96].”
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“Mammals express 3 closely related TGFb isoforms, TGFb1, TGFb2, and TGFb3, which bind to and signal through the TGFb receptor complex.(5) Transforming growth factor-b is present on the cell surface or within tissue matrix as latent TGFb, in which the TGFb prodomain remains noncovalently associated with the growth facto…”
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“The heteromeric effector complex is translocated to the nucleus to regulate the specific target gene expression.(22,25) Meanwhile, the TGFβ1-Smad pathway also has a negative feedback mechanism mediated by the inhibitory Smad7 that competitively binds to TβR1 and blocks the Smad intracellular signal transduction.”
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“For example, whereas transforming growth factor-beta (TGFb) is widely implicated as a pro-fibrotic cytokine involved in SSc [8], it has multiple other functions and is produced in an inactive ‘latent’ form, often attached to cell surface proteins and/or extracellular matrix components, which can in turn be activated v…”
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“TGF-β activates these receptor complexes and ultimately Smad2 and Smad3 through phosphorylation by TβRI (Figure 2) [32].”
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“Then, mature TGF-b binds LAP through both covalent (disulfide bridges) and non-covalent interactions (32).”
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“Phosphorylated TGFBR1 promoted the nuclear translocation of SMAD2/3 which eventually regulated the transcription of downstream genes [29].”
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“The Smad2/3-Smad4 complex, after translocation to the nucleus, in cooperation with other transcription factors, coactivators, and corepressors, modulates the expression of TGFβ responsive genes [25,54,77] (Figure 2).”
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The Research Progress in Transforming Growth Factor-β2
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“Upon BMP stimulation, pSmad1/5/8 translocates into the nucleus and undergoes dephosphorylation of its C-terminal sites by protein phosphatases, followed by recycling via nucleocytoplasmic shuttling [27,31,125,126].”
BackgroundMultiple Myeloma Bone Disease: Implication of MicroRNAs in Its Molecular Background
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“BMPs, which are members of the TGF-β superfamily and have been shown to play an also controversial role in MMBD [70].”
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“This intricate regulation underscores the versatility of the TGF‑ β /Smad signaling pathway in main‑ taining cellular homeostasis and its potential as a therapeutic target in diseases characterized by aberrant TGF‑ β signaling, such as fibrosis (48,49).”
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“Deregulation of TGF-b signaling leads to developmental anomalies and disease, whereas enhanced TGF-b signaling contributes to cancer and fibrosis (Derynck and Budi, 2019).”
BackgroundThe role of leucine-rich alpha-2-glycoprotein-1 in proliferation, migration, and invasion of tumors
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“It has been found that both TβRII and TβRII receptors contain active kinase fragments with signal transduction function (Derynck and Budi 2019; Nickel et al.”
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“These results might also be related with an upregulation by TGF-β, a potent stimulator of ECM synthesis [55], which was higher in mEVs than in sEVs (Figure 1Biii).”
BackgroundLu, F., Chen, S., Shi, W., Su, X., Wu, H., & Liu, M. (2022) · PLoS ONE · doi:10.1371/journal.pone.0269094 · Cited by 23
“The human TGF-β family includes 33 genes that encode for homodimeric or heterodimeric secreted cytokines [27, 28].”
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“activation via PI3K‐Akt‐mTOR signaling Previous studies have shown that the PI3K-Akt-mTOR signaling pathway is activated by TGF-β and promotes protein synthesis and cell metabolism, which are required for cell growth, proliferation, and differentiation [22].”
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“The TGF-β signaling pathway [48] plays an important role in the regulation of cell fate during embryonic development and the maintenance of adult tissue homeostasis.”
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The phosphorylation of the Smad2/3 linker region by nemo-like kinase regulates TGF-β signaling
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“The TGF-β ligand binds to TβRII, a constitutively active serine/threonine kinase, which further recruits and phosphorylates TβRI (4).”
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“However, as with other signal transduction pathways, there are many nuances to TGF-β superfamily signaling that act to confer specificity to ligand actions.(70) Notably, TGFB1 binds to a completely different receptor complex compared”
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“The BMPs belong to the family of Transforming Growth Factor β (TGFβ) secreted growth and differentiation factors [1,9].”
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“TGF-β belongs to the TGF superfamily and provides tissue-specific control over proliferation and cell-and tissue-specific motility [41].”
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“After cleavage of the signal peptide, the polypeptide is further processed by proteases to separate the prodomain (termed latency-associated polypeptide (LAP)) from the mature polypeptide, which remains non-covalently associated (Derynck & Budi 2019).”
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Challenges and Opportunities for Drug Repositioning in Fibrodysplasia Ossificans Progressiva
Ventura, F., Williams, E., Ikeya, M., Bullock, A. N., ten Dijke, P., Goumans, M., & Sánchez‐Duffhues, G. (2021) · Biomedicines · doi:10.3390/biomedicines9020213 · Cited by 21
“ALK2R206H requires its type II receptor partners, BMPR2 and ActRIIa to signal after engaging either BMP-6/7 or activin A, but it does not seem to require their type I receptor partners ALK3 or ALK6 [54,56].”
BackgroundInfluentialThe multi-faceted roles of TGF-β in regulation of immunity to infection
Maizels, R. M. (2021) · Advances in immunology · doi:10.1016/bs.ai.2021.05.001 · Cited by 19
Hepsin regulates TGFβ signaling via fibronectin proteolysis
Belitškin, D., Pant, S. M., Munne, P., Suleymanova, I., Belitškina, K., Hongisto, H., Englund, J. I., Raatikainen, T., Klezovitch, O., Vasioukhin, V. I., et al. (2021) · EMBO Reports · doi:10.15252/embr.202152532 · Cited by 22
“TGF b signaling regulation occurs via two discrete activation steps: the processing of latent-TGF b in the extracellular compartment and TGF b receptor-induced activation of downstream signaling, which includes phosphorylation of receptor-associated Smads (R-Smads), such as Smad2 and Smad3 (Derynck & Budi, 2019).”
InfluentialAbrial, M., Basu, S., Huang, M., Butty, V. L., Schwertner, A., Jeffrey, S., Jordan, D., Burns, C. E., & Burns, C. G. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.046979 · Cited by 21
Evaluation of CRISPR/Cas9 mediated TGIF gene editing to inhibit corneal fibrosis in vitro
Tripathi, R., Sinha, N. R., Kempuraj, D., Balne, P. K., Landreneau, J. R., Juneja, A., Webel, A. D., & Mohan, R. R. (2022) · Experimental Eye Research · doi:10.1016/j.exer.2022.109113 · Cited by 21
Regulation and Signaling of TGF-β Autoinduction.
Hariyanto, N. I., Yo, E. C., & Wanandi, S. I. (2021) · PubMed · doi:10.22088/ijmcm.bums.10.4.234 · Cited by 22
“Precursor polypeptides consist of three segments: the peptide segment of the amino-terminal hydrophobic signal that will be released when the protein translocated into the lumen of the rough endoplasmic reticulum, the precursor segment or the N-terminal pro-domain, and the C-terminal segment that will become an active…”
BackgroundJang, H. Y., Kim, S., Park, K., & Kim, J. H. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05851-8 · Cited by 21
Clinical impact of epithelial–mesenchymal transition for cancer therapy
Mukerjee, N., Nag, S., Bhattacharya, B., Alexiou, A. T., Mirgh, D., Mukherjee, D., Adhikari, M. D., Anand, K., Muthusamy, R., Gorai, S., et al. (2024) · Clinical and Translational Discovery · doi:10.1002/ctd2.260 · Cited by 22
Carver, W. E., Fix, E., Fix, C., Fan, D., Chakrabarti, M., & Azhar, M. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30416 · Cited by 21
Pucci, M., Moschetti, M., Urzì, O., Loria, M., Conigliaro, A., Bella, M. A. D., Crescitelli, R., Bagge, R. O., Gallo, A., Santos, M. F., et al. (2023) · Cancer Cell International · doi:10.1186/s12935-023-02916-8 · Cited by 22
TGF-β Isoforms and GDF-15 in the Development and Progression of Atherosclerosis
Liuizė, A., & Mongirdienė, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042104 · Cited by 20
“The role of TGF-β in cell migration, proliferation, differentiation, extracellular matrix production and adhesion is still controversial [10,12,17,18].”
BackgroundOptogenetic approaches to investigate spatiotemporal signaling during development
Rogers, K. W., & Müller, P. (2019) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2019.11.009 · Cited by 23
Brkić, J., Dunk, C., Shan, Y., O’Brien, J. A., Lye, P., Qayyum, S., Yang, P., Matthews, S. G., Lye, S. J., & Peng, C. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00436 · Cited by 20
Luo, K., He, J., Yu, D., & Açil, Y. (2019) · Europe PMC (PubMed Central) · Cited by 19
Harnessing Carcinoma Cell Plasticity Mediated by TGF-β Signaling
Wang, X., & Thiery, J. P. (2021) · Cancers · doi:10.3390/cancers13143397 · Cited by 18
“The regulatory Smad2/3 proteins then form a trimeric complex with the co-Smad4 (Smad2/3/4) and translocate into the nucleus to regulate target gene transcription [77].”
BackgroundBiological role of heparan sulfate in osteogenesis: A review
Xu, Z., Chen, S., Feng, D., Liu, Y., Wang, Q., Gao, T., Liu, Z., Zhang, Y., Chen, J., & Qiu, L. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118490 · Cited by 23
TGF‐β1 signaling and Smad7 control T‐cell responses in health and immune‐mediated disorders
Laudisi, F., Stolfi, C., Monteleone, I., & Monteleone, G. (2023) · European Journal of Immunology · doi:10.1002/eji.202350460 · Cited by 22
“…hypothesis is that TGF-β 1-mediated induction of the transcription factor forkhead box P3 (Foxp3), the lineage-specific transcription factor that is essential for the development of Tregs, occurs through a pathway that does not require direct binding of Smad molecules to the Foxp3 locus [17, 23].”
BackgroundTakahashi, K., Kobayashi, M., Katsumata, H., Tokizaki, S., Anzai, T., Ikeda, Y., Alcaide, D., Maeda, K., Ishihara, M., Tahara, K., et al. (2023) · Cancer Science · doi:10.1111/cas.16045 · Cited by 19
“3 TGF-β binds to serine–threonine kinase type receptors (TGF-β type I and type II receptors; T β RI and T β RII) 4 and phosphorylates Smad2/3.”
BackgroundInfluentialJiménez-Ortega, R. F., Ortega-Meléndez, A. I., Patiño, N., Rivera‐Paredez, B., Hidalgo‐Bravo, A., & Velázquez‐Cruz, R. (2024) · Biology · doi:10.3390/biology13070505 · Cited by 19
“The transforming growth factors bind to a tetrameric receptor complex comprising two TGF-β receptors of the type I (T β RI/ALK5) and two type II receptor kinases (T β RII) [88].”
BackgroundLiu, K., Tian, F., Chen, X., Liu, B., Tian, S., Hou, Y., Wang, L., Han, M., Peng, S., Tan, Y., et al. (2024) · Advanced Science · doi:10.1002/advs.202402327 · Cited by 19
Pulmonary Arterial Hypertension and TGF-β Superfamily Signaling: Focus on Sotatercept
Stump, B., & Waxman, A. B. (2024) · BioDrugs · doi:10.1007/s40259-024-00680-3 · Cited by 20
“The TGF-β superfamily is composed of 30 structurally similar cytokines that include the prototypic TGF-β proteins as well as activins, BMPs, GDFs, and Müllerian inhibiting sub-stances (MIS), and their respective cognate receptor complexes [13].”
Chawalitpong, S., Ichikawa, S., Uchibori, Y., Nakamura, S., & Katayama, S. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b02725 · Cited by 19
TGFβ as a gatekeeper of BMP action in the developing growth plate
Wang, W., Rigueur, D., & Lyons, K. M. (2020) · Bone · doi:10.1016/j.bone.2020.115439 · Cited by 19
Protective effect of Alpinetin on rats with chronic obstructive pulmonary disease
Su, Y., Tao, X., & Xu, J. (2020) · Food Science & Nutrition · doi:10.1002/fsn3.1952 · Cited by 19
“∗∗p < .01 compared with the control group; ##p < .01 compared with COPD group as cell proliferation, division, apoptosis, immune, and inflammatory responses (Derynck & Budi, 2019; Ma et al., 2018; Massagué et al., 2005).”
ResultSolomonov, I., Kollet, Ó., & Sagi, I. (2025) · FEBS Journal · doi:10.1111/febs.70292 · Cited by 22
Chu, K., Malik, A., Thamilselvan, V., & Martı́nez-Hackert, E. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102076 · Cited by 20
Arl15 upregulates the TGFβ family signaling by promoting the assembly of the Smad-complex
Shi, M., Tie, H. C., Mahajan, D., Sun, X., Zhou, Y., Boh, B. K., Vardy, L. A., & Lü, L. (2022) · eLife · doi:10.7554/elife.76146 · Cited by 18
“5a) had increased presence in the nucleus under the same treatment, consistent with our current knowledge of the TGFβ family signaling pathway(Derynck and Budi, 2019; Massague, 2012; Schmierer and Hill, 2007; Wrana, 2013).”
BackgroundResultInfluentialYakymovych, I., Yakymovych, M., Hamidi, A., Landström, M., & Heldin, C. (2022) · Science Signaling · doi:10.1126/scisignal.abp9521 · Cited by 19
“The kinase activity of TβRII is necessary for Src activation by TGF-β1 The binding of TGF-β1 to TβRII and TβRI is known to stabilize the receptor complex (3, 4).”
BackgroundInfluentialWang, L., Gu, S., Chen, F., Yu, Y., Cao, J., Li, X., Gao, C., Chen, Y., Yuan, S., Liu, X., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01327-5 · Cited by 19
“After phosphorylation, Smad2/3 forms a trimeric complex with Smad4 and transduces its transcriptional functions.(1,4) This process is sophisticatedly modulated in a context-dependent manner.”
BackgroundFrom bench to bedside: The promise of sotatercept in hematologic disorders
Lan, Z., Lv, Z., Zuo, W., & Xiao, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115239 · Cited by 18
Regulatory expression of bone morphogenetic protein 6 by 2,2′-dipyridyl
Noguchi, T., Ikeda, M., Murakami, M., Masuzawa, M., Imamura, T., Hashimoto, O., Matsui, T., & Funaba, M. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129610 · Cited by 18
Metadata
- Authors
- Derynck, R., & Budi, E. H.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Derynck, Rik
- Venue
- Science Signaling
- Published
- 2019-02-26
- Volume
- 12
- Issue
- 570
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- 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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