ArticleThe EMBO journal2020
Structural basis of Focal Adhesion Kinase activation on lipid membranes.
Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 82 citations in OpenAlex.
- Sweetening the bonds: how O-GlcNAcylation modulates cell adhesion.Acta pharmacologica Sinica · 2026Review
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- FAK modulates immune response and fibroblast activation in biomaterial-induced fibrosis.Biomaterials · 2026Article
- RPRD1A drives lenvatinib resistance in hepatocellular carcinoma via the ITGA5-FAK signaling axis.Molecular biomedicine · 2026Article
- Chlorogenic Acid Alleviates Ferroptosis Collectively Induced by Lipopolysaccharide and Interleukin-6 in Bovine Mammary Epithelial Cells.Journal of agricultural and food chemistry · 2025Article
- Safety, pharmacokinetic, pharmacodynamic, and efficacy properties of orally administered APG-2449 in patients with advancedEClinicalMedicine · 2025Article
- Mechanochemical waves in focal adhesions during cell migration.Science advances · 2025Article
- Activation of Focal Adhesion Pathway byAnimals : an open access journal from MDPI · 2025Article
- Article
- Targeting the hydrophobic pockets of FAK/PYK2 FAT domain: a highly effective inhibitory strategy suppressing tumor growth and eliminating metastasis.Cell communication and signaling : CCS · 2025Article
- Phospho-regulated tethering of focal adhesion kinase to vinculin links force transduction to focal adhesion signaling.Cell communication and signaling : CCS · 2025Article
- Targeting FAK to Potentiate Immune Checkpoint Therapy in Solid Tumors.Journal of cancer immunology · 2025Article
- Focal adhesion kinase signaling - tumor vulnerabilities and clinical opportunities.Journal of cell science · 2024Review
- ZDHHC5-mediated S-palmitoylation of FAK promotes its membrane localization and epithelial-mesenchymal transition in glioma.Cell communication and signaling : CCS · 2024Article
- Roles and inhibitors of FAK in cancer: current advances and future directions.Frontiers in pharmacology · 2024Review
- Polarized focal adhesion kinase activity within a focal adhesion during cell migration.Nature chemical biology · 2023Article
- The interplay between cell wall integrity and cell cycle progression in plants.Plant molecular biology · 2023Review
- A selective CB2R agonist (JWH133) protects against pulmonary fibrosis through inhibiting FAK/ERK/S100A4 signaling pathways.BMC pulmonary medicine · 2023Article
- Preadipocytes in human granulation tissue: role in wound healing and response to macrophage polarization.Inflammation and regeneration · 2023Article
- Targeting FAK/PYK2 with SJP1602 for Anti-Tumor Activity in Triple-Negative Breast Cancer.Current issues in molecular biology · 2023Article
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Authors and funding
17 authors at 5 institutions in 4 countries.
Funding
Abstract
Focal adhesion kinase (FAK) is a key component of the membrane proximal signaling layer in focal adhesion complexes, regulating important cellular processes, including cell migration, proliferation, and survival. In the cytosol, FAK adopts an autoinhibited state but is activated upon recruitment into focal adhesions, yet how this occurs or what induces structural changes is unknown. Here, we employ cryo-electron microscopy to reveal how FAK associates with lipid membranes and how membrane interactions unlock FAK autoinhibition to promote activation. Intriguingly, initial binding of FAK to the membrane causes steric clashes that release the kinase domain from autoinhibition, allowing it to undergo a large conformational change and interact itself with the membrane in an orientation that places the active site toward the membrane. In this conformation, the autophosphorylation site is exposed and multiple interfaces align to promote FAK oligomerization on the membrane. We show that interfaces responsible for initial dimerization and membrane attachment are essential for FAK autophosphorylation and resulting cellular activity including cancer cell invasion, while stable FAK oligomerization appears to be needed for optimal cancer cell proliferation in an anchorage-independent manner. Together, our data provide structural details of a key membrane bound state of FAK that is primed for efficient autophosphorylation and activation, hence revealing the critical event in integrin mediated FAK activation and signaling at focal adhesions.
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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.