The Fibroblast Growth Factor signaling pathway
Open accessAbstract
The signaling component of the mammalian Fibroblast Growth Factor ( FGF ) family is comprised of eighteen secreted proteins that interact with four signaling tyrosine kinase FGF receptors ( FGFRs ). Interaction of FGF ligands with their signaling receptors is regulated by protein or proteoglycan cofactors and by extracellular binding proteins. Activated FGFRs phosphorylate specific tyrosine residues that mediate interaction with cytosolic adaptor proteins and the RAS‐MAPK , PI3K‐AKT , PLCγ , and STAT intracellular signaling pathways. Four structurally related intracellular non‐signaling FGFs interact with and regulate the family of voltage gated sodium channels. Members of the FGF family function in the earliest stages of embryonic development and during organogenesis to maintain progenitor cells and mediate their growth, differentiation, survival, and patterning. FGFs also have roles in adult tissues where they mediate metabolic functions, tissue repair, and regeneration, often by reactivating developmental signaling pathways. Consistent with the presence of FGFs in almost all tissues and organs, aberrant activity of the pathway is associated with developmental defects that disrupt organogenesis, impair the response to injury, and result in metabolic disorders, and cancer. WIREs Dev Biol 2015, 4:215–266. doi: 10.1002/wdev.176 This article is categorized under: Early Embryonic Development > Development to the Basic Body Plan Nervous System Development > Vertebrates: General Principles Birth Defects > Organ Anomalies
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The fibroblast growth factor signaling pathway, particularly FGF-1 and FGF-2, plays a crucial role in hepatocyte division and angiogenesis.
“The fibroblast growth factor (FGF) signalling pathway - particularly FGF-1 and FGF-2—plays a crucial role in hepatocyte division and angiogenesis.”
From Liver regeneration after partial hepatectomy: Triggers and mechanisms (2025) · cites this paper as [64]
The Pathway Components section reports that FGF1 and FGF2 promote endothelial-cell proliferation, and the Pathway Regulation section describes an FGF1/FGF2-binding protein as pro-angiogenic. But the hepatocyte proliferative signal identified in Pathway Components is FGF19 acting through FGFR4; the copy does not establish that FGF1 or FGF2 drives hepatocyte division. Page numbers were not available in the indexed passages. (LLM, conf=0.88)
Experimental — accuracy not yet measuredFGF-2 participates in balancing liver fibrosis and regeneration, indicating a dual role in hepatic homeostasis.
“Importantly, FGF-2 also participates in balancing liver fibrosis and regeneration, highlighting its dual role in hepatic homeostasis[64].”
From Liver regeneration after partial hepatectomy: Triggers and mechanisms (2025) · cites this paper as [64]
The Introduction (page unavailable) links endothelial FGF-receptor signaling to liver regeneration and fibrosis, and says FGF signaling may increase or decrease tissue fibrosis. It does not identify FGF-2 as the factor balancing these processes in the liver, so the FGF-2-specific claim is unsupported. (LLM, conf=0.82)
Experimental — accuracy not yet measuredDuctular profiles were observed not only in portal tracts or periportal zones, but also within liver lobules including adjacent areas to various caliber branches of liver veins.
“Besides, the ductular profiles were observed not only in the portal tracts or periportal zones, but also within the liver lobules including the adjacent areas to the various caliber branches of the liver veins (Figure 4)[64].”
From Liver regeneration after partial hepatectomy: Triggers and mechanisms (2025) · cites this paper as [64]
The Pathway Components passage discusses FGF signaling in hepatocytes, while the References mention liver-related studies; neither addresses where ductular profiles were observed. Searches for ductular profiles in portal, periportal, and lobular areas, including areas near liver veins, found no supporting passage in our copy. (LLM, conf=0.76)
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The breadth of FGF21's metabolic actions are governed by FGFR1 in adipose tissue
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FGF binding and FGF receptor activation by synthetic heparan-derived di- and trisaccharides.
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FGF/FGFR signaling in health and disease
Xie, Y., Su, N., Yang, J., Tan, Q., Huang, S., Jin, M., Ni, Z., Zhang, B., Zhang, D., Luo, F., et al. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00222-7 · Cited by 904 · see citing works
Targeting fibrosis: mechanisms and clinical trials
Zhao, M., Wang, L., Wang, M., Zhou, S., Lu, Y., Cui, H., Racanelli, A. C., Zhang, L., Ye, T., Ding, B., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01070-3 · Cited by 547 · see citing works
Sanyal, A., Charles, E. D., Neuschwander-Tetri, B. A., Loomba, R., Harrison, S. A., Abdelmalek, M. F., Lawitz, E. J., Halegoua-DeMarzio, D., Kundu, S., Noviello, S., et al. (2018) · The Lancet · doi:10.1016/s0140-6736(18)31785-9 · Cited by 550 · see citing works
The Role of Fibroblast Growth Factor (FGF) Signaling in Tissue Repair and Regeneration
Farooq, M., Khan, A. W., Kim, M., & Choi, S.-D. (2021) · Cells · doi:10.3390/cells10113242 · Cited by 342 · see citing works
“Their binding affinity with heparan sulfate is relatively lower [34].”
BackgroundKrook, M. A., Reeser, J. W., Ernst, G., Barker, H. D., Wilberding, M., Li, G., Chen, H., & Roychowdhury, S. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01157-0 · Cited by 369 · see citing works
Fibroblast Growth Factor 21—Metabolic Role in Mice and Men
Staiger, H., Keuper, M., Berti, L., Hrabě de Angelis, M., & Häring, H.-U. (2017) · Endocrine Reviews · doi:10.1210/er.2017-00016 · Cited by 270 · see citing works
Savin, I. A., Аркадьевна, З. М., & Васильевна, С. А. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314959 · Cited by 288 · see citing works
Alzheimer’s Disease: An Update and Insights Into Pathophysiology
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Role of JAK/STAT in Interstitial Lung Diseases; Molecular and Cellular Mechanisms
Montero, P., Milara, J., Roger, I., & Cortijo, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126211 · Cited by 260 · see citing works
“FGF is also increased in the lung of progressive fibrosing-ILD [53] and activated FGF-receptor phosphorylates STAT1, STAT3, and STAT5 [38,39,54].”
BackgroundThree subtypes of lung cancer fibroblasts define distinct therapeutic paradigms
Hu, H., Piotrowska, Z., Hare, P. J., Chen, H., Mulvey, H. E., Mayfield, A., Noeen, S., Kattermann, K. E., Greenberg, M., Williams, A. F., et al. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.09.003 · Cited by 260 · see citing works
Fibroblast growth factor 19 regulates skeletal muscle mass and ameliorates muscle wasting in mice
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Targeting FGFR overcomes EMT-mediated resistance in EGFR mutant non-small cell lung cancer
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Fibroblast Growth Factor in Diabetic Foot Ulcer: Progress and Therapeutic Prospects
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The quiescent endothelium: signalling pathways regulating organ-specific endothelial normalcy
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FGFR-targeted therapeutics: clinical activity, mechanisms of resistance and new directions
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“FGFR#b and FGFR#c are splice variants derived from FGFR1 – 3 with distinct ligand-binding affinities, owing to divergence in the latter half of the third immunoglobulin-like domain 27,30 .”
Tillman, E. J., & Rolph, T. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.601290 · Cited by 209 · see citing works
“The bKlotho/FGF21 receptor complex interacts specifically with the cognate receptors: FGFR1c, FGFR2c, or FGFR3c (40, 41), enabling downstream FGFR signaling via pathways including the mitogen-activated protein kinase (MAPK) and AKT signaling networks (79).”
BackgroundFGF23 signalling and physiology
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Inhibition of FGF‐FGFR and VEGF‐VEGFR signalling in cancer treatment
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Cardoneanu, A., Macovei, L., Burlui, A., Mihai, I., Bratoiu, I., Rezus, I., Richter, P., Tamba, B., & Rezuș, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010171 · Cited by 168 · see citing works
“There are 22 ligands in the FGF family, all of which bind to one of four different FGFRs to perform various tasks [46].”
BackgroundHarrison, S. A., Rolph, T., Knott, M., & Dubourg, J. (2024) · Journal of Hepatology · doi:10.1016/j.jhep.2024.04.034 · Cited by 176 · see citing works
Niu, Z., Jin, R., Zhang, Y., & Li, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01200-x · Cited by 172 · see citing works
Multi-omic Profiling Reveals Dynamics of the Phased Progression of Pluripotency
Yang, P., Humphrey, S. J., Cinghu, S., Pathania, R., Oldfield, A. J., Kumar, D., Perera, D., Yang, J. Y. H., James, D. E., Mann, M., et al. (2019) · Cell Systems · doi:10.1016/j.cels.2019.03.012 · Cited by 146 · see citing works
New developments in the biology of fibroblast growth factors
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Self-citationCancer Stem Cells—Key Players in Tumor Relapse
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The Effect of Platelet-Rich Plasma on the Intra-Articular Microenvironment in Knee Osteoarthritis
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Ruan, R., Li, L., Li, X., Huang, C., Zhanmin, Z., Zhong, H., Zeng, S., Shi, Q., Yang, X., Zeng, Q., et al. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01761-7 · Cited by 130 · see citing works
“FGF/FGFR signaling oncogenic dysregulation and treatment FGF was originally extracted from the brain and pituitary gland as a mitogen for fibroblasts, and the 22 identified FGFs are divided into two major groups according to their function; secreted signaling proteins that signal to RTK(FGF1-10,16–23), and intracellul…”
BackgroundMolecular signaling in temporomandibular joint osteoarthritis
Lu, K., Ma, F., Yi, D., Yu, H., Tong, L.-P., & Chen, D. (2021) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2021.07.001 · Cited by 118 · see citing works
“exert various functions mainly through binding to 4 distinct FGF receptors (FGFRs) [64].”
BackgroundFibroblast Growth Factor Receptors (FGFRs) and Noncanonical Partners in Cancer Signaling
Ferguson, H. R., Smith, M. P., & Francavilla, C. (2021) · Cells · doi:10.3390/cells10051201 · Cited by 137 · see citing works
“FGF oncogenic signaling primarily occurs through FGFR1-4 amplification, translocation and/or increased expression, and very rarely have mutations in FGF genes been associated with oncogenic signaling [3].”
BackgroundTargeting FGFR for cancer therapy
Zhang, P., Yue, L., Leng, Q.-Q., Chang, C., Gan, C.-L., Ye, T., & Cao, D. (2024) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01558-1 · Cited by 113 · see citing works
“The canonical downstream signaling routes of FGF/FGFR encompass the Ras/Raf-MEK-MAPK (mitogen-activated protein kinase) pathway, phosphatidylinositol-3 kinase/ protein kinase B (PI3K/AKT) pathway, PLCγ pathway, as well as signaling intermediates and transcription activators (STATs) [7, 21].”
BackgroundDiabetic Wound Repair: From Mechanism to Therapeutic Opportunities
Wang, R., Gu, S., Kim, Y. H., Lee, A., Lin, H., & Jiang, D. (2025) · MedComm · doi:10.1002/mco2.70406 · Cited by 111 · see citing works
“Endocrine FGFs influence carbohydrate and lipid metabolism, while paracrine FGFs drive processes like angiogenesis, fibroblast proliferation, and granulation tissue formation [297, 298].”
Comprehensive multi-omic profiling of somatic mutations in malformations of cortical development
Chung, C., Yang, X., Bae, T., Vong, K. I., Mittal, S., Donkels, C., Phillips, H. W., Li, Z., Marsh, A. P. L., Breuss, M. W., et al. (2023) · Nature Genetics · doi:10.1038/s41588-022-01276-9 · Cited by 107 · see citing works
Fibroblast Growth Factor Signalling in the Diseased Nervous System
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Targeting Fibrosis: From Molecular Mechanisms to Advanced Therapies
Di, X., Li, Y., Wei, J., Li, T., & Liao, B. (2024) · Advanced Science · doi:10.1002/advs.202410416 · Cited by 83 · see citing works
FGF/FGFR signaling: From lung development to respiratory diseases
Yang, L., Zhou, F., Zheng, D., Wang, D., Li, X., Zhao, C., & Huang, X. (2021) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2021.09.002 · Cited by 116 · see citing works
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Markers of liver regeneration—the role of growth factors and cytokines: a systematic review
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FGF/FGFR-Dependent Molecular Mechanisms Underlying Anti-Cancer Drug Resistance
Szymczyk, J., Służalska, K., Materla, I., Opalinski, L., Otlewski, J., & Zakrzewska, M. (2021) · Cancers · doi:10.3390/cancers13225796 · Cited by 80 · see citing works
Growth and mechanobiology of the tendon-bone enthesis
Killian, M. L. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.07.015 · Cited by 74 · see citing works
Signaling pathways in liver cancer: pathogenesis and targeted therapy
Xue, Y., Ruan, Y., Wang, Y., Xiao, P., & Xu, J. (2024) · Molecular Biomedicine · doi:10.1186/s43556-024-00184-0 · Cited by 81 · see citing works
FGFR families: biological functions and therapeutic interventions in tumors
Liu, Q., Huang, J., Yan, W., Liu, Z., Liu, S., & Fang, W. (2023) · MedComm · doi:10.1002/mco2.367 · Cited by 77 · see citing works
Cellular Mechanisms of FGF-Stimulated Tissue Repair
Prudovsky, I. (2021) · Cells · doi:10.3390/cells10071830 · Cited by 77 · see citing works
“Moreover, the FGFR signaling is tightly controlled by a group of negative regulators, including SPRY1-4, SEF, DUSP6, SHP2, and CBL [5,8].”
BackgroundInfluentialThe context-dependent, combinatorial logic of BMP signalingPreprint
Klumpe, H. E., Langley, M. A., Linton, J. M., Su, C. J., Antebi, Y., & Elowitz, M. (2020) · bioRxiv · doi:10.1101/2020.12.08.416503 · Cited by 77 · see citing works
“Cell-cell communication pathways such as BMP, Wnt, and FGF play pivotal roles in normal development, disease, therapeutics, and regenerative medicine (Nusse, 2005; Ornitz and Itoh, 2015; Salazar et al., 2016).”
BackgroundMyofibroblast dedifferentiation proceeds via distinct transcriptomic and phenotypic transitions
Fortier, S. M., Penke, L. R. K., King, D., Pham, T. X., Ligresti, G., & Peters-Golden, M. L. (2021) · JCI Insight · doi:10.1172/jci.insight.144799 · Cited by 90 · see citing works
“Next, we explored FGF2 signaling and found that its ability to reduce expression of α SMA and collagen I was overcome by inhibition of the MEK/ERK pathway (Figure 1E and Supplemental Figure 1A; supplemental material available online with this article; https://doi.org/10.1172/jci.insight.144799DS1) but not by inhibitio…”
InfluentialTan, Y., Zhou, H., Lin, Y.-J., Yi, L., Chen, Z.-G., Cao, Q.-D., Guo, Y., Wang, Z.-N., Chen, S.-D., Li, Y., et al. (2022) · Military Medical Research · doi:10.1186/s40779-022-00366-3 · Cited by 73
“FGF2 belongs to the larger FGF family, and four highaffinity receptor tyrosine kinases have been identified as FGF receptors (FGFRs), including FGFR1 to FGFR4 [4].”
BackgroundVEGF-B prevents excessive angiogenesis by inhibiting FGF2/FGFR1 pathway
Lee, C., Chen, R., Sun, G., Liu, X., Lin, X., He, C., Xing, L., Liu, L., Jensen, L. D., Kumar, A., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01539-9 · Cited by 72 · see citing works
“2h, i), consistent with previous observations.(35) An SPR assay showed that VEGF-B bound to FGFR1 DII-III with a KD value similar to that of FGF2 (49 nM for VEGF-B and 63 nM for FGF2; Fig.”
ResultSelf-citationMolecular mechanisms of stem/progenitor cell maintenance in the adrenal cortex
Lerario, A. M., Finco, I., LaPensee, C., & Hammer, G. D. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00052 · Cited by 68 · see citing works
Ardizzone, A., Bova, V., Casili, G., Repici, A., Lanza, M., Giuffrida, R., Colarossi, C., Mare, M., Cuzzocrea, S., Esposito, E., et al. (2023) · Cells · doi:10.3390/cells12071002 · Cited by 73 · see citing works
Khosravi, F., Ahmadvand, N., Bellusci, S., & Sauer, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672935 · Cited by 74 · see citing works
“Based on a phylogenetic analysis, FGFs are categorized into 7 subfamilies, which are either intracellular or secreted factors with autocrine, paracrine, and/or endocrine functions (Ornitz and Itoh, 2015).”
BackgroundDolivo, D. M., Larson, S. A., & Dominko, T. (2017) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2017.08.013 · Cited by 69 · see citing works
PERK regulates skeletal muscle mass and contractile function in adult mice
Gallot, Y. S., Bohnert, K. R., Straughn, A. R., Xiong, G., Hindi, S. M., & Kumar, A. (2019) · The FASEB Journal · doi:10.1096/fj.201800683rr · Cited by 67 · see citing works
FGF23 and Vitamin D Metabolism
Latic, N., & Erben, R. (2021) · JBMR Plus · doi:10.1002/jbm4.10558 · Cited by 67 · see citing works
“FGF receptors are tyrosine kinase receptors, inducing phosphorylation of downstream molecules after ligand binding.((19)) In contrast to paracrine FGFs, endocrine FGFs lack a functional heparan sulfate-binding domain, and require the presence of the transmembrane co-receptor proteins αKlotho and βKlotho for high affin…”
BackgroundRole of fibroblast growth factor signalling in hepatic fibrosis
Seitz, T., & Hellerbrand, C. (2021) · Liver International · doi:10.1111/liv.14863 · Cited by 64 · see citing works
Signaling Pathways in Bone Development and Their Related Skeletal Dysplasia
Guasto, A., & Cormier‐Daire, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094321 · Cited by 84 · see citing works
“These proteins activate multiple signaling pathways, including JAK-STAT, proteinase kinase C (PKC), mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase (PI3K), [138].”
BackgroundThe Potential of FGF-2 in Craniofacial Bone Tissue Engineering: A Review
Novais, A., Chatzopoulou, E., Chaussain, C., & Gorin, C. (2021) · Cells · doi:10.3390/cells10040932 · Cited by 61 · see citing works
“Canonical FGFs exert their pleiotropic effects by binding and activating the FGFR subfamily of receptor tyrosine kinases that are coded by four genes (FGFR-1, FGFR-2, FGFR3, and FGFR-4) in mammals.”
BackgroundInfluentialTang, L.-Y., Wu, M., Lu, S.-Y., Zhang, H.-X., Shen, Y., Shen, C.-L., Liang, H., Ge, H.-Y., Ding, X., & Wang, Z.-G. (2020) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.4230 · Cited by 61 · see citing works
“FGF9 binds to FGFRs to activate downstream cascades, including MAPK, PI3K/AKT, and PLCγ, that transduce multiple signals to regulate cell proliferation and differentiation.((7)) PathScan RTK signaling antibody array and Western blot analysis of MC3T3-E1 cells showed that wild-type FGF9 protein significantly activated…”
BackgroundRecent Advances in Craniosynostosis
Yilmaz, E., Mihci, E., Nur, B., Alper, Ö. M., & Taçoy, Ş. (2019) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2019.01.018 · Cited by 63 · see citing works
Li, H.-Z., Zhang, J., Yuan, D., Xie, W.-Q., Ladel, C., Mobasheri, A., & Li, Y. (2024) · Military Medical Research · doi:10.1186/s40779-024-00544-5 · Cited by 60 · see citing works
“FGFs share a similar core structure comprising 120 – 130 amino acids arranged in 12 antiparallel β chains (β1-12), which exhibit high affinity for FGFRs and heparin [12].”
BackgroundIrreversibility of Pulmonary Fibrosis
Yu, Q. Y., & Tang, X. X. (2022) · Aging and Disease · doi:10.14336/ad.2021.0730 · Cited by 82 · see citing works
“In addition, genes related to lung development (such as FGF10) are markedly increased in the resolution stage of BLM-induced pulmonary fibrosis [34, 35].”
BackgroundRole of bFGF in Acquired Resistance upon Anti-VEGF Therapy in Cancer
Zahra, F. T., Sajib, M. S., & Mikelis, C. M. (2021) · Cancers · doi:10.3390/cancers13061422 · Cited by 60 · see citing works
“Among the members of the FGF1 subfamily, FGF1 can bind all FGFRs whereas bFGF has preference to the c isoforms of FGFR1, FGFR2 and FGFR3 [39,40].”
BackgroundInfluentialDecoding FGF/FGFR Signaling: Insights into Biological Functions and Disease Relevance
Edirisinghe, O., Ternier, G., Alraawi, Z., & Kumar, T. K. S. (2024) · Biomolecules · doi:10.3390/biom14121622 · Cited by 60 · see citing works
Lim, M. Y. C., & Ho, H. K. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115985 · Cited by 59 · see citing works
Chen, M. Z., Chang, J. C., Zavala-Solorio, J., Kates, L., Thai, M., Ogasawara, A., Bai, X., Flanagan, S., Nunez, V., Phamluong, K., et al. (2017) · Molecular Metabolism · doi:10.1016/j.molmet.2017.09.003 · Cited by 58 · see citing works
Biological and pharmacological functions of the FGF19- and FGF21-coreceptor beta klotho
Aaldijk, A. S., Verzijl, C. R. C., Jonker, J. W., & Struik, D. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1150222 · Cited by 63 · see citing works
“Ultimately, altered FGFR activity is linked to the modulation of a wide range of cellular responses, such as growth, proliferation, differentiation, migration, and apoptosis (13).”
BackgroundLatic, N., & Erben, R. G. (2022) · Nutrients · doi:10.3390/nu14235186 · Cited by 61 · see citing works
“FGFRs are tyrosine kinase receptors, and ligand binding results in dimerization and subsequent activation of intracellular phosphorylation cascades [54].”
BackgroundBiological Significance and Targeting of the FGFR Axis in Cancer
Chioni, A., & Grose, R. (2021) · Cancers · doi:10.3390/cancers13225681 · Cited by 58 · see citing works
“Paracrine FGFs bind strongly to HSPGs, which possess cofactor functions to prevent the FGFs from diffusing through the extracellular matrix (ECM) as well as regulating the FGFR specificity [11,18].”
BackgroundInfluentialImproved cryopreservation of in vitro produced bovine embryos using FGF2, LIF, and IGF1
Stoecklein, K., Ortega, M., Spate, L., Murphy, C., & Prather, R. (2021) · PLoS ONE · doi:10.1371/journal.pone.0243727 · Cited by 58
“Growth factors such as LIF, IGF1, and FGF2 activate the mitogen-activated protein kinase (MAPK) signaling cascade [51, 55, 56], which has a role in cellular metabolism and lipolysis [57–59].”
BackgroundTargeting the Fibroblast Growth Factor Receptor (FGFR) Family in Lung Cancer
Pacini, L., Jenks, A. D., Lima, N. C., & Huang, P. H. (2021) · Cells · doi:10.3390/cells10051154 · Cited by 56 · see citing works
“The region outside the conserved core is comprised of variable amino acid sequences that determine the selectivity of binding of distinct FGFs to different FGFR family members [9].”
BackgroundPreclinical characterization of bemarituzumab, an anti-FGFR2b antibody for the treatment of cancer
Xiang, H., Chan, A., Ahene, A., Bellovin, D., Deng, R., Hsu, A. W., Jeffry, U., Palencia, S., Powers, J. M., Zanghi, J., et al. (2021) · mAbs · doi:10.1080/19420862.2021.1981202 · Cited by 56 · see citing works
“FGF-mediated phosphorylation of FGFR2b activates a signal transduction cascade that ultimately results in cell proliferation.(15) Therefore, the effect of bemarituzumab on FGFR2 phosphorylation and tumor cell proliferation was assessed in the SNU-16 human gastric cancer cell line.”
BackgroundAngiogenesis in Lung Cancer: Understanding the Roles of Growth Factors
Ngaha, T. Y. S., Zhilenkova, A., Essogmo, F. E., Uchendu, I., Abah, M., Fossa, L., Sangadzhieva, Z. D., Sanikovich, V., Rusanov, A. S., Pirogova, Y. N., et al. (2023) · Cancers · doi:10.3390/cancers15184648 · Cited by 55 · see citing works
“- Platelet Derived Growth Factor (PDGF) α / β : They belong to the PDGF receptor tyrosine kinase family and have been linked to lung cancer angiogenesis.”
BackgroundInfluentialCellular crosstalk in fibrosis: Insights into macrophage and fibroblast dynamics
Froom, Z. S. C. S., Callaghan, N. I., & Huyer, L. D. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110203 · Cited by 58 · see citing works
Mechanisms of Muscle Cells Alterations and Regeneration Decline During Aging.
Chinvattanachot, G., Rivas, D., & Duque, G. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102589 · Cited by 54 · see citing works
“…extensively studied trophic factors that enable myogenic proliferation and differentiation through various intracellular signaling pathways, including p38 α / β MAPK, ERK/MAPK and STAT (Charg ´ e and Rudnicki, 2004; Kim and Bar-Sagi, 2004; Ornitz and Itoh, 2015; Mossahebi-Mohammadi et al., 2020).”
Interplay Between Extracellular Matrix Remodeling and Angiogenesis in Tumor Ecosystem.
Siddhartha, R., & Garg, M. (2023) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-22-0595 · Cited by 54 · see citing works
Enriched Environment Promotes Adult Hippocampal Neurogenesis through FGFRs
Grońska-Pęski, M., Gonçalves, J., & Hébert, J. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.2286-20.2021 · Cited by 54 · see citing works
“We initially examined ERK phosphorylation because it is a canonical mediator of extracellular receptor kinases, including FGFRs, in progenitor cells (Hébert, 2011; Ornitz and Itoh, 2015; Brewer et al., 2016; MossahebiMohammadi et al., 2020).”
BackgroundSchumacher, J. D., Kong, B., Pan, Y., Zhan, L., Sun, R., Aa, J., Rizzolo, D., Richardson, J. R., Chen, A., Goedken, M., et al. (2017) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2017.06.023 · Cited by 53 · see citing works
Fibroblast growth factor receptor signalling dysregulation and targeting in breast cancer
Francavilla, C., & O'Brien, C. (2022) · Open Biology · doi:10.1098/rsob.210373 · Cited by 53 · see citing works
“The endocrine FGF15/19 subfamily has higher affinity for the mesenchymal isoforms of FGFR1–3 [4] (figure 2b).”
BackgroundInfluentialThe regulation of FGF23 under physiological and pathophysiological conditions
Rausch, S., & Föller, M. (2022) · Pflügers Archiv: European Journal of Physiology · doi:10.1007/s00424-022-02668-w · Cited by 53 · see citing works
The neural crest cell hypothesis: no unified explanation for domestication
Johnsson, M., Henriksen, R., & Wright, D. (2021) · Genetics · doi:10.1093/genetics/iyab097 · Cited by 51 · see citing works
Edman, N. I., Phal, A., Redler, R. L., Schlichthaerle, T., Srivatsan, S. R., Ehnes, D. D., Etemadi, A., An, S. J., Favor, A., Li, Z., et al. (2024) · Cell · doi:10.1016/j.cell.2024.05.025 · Cited by 61 · see citing works
“24,37,38 We evaluated the signaling activity of our designs by screening them in serum-starved Chinese hamster ovary (CHO) cells stably expressing hFGFR1c (CHO-R1c) at 10 nM each for 15 min at 37 " C. Downstream activation through phosphorylation of ERK1/2 and FGFR1 (Y653/654) was analyzed by…”
MethodNegative Regulation of FGFR (Fibroblast Growth Factor Receptor) Signaling
Szybowska, P., Kostas, M., Wesche, J., Haugsten, E. M., & Więdłocha, A. (2021) · Cells · doi:10.3390/cells10061342 · Cited by 61 · see citing works
“There are several excellent reviews on FGFR signaling and therefore, this will not be discussed in further detail here [9,16,20].”
BackgroundInfluentialDecoding Tumor Angiogenesis for Therapeutic Advancements: Mechanistic Insights
Kaur, G., & Roy, B. (2024) · Biomedicines · doi:10.3390/biomedicines12040827 · Cited by 53 · see citing works
“Further, the interaction of FGFs with their high-affinity receptors activates intrinsic tyrosine kinase, which is involved in inducing early gene transcription and cell proliferation [61].”
BackgroundThe role of fibroblast growth factor 8 in cartilage development and disease
Chen, H.-R., Cui, Y., Zhang, D., Xie, J., & Zhou, X.-D. (2022) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17174 · Cited by 50 · see citing works
The Roles and Pharmacological Effects of FGF21 in Preventing Aging-Associated Metabolic Diseases
Yan, J., Nie, Y., Cao, J., Luo, M., Yan, M., Chen, Z., & He, B. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.655575 · Cited by 53 · see citing works
“Four family members (FGF11, FGF12, FGF13, and FGF14) cannot bind to FGFR are more correctly referred to as FGF homologous factors (38).”
BackgroundAdvances in targeted therapy of cholangiocarcinoma
Li, Y., Yu, J., Zhang, Y., Peng, C., Song, Y., & Liu, S.-L. (2024) · Annals medicus · doi:10.1080/07853890.2024.2310196 · Cited by 49 · see citing works
“FGFR is expressed in a variety of cell types and consists of four intracellular trans-membrane receptors with tyrosine kinase domains (FGFR1-4) encoded by FLG, BEK, CEK-2, and FREK genes [30].”
BackgroundArdizzone, A., Scuderi, S., Giuffrida, D., Colarossi, C., Puglisi, C., Campolo, M., Cuzzocrea, S., Esposito, E., & Paterniti, I. (2020) · Cancers · doi:10.3390/cancers12123825 · Cited by 49
“Once activated, the receptor can in turn phosphorylate and activate various signal transducer molecules, both directly and indirectly such as AKT and the anti-apoptotic pathway dependent on this, as well as the Ras-R f-MEK-ERK pathway [49,50].”
BackgroundFougerat, A., Bruse, J., Polizzi, A., Montagner, A., Guillou, H., & Wahli, W. (2024) · Progress in Lipid Research · doi:10.1016/j.plipres.2024.101303 · Cited by 54 · see citing works
“FGF21 signals by binding to a tyrosine kinase FGF receptor (FGFR) [172,173].”
Lassen, T. R., Just, J., Hjortbak, M. V., Jespersen, N. R., Stenz, K. T., Gu, T., Yan, Y., Su, J., Hansen, J., Bæk, R., et al. (2021) · Basic Research in Cardiology · doi:10.1007/s00395-021-00856-w · Cited by 52 · see citing works
Optogenetic actuator – ERK biosensor circuits identify MAPK network nodes that shape ERK dynamics
Dessauges, C., Mikelson, J., Dobrzyński, M., Jacques, M., Frismantiene, A., Gagliardi, P. A., Khammash, M., & Pertz, O. (2022) · Molecular Systems Biology · doi:10.15252/msb.202110670 · Cited by 48 · see citing works
“As phospholipase C mediates Ca 2 + signaling in response to FGFR activation (Ornitz & Itoh, 2015), this further validates the role of Ca 2 + signaling in formation of the dip (Appendix Fig S1D –”
Seitz, T., Freese, K., Dietrich, P., Thasler, W. E., Bosserhoff, A., & Hellerbrand, C. (2020) · Scientific Reports · doi:10.1038/s41598-020-61510-4 · Cited by 47 · see citing works
FGF-based drug discovery: advances and challenges
Chen, G., Chen, L., Li, X., & Mohammadi, M. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-01125-w · Cited by 51 · see citing works
Current progress in growth factors and extracellular vesicles in tendon healing
Wang, Y., & Li, J. (2023) · International Wound Journal · doi:10.1111/iwj.14261 · Cited by 49 · see citing works
“57 In a rabbit model of synovial tendon injury, bFGF mRNA was found to be upregulated in tendon cells and tendon sheath fibroblasts.”
BackgroundA review on biomaterials-based scaffold: An emerging tool for bone tissue engineering
Francis, A. P., Augustus, A. R., Chandramohan, S., Bhat, S., Priya, V., & Rajagopalan, R. (2022) · Materials Today Communications · doi:10.1016/j.mtcomm.2022.105124 · Cited by 47 · see citing works
Manzari‐Tavakoli, A., Babajani, A., Farjoo, M. H., Hajinasrollah, M., Bahrami, S., & Niknejad, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.827275 · Cited by 62 · see citing works
“The phylogenetic analysis suggests that FGF protein family members can be arranged into seven subfamilies containing FGF1 (FGF1, 2), FGF4 (FGF4, 5, 6), FGF7 (FGF3, 7, 10, 22), FGF8 (FGF7, 17, 18), FGF9 (FGF9, 16, 20), and FGF15/19 (FGF15/19, 21, 23) subfamily (Ornitz and Itoh, 2015).”
BackgroundNovel Therapeutic Targets in Liver Fibrosis
Zhang, J., Liu, Q., He, J., & Li, Y. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.766855 · Cited by 46 · see citing works
Miricescu, D., Bădoiu, S. C., Stănescu-Spînu, I.-I., Totan, A., Ștefani, C., & Greabu, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179512 · Cited by 62 · see citing works
“ROS and RNS can modulate all three members of the MAPK family signaling pathway [169] and PI3K/AKT [170].”
BackgroundInfluentialRoles of Fibroblast Growth Factors and Their Therapeutic Potential in Treatment of Ischemic Stroke
Dordoe, C., Chen, K., Huang, W., Chen, J., HU, J. L., Wang, X. B., & Lin, L. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.671131 · Cited by 52 · see citing works
The physiology of MASLD: molecular pathways between liver and adipose tissues
Lee, W., Kipp, Z. A., Bates, E. A., Pauss, S. N., Martinez, G. J., & Hinds, T. D. (2025) · Clinical Science · doi:10.1042/cs20257571 · Cited by 47 · see citing works
“In the liver, FGF21 binds to FGFR1c and forms a complex with β-Klotho (KLB), which increases proliferator-activated receptor gamma coactivator 1α (PGC-1α) expression [68,69].”
- Authors
- Ornitz, D. M., & Itoh, N.
- Affiliations
- Washington University in St. Louis (US)
- Kyoto University (JP)
- Corresponding author
- Ornitz, David M.
- ORCID
- Ornitz, David M.
- Venue
- WIREs Developmental Biology
- Publisher
- Wiley
- Published
- 2015-03-13
- Volume
- 4
- Issue
- 3
- Pages
- 215-266
- ISSN
- 1759-7684 (ISSN-L)
- 1759-7692
- PMC
- PMC4393358
- OpenAlex
- W2054195724
- Cited by
- 2,050
- References
- 769
- Citations by year
- 2026: 121 · 2025: 185 · 2024: 206 · 2023: 206 · 2022: 218 · 2021: 273 · 2020: 220 · 2019: 215 · 2018: 172 · 2017: 133 · 2016: 72 · 2015: 25 · 2014: 1
- FWCI
- 12.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Wiley Interdisciplinary Reviews Developmental Biology (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (HL105732, HL111190, HD049808)
- Action on Hearing Loss (G59)
- march of dimes (FY14-329)
- Ministry of Education, Science, Sports, and Culture of Japan (25460065)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fibroblast Growth Factor Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Keywords
- FGF signaling, fibroblast growth factor receptor, FGF ligands, receptor tyrosine kinase, RAS/MAPK pathway, PI3K/Akt signaling, PLCγ signaling, STAT signaling, voltage-gated sodium channels, embryonic development, organogenesis, tissue regeneration, cancer, metabolic disorders
- MeSH terms
- Animals, Cell Differentiation, Cell Movement, Energy Metabolism, Fibroblast Growth Factors, Homeostasis, Humans, Models, Biological, Signal Transduction, Receptors, Fibroblast Growth Factor, Organogenesis, Embryonic Development, Cell Proliferation, Voltage-Gated Sodium Channels
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