ArticleMolecular biology of the cell2003
Opposing roles of integrin alpha6Abeta1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 69 citations in OpenAlex.
- Porcine Single-Eye Retinal Pigment Epithelium Cell Culture for Barrier and Polarity Studies.Cells · 2025Article
- Extracellular matrix: Dystroglycan interactions-Roles for the dystrophin-associated glycoprotein complex in skeletal tissue dynamics.International journal of experimental pathology · 2025Review
- The role of laminins in cancer pathobiology: a comprehensive review.Journal of translational medicine · 2025Review
- Involvement of abnormal dystroglycan expression and matriglycan levels in cancer pathogenesis.Cancer cell international · 2022Review
- Integrin-mediated interactions with a laminin-presenting substrate modulate biosynthesis and phenotypic expression for cells of the human nucleus pulposus.European cells & materials · 2021Article
- Effects of Mini-Dystrophin on Dystrophin-Deficient, Human Skeletal Muscle-Derived Cells.International journal of molecular sciences · 2020Article
- A Family of Laminin α2 Chain-Deficient Mouse Mutants: Advancing the Research on LAMA2-CMD.Frontiers in molecular neuroscience · 2020Review
- The dystroglycan receptor maintains glioma stem cells in the vascular niche.Acta neuropathologica · 2019Article
- Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains.Frontiers in molecular biosciences · 2019Review
- Lassa Virus Cell Entry Reveals New Aspects of Virus-Host Cell Interaction.Journal of virology · 2017Review
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- Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.Cellular microbiology · 2013Article
- Binding of Lassa virus perturbs extracellular matrix-induced signal transduction via dystroglycan.Cellular microbiology · 2012Article
- Fer kinase regulates cell migration through α-dystroglycan glycosylation.Molecular biology of the cell · 2012Article
- Activation of brain endothelium by pneumococcal neuraminidase NanA promotes bacterial internalization.Cellular microbiology · 2010Article
- Proliferative, structural and molecular features of the Mdx mouse prostate.International journal of experimental pathology · 2010Article
- Dystroglycan is not required for maintenance of the luminal epithelial basement membrane or cell polarity in the mouse prostate.The Prostate · 2010Article
- Integrin α6β4 in colorectal cancer.World journal of gastrointestinal pathophysiology · 2010Article
- Dystroglycan versatility in cell adhesion: a tale of multiple motifs.Cell communication and signaling : CCS · 2010Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laminin-integrin interactions can in some settings activate the extracellular signal-regulated kinases (ERKs) but the control mechanisms are poorly understood. Herein, we studied ERK activation in response to two laminins isoforms (-1 and -10/11) in two epithelial cell lines. Both cell lines expressed beta1-containing integrins and dystroglycan but lacked integrin alpha6beta4. Antibody perturbation assays showed that both cell lines bound to laminin-10/11 via the alpha3beta1and alpha6beta1 integrins. Although laminin-10/11 was a stronger adhesion complex than laminin-1 for both cell lines, both laminins activated ERK in only one of the two cell lines. The ERK activation was mediated by integrin alpha6beta1 and not by alpha3beta1 or dystroglycan. Instead, we found that dystroglycan-binding domains of both laminin-1 and -10/11 suppressed integrin alpha6beta1-mediated ERK activation. Moreover, the responding cell line expressed the two integrin alpha6 splice variants, alpha6A and alpha6B, whereas the nonresponding cell line expressed only alpha6B. Furthermore, ERK activation was seen in cells transfected with the integrin alpha6A subunit, but not in alpha6B-transfected cells. We conclude that laminin-1 and -10/11 share the ability to induce ERK activation, that this is regulated by integrin alpha6Abeta1, and suggest a novel role for dystroglycan-binding laminin domains as suppressors of this activation.
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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.