ArticleThe Journal of biological chemistry2014
Kindlin-2 tyrosine phosphorylation and interaction with Src serve as a regulatable switch in the integrin outside-in signaling circuit.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Beyond Integrin Activation: Kindlin-3 as an Organiser of Immune Receptor Signalling.International journal of molecular sciences · 2026Review
- Structural basis of kindlin-3 in leukocyte adhesion deficiency III.Journal of thrombosis and haemostasis : JTH · 2026Article
- FAK-dependent activation of src family kinase member BLK contributed to endometrial fibrosis via endoplasmic reticulum stress.Cell & bioscience · 2025Article
- The NADC30-like PRRSV activates the integrin αV subunit to facilitate its entry into Marc-145 cells.PloS one · 2025Article
- Kindlin-2 promotes Src-mediated tyrosine phosphorylation of androgen receptor and contributes to breast cancer progression.Cell death & disease · 2022Article
- Kindlin for the Fire: Targeting Proline Synthesis to Extinguish Matrix Production in Pulmonary Fibrosis.American journal of respiratory cell and molecular biology · 2021Article
- Review
- Kindlin-2 mediates mechanotransduction in bone by regulating expression of Sclerostin in osteocytes.Communications biology · 2021Article
- Role of Kindlin-2 in cancer progression and metastasis.Annals of translational medicine · 2020Review
- The new genetic landscape of Alzheimer's disease: from amyloid cascade to genetically driven synaptic failure hypothesis?Acta neuropathologica · 2019Review
- Site-specific phosphorylation regulates the functions of kindlin-3 in a variety of cells.Life science alliance · 2019Article
- Kindlin-1 Regulates Epidermal Growth Factor Receptor Signaling.The Journal of investigative dermatology · 2019Article
- Src-mediated phosphorylation converts FHL1 from tumor suppressor to tumor promoter.The Journal of cell biology · 2018Article
- Kindlin-2 regulates mesenchymal stem cell differentiation through control of YAP1/TAZ.The Journal of cell biology · 2018Article
- Kindlin-2 Association with Rho GDP-Dissociation InhibitorJournal of the American Society of Nephrology : JASN · 2017Article
- Kindlin supports platelet integrin αIIbβ3 activation by interacting with paxillin.Journal of cell science · 2017Article
- Optogenetic interrogation of integrin αVβ3 function in endothelial cells.Journal of cell science · 2017Article
- Genome-wide, high-content siRNA screening identifies the Alzheimer's genetic risk factor FERMT2 as a major modulator of APP metabolism.Acta neuropathologica · 2017Article
- Mapping Heart Development in Flies: Src42A Acts Non-Autonomously to Promote Heart Tube Formation in Drosophila.Veterinary sciences · 2017Article
- Focal adhesion kinase signaling in unexpected places.Current opinion in cell biology · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Integrin-mediated cell-extracellular matrix (ECM) adhesion is critical for control of intracellular signaling; however, the mechanisms underlying this "outside-in" signaling are incompletely understood. Here we show that depletion of kindlin-2 impairs integrin outside-in signaling. Kindlin-2 is tyrosine-phosphorylated upon cell-ECM adhesion. Furthermore, kindlin-2 binds Src in a cell-ECM adhesion-regulatable fashion. At the molecular level, the kindlin-2·Src interaction is mediated by the kindlin-2 F0 and the Src SH2 and SH3 domains. Src activation increases kindlin-2 tyrosine phosphorylation and the kindlin-2·Src interaction. Conversely, inhibition of Src reduces kindlin-2 tyrosine phosphorylation and diminishes the kindlin-2·Src interaction. Finally, disruption of the kindlin-2·Src interaction, unlike depletion of kindlin-2, impairs neither cell-ECM adhesion nor cell-ECM adhesion-induced focal adhesion kinase Tyr-397 phosphorylation. However, it markedly inhibits cell-ECM adhesion-induced paxillin tyrosine phosphorylation, cell migration, and proliferation. These results suggest that kindlin-2 tyrosine phosphorylation and interaction with Src serve as a regulatable switch downstream of focal adhesion kinase in the integrin outside-in signaling circuit, relaying signals from cell-ECM adhesion to paxillin that control cell migration and proliferation.
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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.