ArticleThe Journal of biological chemistry2009
An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.
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 31 papers.
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Who cites it
31 citing papers in PubMed, 53 citations in OpenAlex.
- N-Glycosylation as a Key Requirement for the Positive Interaction of Integrin and uPAR in Glioblastoma.International journal of molecular sciences · 2025Article
- Structural insights into the molecular recognition of integrin αVβ3 by RGD-containing ligands: The role of the specificity-determining loop (SDL).bioRxiv : the preprint server for biology · 2024Article
- Review
- Biosynthesis and Biological Significances of LacdiNAc Group onBiomolecules · 2022Review
- Interferon lambda 4 impairs hepatitis C viral antigen presentation and attenuates T cell responses.Nature communications · 2021Article
- Ascites from Ovarian Cancer Induces Novel Fucosylated Proteins.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2019Article
- Review
- A complex between phosphatidylinositol 4-kinase IIα and integrin α3β1 is required forThe Journal of biological chemistry · 2019Article
- The importance of N-glycosylation on βScientific reports · 2017Article
- N-Glycosylation of integrin α5 acts as a switch for EGFR-mediated complex formation of integrin α5β1 to α6β4.Scientific reports · 2016Article
- Preventing E-cadherin aberrant N-glycosylation at Asn-554 improves its critical function in gastric cancer.Oncogene · 2016Article
- Atomic visualization of a flipped-back conformation of bisected glycans bound to specific lectins.Scientific reports · 2016Article
- Glycosylation of solute carriers: mechanisms and functional consequences.Pflugers Archiv : European journal of physiology · 2016Review
- PKN3 is the major regulator of angiogenesis and tumor metastasis in mice.Scientific reports · 2016Article
- Glycomic Approaches for the Discovery of Targets in Gastrointestinal Cancer.Frontiers in oncology · 2016Review
- Hijacking the Hexosamine Biosynthetic Pathway to Promote EMT-Mediated Neoplastic Phenotypes.Frontiers in oncology · 2016Review
- Epitopes in α8β1 and other RGD-binding integrins delineate classes of integrin-blocking antibodies and major binding loops in α subunits.Scientific reports · 2015Article
- Effect of ITGA5 down-regulation on the migration capacity of human dental pulp stem cells.International journal of clinical and experimental pathology · 2015Article
- Hexosamine-Induced TGF-β Signaling and Osteogenic Differentiation of Dental Pulp Stem Cells Are Dependent on N-Acetylglucosaminyltransferase V.BioMed research international · 2015Article
- An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.The Journal of biological chemistry · 2014Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently we reported that N-glycans on the beta-propeller domain of the integrin alpha5 subunit (S-3,4,5) are essential for alpha5beta1 heterodimerization, expression, and cell adhesion. Herein to further investigate which N-glycosylation site is the most important for the biological function and regulation, we characterized the S-3,4,5 mutants in detail. We found that site-4 is a key site that can be specifically modified by N-acetylglucosaminyltransferase III (GnT-III). The introduction of bisecting GlcNAc into the S-3,4,5 mutant catalyzed by GnT-III decreased cell adhesion and migration on fibronectin, whereas overexpression of N-acetylglucosaminyltransferase V (GnT-V) promoted cell migration. The phenomenon is similar to previous observations that the functions of the wild-type alpha5 subunit were positively and negatively regulated by GnT-V and GnT-III, respectively, suggesting that the alpha5 subunit could be duplicated by the S-3,4,5 mutant. Interestingly GnT-III specifically modified the S-4,5 mutant but not the S-3,5 mutant. This result was confirmed by erythroagglutinating phytohemagglutinin lectin blot analysis. The reduction in cell adhesion was consistently observed in the S-4,5 mutant but not in the S-3,5 mutant cells. Furthermore mutation of site-4 alone resulted in a substantial decrease in erythroagglutinating phytohemagglutinin lectin staining and suppression of cell spread induced by GnT-III compared with that of either the site-3 single mutant or wild-type alpha5. These results, taken together, strongly suggest that N-glycosylation of site-4 on the alpha5 subunit is the most important site for its biological functions. To our knowledge, this is the first demonstration that site-specific modification of N-glycans by a glycosyltransferase results in functional regulation.
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