ArticleScientific reports2015
Focal adhesion kinase-dependent focal adhesion recruitment of SH2 domains directs SRC into focal adhesions to regulate cell adhesion and migration.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 66 citations in OpenAlex.
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- Unraveling the carcinogenic mechanisms of benzo[a]pyrene in prostate cancer: a multi-omics approach.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Integrin and Its Associated Proteins as a Mediator for Mechano-Signal Transduction.Biomolecules · 2025Review
- Understanding the Role of Connexins in Hepatocellular Carcinoma: Molecular and Prognostic Implications.Cancers · 2024Review
- Fabrication of 3D matrix microenvironment by two-photon lithography for mechanobiology study.Mechanobiology in medicine · 2023Review
- Focal adhesion kinase activation is involved in contractile stimulation-induced detrusor muscle contraction in mice.European journal of pharmacology · 2023Article
- Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase.eLife · 2023Article
- A luciferase fragment complementation assay to detect focal adhesion kinase (FAK) signaling events.Heliyon · 2023Article
- Proteomic Markers for Mechanobiological Properties of Metastatic Cancer Cells.International journal of molecular sciences · 2023Review
- Thy-1 (CD90)-regulated cell adhesion and migration of mesenchymal cells: insights into adhesomes, mechanical forces, and signaling pathways.Frontiers in cell and developmental biology · 2023Review
- Dissecting protein tyrosine phosphatase signaling by engineered chemogenetic control of its activity.The Journal of cell biology · 2022Article
- FAK in Cancer: From Mechanisms to Therapeutic Strategies.International journal of molecular sciences · 2022Review
- Functional and clinical characteristics of focal adhesion kinases in cancer progression.Frontiers in cell and developmental biology · 2022Review
- Umbelliferone and scopoletin target tyrosine kinases on fibroblast-like synoviocytes to block NF-κB signaling to combat rheumatoid arthritis.Frontiers in pharmacology · 2022Article
- CK2β Is a Gatekeeper of Focal Adhesions Regulating Cell Spreading.Frontiers in molecular biosciences · 2022Article
- Migfilin: Cell Adhesion Effect and Comorbidities.OncoTargets and therapy · 2022Review
- Current hydrogel advances in physicochemical and biological response-driven biomedical application diversity.Signal transduction and targeted therapy · 2021Review
- Article
- The Relevance of the SH2 Domain for c-Src Functionality in Triple-Negative Breast Cancer Cells.Cancers · 2021Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Directed cell migration requires dynamical control of the protein complex within focal adhesions (FAs) and this control is regulated by signaling events involving tyrosine phosphorylation. We screened the SH2 domains present in tyrosine-specific kinases and phosphatases found within FAs, including SRC, SHP1 and SHP2, and examined whether these enzymes transiently target FAs via their SH2 domains. We found that the SRC_SH2 domain and the SHP2_N-SH2 domain are associated with FAs, but only the SRC_SH2 domain is able to be regulated by focal adhesion kinase (FAK). The FAK-dependent association of the SRC_SH2 domain is necessary and sufficient for SRC FA targeting. When the targeting of SRC into FAs is inhibited, there is significant suppression of SRC-mediated phosphorylation of paxillin and FAK; this results in an inhibition of FA formation and maturation and a reduction in cell migration. This study reveals an association between FAs and the SRC_SH2 domain as well as between FAs and the SHP2_N-SH2 domains. This supports the hypothesis that the FAK-regulated SRC_SH2 domain plays an important role in directing SRC into FAs and that this SRC-mediated FA signaling drives cell migration.
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