ArticleThe Journal of cell biology1996
The intracellular functions of alpha6beta4 integrin are regulated by EGF.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 184 citations in OpenAlex.
- Regulation of Kinase Signaling Pathways by α6β4-Integrins and Plectin in Prostate Cancer.Cancers · 2022Review
- Integrin α6β4 signals through DNA damage response pathway to sensitize breast cancer cells to cisplatin.Frontiers in oncology · 2022Article
- EGFR-dependent tyrosine phosphorylation of integrin β4 is not required for downstream signaling events in cancer cell lines.Scientific reports · 2021Article
- Adhesion-growth factor crosstalk regulates AURKB activation and ERK signalling in re-adherent fibroblasts.Journal of biosciences · 2021Article
- Interplay between Cell-Surface Receptors and Extracellular Matrix in Skin.Biomolecules · 2020Review
- EGF/EGFR upregulates and cooperates with Netrin-4 to protect glioblastoma cells from DNA damage-induced senescence.BMC cancer · 2018Article
- Complexes of α6β4 integrin and vimentin act as signaling hubs to regulate epithelial cell migration.Journal of cell science · 2018Article
- Roles of Integrin α6β4 Glycosylation in Cancer.Cancers · 2017Review
- Epstein-Barr virus-encoded LMP2A stimulates migration of nasopharyngeal carcinoma cells via the EGFR/CaBiology open · 2017Article
- αAmerican journal of respiratory cell and molecular biology · 2017Article
- α6β4 Integrin Genetic Variations (A380T and R1281W) and Breast Cancer Risk in an Argentinian Population.International journal of molecular sciences · 2016Article
- Elevated integrin α6β4 expression is associated with venous invasion and decreased overall survival in non-small cell lung cancer.Human pathology · 2016Article
- Integrin α6β4 Promotes Autocrine Epidermal Growth Factor Receptor (EGFR) Signaling to Stimulate Migration and Invasion toward Hepatocyte Growth Factor (HGF).The Journal of biological chemistry · 2015Article
- Clinical significance of the integrin α6β4 in human malignancies.Laboratory investigation; a journal of technical methods and pathology · 2015Review
- Convergence of eicosanoid and integrin biology: 12-lipoxygenase seeks a partner.Molecular cancer · 2015Article
- Molecular architecture and function of the hemidesmosome.Cell and tissue research · 2015Review
- Molecular architecture and function of the hemidesmosome.Cell and tissue research · 2015Review
- Up-regulation of integrin α6β4 expression by mitogens involved in dairy cow mammary development.In vitro cellular & developmental biology. Animal · 2015Article
- Article
- Cytoplasmic domain interactions of syndecan-1 and syndecan-4 with α6β4 integrin mediate human epidermal growth factor receptor (HER1 and HER2)-dependent motility and survival.The Journal of biological chemistry · 2014Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Upon ligand binding, the alpha6beta4 integrin becomes phosphorylated on tyrosine residues and combines sequentially with the adaptor molecules Shc and Grb2, linking to the ras pathway, and with cytoskeletal elements of hemidesmosomes. Since alpha6beta4 is expressed in a variety of tissues regulated by the EGF receptor (EGFR), we have examined the effect of EGF on the cytoskeletal and signaling functions of alpha6beta4. Experiments of immunoblotting with anti-phosphotyrosine antibodies and immunoprecipitation followed by phosphoamino acid analysis and phosphopeptide mapping showed that activation of the EGFR causes phosphorylation of the beta4 subunit at multiple tyrosine residues, and this event requires ligation of the integrin by laminins or specific antibodies. Immunoprecipitation experiments indicated that stimulation with EGF does not result in association of alpha6beta4 with Shc. In contrast, EGF can partially suppress the recruitment of Shc to ligated alpha6beta4. Immunofluorescent analysis revealed that EGF treatment does not induce increased assembly of hemidesmosomes, but instead causes a deterioration of these adhesive structures. Finally, Boyden chamber assays indicated that exposure to EGF results in upregulation of alpha6beta4-mediated cell migration toward laminins. We conclude that EGF-dependent signals suppress the association of activated alpha6beta4 with both signaling and cytoskeletal molecules, but upregulate alpha6beta4-dependent cell migration. The changes in alpha6beta4 function induced by EGF may play a role during wound healing and tumorigenesis.
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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.