ArticlePloS one2011
N-glycosylation of ß4 integrin controls the adhesion and motility of keratinocytes.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 45 citations in OpenAlex.
- Integrins in Cancer Drug Resistance: Molecular Mechanisms and Clinical Implications.International journal of molecular sciences · 2025Review
- Integrin α6β4 Confers Doxorubicin Resistance in Cancer Cells by Suppressing Caspase-3-Mediated Apoptosis: Involvement of N-Glycans on β4 Integrin Subunit.Biomolecules · 2023Article
- Native Autoantigen Complex Detects Pemphigoid Autoantibodies.JID innovations : skin science from molecules to population health · 2023Article
- Non-canonical integrin signaling activates EGFR and RAS-MAPK-ERK signaling in small cell lung cancer.Theranostics · 2023Article
- Lack of NPR1 Increases Vascular Endothelial Adhesion through Induction of Integrin Beta 4.International journal of molecular sciences · 2022Article
- TM4SF1 promotes esophageal squamous cell carcinoma metastasis by interacting with integrin α6.Cell death & disease · 2022Article
- The cell surface protein MUL_3720 confers binding of the skin pathogen Mycobacterium ulcerans to sulfated glycans and keratin.PLoS neglected tropical diseases · 2021Article
- Extracellular Vesicles and Glycosylation.Advances in experimental medicine and biology · 2021Article
- Quantitative analysis of β1,6GlcNAc-branched N-glycans on β4 integrin in cutaneous squamous cell carcinoma.Fukushima journal of medical science · 2020Article
- Determination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics.Chemical science · 2020Article
- Interplay between Cell-Surface Receptors and Extracellular Matrix in Skin.Biomolecules · 2020Review
- N-Acetylglucosaminyltransferase III (GnT-III) but not N-Acetylgalactosaminyltransferase-6 and 8 are Differentially Expressed in Invasive and In Situ Ductal Carcinoma of the Breast.Pathology oncology research : POR · 2019Article
- Roles of Integrin α6β4 Glycosylation in Cancer.Cancers · 2017Review
- Specific N-glycan alterations are coupled in EMT induced by different density cultivation of MCF 10A epithelial cells.Glycoconjugate journal · 2017Article
- N-Glycosylation of integrin α5 acts as a switch for EGFR-mediated complex formation of integrin α5β1 to α6β4.Scientific reports · 2016Article
- Review
- Glycomics and glycoproteomics of membrane proteins and cell-surface receptors: Present trends and future opportunities.Electrophoresis · 2016Review
- High mannose-binding Pseudomonas fluorescens lectin (PFL) downregulates cell surface integrin/EGFR and induces autophagy in gastric cancer cells.BMC cancer · 2016Article
- Integrin α5 Suppresses the Phosphorylation of Epidermal Growth Factor Receptor and Its Cellular Signaling of Cell Proliferation via N-Glycosylation.The Journal of biological chemistry · 2015Article
- Role of Integrin β4 in Lung Endothelial Cell Inflammatory Responses to Mechanical Stress.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α6ß4 integrin is an essential component of hemidesmosomes and modulates cell migration in wound healing and cancer invasion. To elucidate the role of N-glycosylation on ß4 integrin, we investigated keratinocyte adhesion and migration through the re-expression of wild-type or N-glycosylation-defective ß4 integrin (ΔNß4) in ß4 integrin null keratinocytes. N-glycosylation of ß4 integrin was not essential for the heterodimer formation of ß4 integrin with α6 integrin and its expression on a cell surface, but N-glycosylation was required for integrin-mediated cell adhesion and migration. Concomitantly with the reduction of ß4 integrin in the membrane microdomain, the intracellular signals of Akt and ERK activation were decreased in cells expressing ΔNß4 integrin. Forced cross-linking of ß4 integrin rescued the decreased ERK activation in ΔNß4 integrin-expressing cells to a similar extent in wild-type ß4 integrin-expressing cells. Surprisingly, compared with cells expressing wild-type ß4 integrin, an alternation in N-glycan structures expressed on epidermal growth factor receptor (EGFR), and the induction of a stronger association between EGFR and ß4 integrin were observed in ΔNß4 integrin-expressing cells. These results clearly demonstrated that N-glycosylation on ß4 integrin plays an essential role in keratinocyte cellular function by allowing the appropriate complex formation on cell surfaces.
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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.