ArticleOncogene1999
Src is required for cell migration and shape changes induced by fibroblast growth factor 1.
Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 85 citations in OpenAlex.
- Context-dependent peptide recognition shapes tyrosine kinase substrate specificity beyond consensus motifs.bioRxiv : the preprint server for biology · 2026Article
- Large-scale control over collective cell migration using light-activated epidermal growth factor receptors.Cell systems · 2025Article
- Large-scale control over collective cell migration using light-controlled epidermal growth factor receptors.bioRxiv : the preprint server for biology · 2024Article
- Article
- 27-Hydroxycholesterol induces expression of zonula occludens-1 in monocytic cells via multiple kinases pathways.Scientific reports · 2022Article
- Regulation of Transplanted Cell Homing by FGF1 and PDGFB after Doxorubicin Myocardial Injury.Cells · 2021Article
- The phosphatase Shp1 interacts with and dephosphorylates cortactin to inhibit invadopodia function.Cell communication and signaling : CCS · 2021Article
- Effects of the Tumor Environment on Ion Channels: Implication for Breast Cancer Progression.Reviews of physiology, biochemistry and pharmacology · 2021Review
- FAK-Dependent Cell Motility and Cell Elongation.Cells · 2020Review
- A single tyrosine phosphorylation site in cortactin is important for filopodia formation in neuronal growth cones.Molecular biology of the cell · 2019Article
- The inositol phosphatase SHIP2 enables sustained ERK activation downstream of FGF receptors by recruiting Src kinases.Science signaling · 2018Article
- ZDHHC3 Tyrosine Phosphorylation Regulates Neural Cell Adhesion Molecule Palmitoylation.Molecular and cellular biology · 2016Article
- Genetic insights into the mechanisms of Fgf signaling.Genes & development · 2016Review
- Src tyrosyl phosphorylates cortactin in response to prolactin.Biochemical and biophysical research communications · 2015Article
- Increased FGF1-FGFRc expression in idiopathic pulmonary fibrosis.Respiratory research · 2015Article
- Fibroblast growth factor signaling in the vasculature.Current atherosclerosis reports · 2015Review
- Eph- and ephrin-dependent mechanisms in tumor and stem cell dynamics.Cellular and molecular life sciences : CMLS · 2014Review
- Synergistic effect of EMS1-shRNA and sorafenib on proliferation, migration, invasion and endocytosis of SMMC-7721.Journal of molecular histology · 2014Article
- Impact of fibroblast growth factor-binding protein-1 expression on angiogenesis and wound healing.The American journal of pathology · 2011Article
- Cortactin branches out: roles in regulating protrusive actin dynamics.Cell motility and the cytoskeleton · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Fibroblast growth factor 1 (FGF-1) is a potent chemotactic factor and induces tyrosine phosphorylation of a cortical actin-associated protein (cortactin). The tyrosine phosphorylation of cortactin induced by FGF-1 requires the tyrosine residues 421, 482 and 466, which are targeted by the protein tyrosine kinase Src in vitro. Furthermore, FGF-1 is unable to induce tyrosine phosphorylation of cortactin within the cells derived from Src knockout mice (Src-/-), indicating that Src is required for the tyrosine phosphorylation of cortactin induced by FGF-1. Although Src-/- cells are able to undergo rapid proliferation, they are impaired to respond to FGF-1 for the shape change and cell migration. Morphological analysis further reveals that FGF-1 fails to induce the formation of polarized lamellipodia and the translocation of cortactin into the leading edge of Src-/- cells. Consistent with the mitogenic response to FGF-1, the lack of Src does not affect the tyrosine phosphorylation of Snt (or Frs2), a FGF-1 early signaling protein that links to Ras. Therefore, our data support the notion that Src and cortactin participate in a FGF signal pathway for cell migration and shape change rather than mitogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.