ArticleThe Journal of biological chemistry2009
Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis.
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 33 papers.
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Who cites it
33 citing papers in PubMed, 66 citations in OpenAlex.
- Focal adhesion kinase: from biological functions to therapeutic strategies.Experimental hematology & oncology · 2023Review
- Long range inter-chromosomal interaction of Oct4 distal enhancer loci regulates ESCs pluripotency.Cell death discovery · 2023Article
- Enhancing the Bioactivity of Bicyclic Peptides Targeted to Grb7-SH2 by Restoring Cell Permeability.Biomedicines · 2022Article
- circCDYL2 promotes trastuzumab resistance via sustaining HER2 downstream signaling in breast cancer.Molecular cancer · 2022Article
- Up-regulated GRB7 protein in gastric cancer cells correlates with clinical properties and increases proliferation and stem cell properties.Frontiers in oncology · 2022Article
- Aquaporin-1 facilitates proliferation and invasion of gastric cancer cells via GRB7-mediated ERK and Ras activation.Animal cells and systems · 2020Article
- Article
- Direct Interaction between Calmodulin and the Grb7 RA-PH Domain.International journal of molecular sciences · 2020Article
- Phosphotyrosine isosteres: past, present and future.Organic & biomolecular chemistry · 2020Review
- Identification of new binding proteins of focal adhesion kinase using immunoprecipitation and mass spectrometry.Scientific reports · 2019Article
- Review
- Global expression profiling and pathway analysis of mouse mammary tumor reveals strain and stage specific dysregulated pathways in breast cancer progression.Cell cycle (Georgetown, Tex.) · 2018Article
- Article
- Novel roles of Src in cancer cell epithelial-to-mesenchymal transition, vascular permeability, microinvasion and metastasis.Life sciences · 2016Review
- Grb7 and Hax1 may colocalize partially to mitochondria in EGF-treated SKBR3 cells and their interaction can affect Caspase3 cleavage of Hax1.Journal of molecular recognition : JMR · 2016Article
- Unexpected involvement of staple leads to redesign of selective bicyclic peptide inhibitor of Grb7.Scientific reports · 2016Article
- An EGFR/Src-dependent β4 integrin/FAK complex contributes to malignancy of breast cancer.Scientific reports · 2015Article
- Focal adhesion kinase and p53 synergistically decrease neuroblastoma cell survival.The Journal of surgical research · 2015Article
- Emerging roles of focal adhesion kinase in cancer.BioMed research international · 2015Review
- Gene Expression-Genotype Analysis Implicates GSDMA, GSDMB, and LRRC3C as Contributors to Inflammatory Bowel Disease Susceptibility.BioMed research international · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously reported that growth factor receptor-bound protein-7 (Grb7), an Src-homology 2 (SH2)-containing adaptor protein, enables interaction with focal adhesion kinase (FAK) to regulate cell migration in response to integrin activation. To further elucidate the signaling events mediated by FAK*Grb7 complexes in promoting cell migration and other cellular functions, we firstly examined the phosphorylated tyrosine site(s) of Grb7 by FAK using an in vivo mutagenesis. We found that FAK was capable of phosphorylating at least 2 of 12 tyrosine residues within Grb7, Tyr-188 and Tyr-338. Moreover, mutations converting the identified Tyr to Phe inhibited integrin-dependent cell migration as well as impaired cell proliferation but not survival compared with the wild-type control. Interestingly, the above inhibitory effects caused by the tyrosine phosphorylation-deficient mutants are probably attributed to their down-regulation of phospho-Tyr-397 of FAK, thereby implying a mechanism by competing with wild-type Grb7 for binding to FAK. Consequently, these tyrosine phosphorylation-deficient mutants evidently altered the phospho-Tyr-118 of paxillin and phosphorylation of ERK1/2 but less on phospho-Ser-473 of AKT, implying their involvement in the FAK*Grb7-mediated cellular functions. Additionally, we also illustrated that the formation of FAK*Grb7 complexes and Grb7 phosphorylation by FAK in an integrin-dependent manner were essential for cell migration, proliferation and anchorage-independent growth in A431 epidermal carcinoma cells, indicating the importance of FAK*Grb7 complexes in tumorigenesis. Our data provide a better understanding on the signal transduction event for FAK*Grb7-mediated cellular functions as well as to shed light on a potential therapeutic in cancers.
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