ArticleMolecular and cellular biology2000
The cytoplasmic tyrosines of integrin subunit beta1 are involved in focal adhesion kinase activation.
Article in Molecular and cellular biology, 2000. 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, 94 citations in OpenAlex.
- Dynamic regulation of integrin β1 phosphorylation supports invasion of breast cancer cells.Nature cell biology · 2025Article
- KLF14 targets ITGB1 to inhibit the progression of cervical cancer via the PI3K/AKT signalling pathway.Discover oncology · 2022Article
- The Sall2 transcription factor promotes cell migration regulating focal adhesion turnover and integrin β1 expression.Frontiers in cell and developmental biology · 2022Article
- BMPR2 acts as a gatekeeper to protect endothelial cells from increased TGFβ responses and altered cell mechanics.PLoS biology · 2019Article
- NDRG4 promoter hypermethylation is a mechanistic biomarker associated with metastatic progression in breast cancer patients.NPJ breast cancer · 2019Article
- Novel sulphamoylated 2-methoxy estradiol derivatives inhibit breast cancer migration by disrupting microtubule turnover and organization.Cancer cell international · 2019Article
- Phagocytic Receptors Activate Syk and Src Signaling during Borrelia burgdorferi Phagocytosis.Infection and immunity · 2017Article
- Integrins in the Spotlight of Cancer.International journal of molecular sciences · 2016Review
- Integrin endosomal signalling suppresses anoikis.Nature cell biology · 2015Article
- Contributions of the integrin β1 tail to cell adhesive forces.Experimental cell research · 2015Article
- MicroRNA- 130b suppresses migration and invasion of colorectal cancer cells through downregulation of integrin β1 [corrected].PloS one · 2014Article
- Focal adhesion complex proteins in epidermis and squamous cell carcinoma.Cell cycle (Georgetown, Tex.) · 2013Review
- The signaling pathway of Campylobacter jejuni-induced Cdc42 activation: Role of fibronectin, integrin beta1, tyrosine kinases and guanine exchange factor Vav2.Cell communication and signaling : CCS · 2011Article
- β1-integrins signaling and mammary tumor progression in transgenic mouse models: implications for human breast cancer.Breast cancer research : BCR · 2011Review
- Significance of talin in cancer progression and metastasis.International review of cell and molecular biology · 2011Review
- The glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry.Journal of virology · 2010Article
- Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation.The Journal of biological chemistry · 2009Article
- Integrin-linked kinase is required for radial sorting of axons and Schwann cell remyelination in the peripheral nervous system.The Journal of cell biology · 2009Article
- Extended interaction of beta1 integrin subunit-deficient cells (GD25) with surfaces modified with fibronectin-derived peptides: Culture optimization, adhesion and cytokine panel studies.Acta biomaterialia · 2008Article
- Expression of integrin-linked kinase is increased in differentiated cells.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2008Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
We have previously shown that mutation of the two tyrosines in the cytoplasmic domain of integrin subunit beta1 (Y783 and Y795) to phenylalanines markedly reduces the capability of beta1A integrins to mediate directed cell migration. In this study, beta1-dependent cell spreading was found to be delayed in GD25 cells expressing beta1A(Y783/795F) compared to that in wild-type GD25-beta1A. Focal adhesion kinase (FAK) tyrosine phosphorylation and activation were severely impaired in response to beta1-dependent adhesion in GD25-beta1A(Y783/795F) cells compared to that in wild-type GD25-beta1A or mutants in which only a single tyrosine was altered (beta1A(Y783F) or beta1A(Y795F)). Phosphorylation site-specific antibodies selective for FAK phosphotyrosine 397 indicated that the defect in FAK phosphorylation via beta1A(Y783/795F) lies at the level of the initial autophosphorylation step. Indeed, beta1A-dependent tyrosine phosphorylation of tensin and paxillin was lost in the beta1A(Y783/795F) cells, consistent with the impairment in FAK activation. In contrast, p130(CAS) overall tyrosine phosphorylation was unaffected by the beta1 mutations. Despite the defect in beta1-mediated FAK activation, FAK was still localized to focal adhesions. Taken together, the phenotype of the GD25-beta1A(Y783/795F) cells resembles, but is distinct from, the phenotype observed in FAK-null cells. These observations argue that tyrosines 783 and 795 within the cytoplasmic tail of integrin subunit beta1A are critical mediators of FAK activation and cell spreading in GD25 cells.
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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.