ArticleThe Journal of biological chemistry2009
Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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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
61 citing papers in PubMed, 102 citations in OpenAlex.
- RACK1 and RPS6 as independent prognostic biomarkers in oral squamous cell carcinoma: a five-year survival analysis.Frontiers in oral health · 2026Article
- A Duality of Function: An Integrative Model of RACK1 as a Switch Between Translational and Signaling Hubs.International journal of molecular sciences · 2025Review
- Nematode serine protease inhibitor SPI-I8 negatively regulates host NF-κB signalling by hijacking MKRN1-mediated polyubiquitination of RACK1.Communications biology · 2025Article
- The c-Abl-RACK1-FAK signaling axis promotes renal fibrosis in mice through regulating fibroblast-myofibroblast transition.Cell communication and signaling : CCS · 2024Article
- RACK1 promotesiScience · 2023Article
- CAP2 promotes gastric cancer metastasis by mediating the interaction between tumor cells and tumor-associated macrophages.The Journal of clinical investigation · 2023Article
- SEMA6C: a novel adhesion-independent FAK and YAP activator, required for cancer cell viability and growth.Cellular and molecular life sciences : CMLS · 2023Article
- Serine-Threonine Kinase Receptor Associate Protein (STRAP) confers an aggressive phenotype in neuroblastoma via regulation of Focal Adhesion Kinase (FAK).Journal of pediatric surgery · 2022Article
- Photoaffinity Probe Reveals the Potential Target of Harringtonolide for Cancer Cell Migration Inhibition.ACS medicinal chemistry letters · 2022Article
- Eukaryotic initiation factor 6 regulates mechanical responses in endothelial cells.The Journal of cell biology · 2022Article
- Endocrine-Disrupting Chemicals' (EDCs) Effects on Tumour Microenvironment and Cancer Progression: Emerging Contribution of RACK1.International journal of molecular sciences · 2020Review
- Controlled Signaling-Insulin-Like Growth Factor Receptor Endocytosis and Presence at Intracellular Compartments.Frontiers in endocrinology · 2020Review
- The regulation of sequence specific NF-κB DNA binding and transcription by IKKβ phosphorylation of NF-κB p50 at serine 80.Nucleic acids research · 2019Article
- RACK1 Specifically Regulates Translation through Its Binding to Ribosomes.Molecular and cellular biology · 2018Article
- RAB40C regulates RACK1 stability via the ubiquitin-proteasome system.Future science OA · 2018Article
- CPNE3 promotes migration and invasion in non-small cell lung cancer by interacting with RACK1 via FAK signaling activation.Journal of Cancer · 2018Article
- RACK1 is necessary for the formation of point contacts and regulates axon growth.Developmental neurobiology · 2017Article
- The RNA-binding protein SERBP1 interacts selectively with the signaling protein RACK1.Cellular signalling · 2017Article
- Asc1p/RACK1 Connects Ribosomes to Eukaryotic Phosphosignaling.Molecular and cellular biology · 2017Article
- The important role of the receptor for activated C kinase 1 (RACK1) in nasopharyngeal carcinoma progression.Journal of translational medicine · 2016Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Focal Adhesion Kinase (FAK) activity is controlled by growth factors and adhesion signals in tumor cells. The scaffolding protein RACK1 (receptor for activated C kinases) integrates insulin-like growth factor I (IGF-I) and integrin signaling, but whether RACK1 is required for FAK function is unknown. Here we show that association of FAK with RACK1 is required for both FAK phosphorylation and dephosphorylation in response to IGF-I. Suppression of RACK1 by small interfering RNA ablates FAK phosphorylation and reduces cell adhesion, cell spreading, and clonogenic growth. Peptide array and mutagenesis studies localize the FAK binding interface to blades I-III of the RACK1 beta-propeller and specifically identify a set of basic and hydrophobic amino acids (Arg-47, Tyr-52, Arg-57, Arg-60, Phe-65, Lys-127, and Lys-130) as key determinants for association with FAK. Mutation of tyrosine 52 alone is sufficient to disrupt interaction of RACK1 with FAK in cells where endogenous RACK1 is suppressed by small interfering RNA. Cells expressing a Y52F mutant RACK1 are impaired in adhesion, growth, and foci formation. Comparative analyses of homology models and crystal structures for RACK1 orthologues suggest a role for Tyr-52 as a site for phosphorylation that induces conformational change in RACK1, switching the protein into a FAK binding state. Tyrosine 52 is further shown to be phosphorylated by c-Abl kinase, and the c-Abl inhibitor STI571 disrupts FAK interaction with RACK1. We conclude that FAK association with RACK1 is regulated by phosphorylation of Tyr-52. Our data reveal a novel mechanism whereby IGF-I and c-Abl control RACK1 association with FAK to facilitate adhesion signaling.
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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.