ArticleBiophysical journal2010
Role of altered sialylation of the I-like domain of beta1 integrin in the binding of fibronectin to beta1 integrin: thermodynamics and conformational analyses.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Spatial N-glycan rearrangement on αNature communications · 2025Article
- Growth factor-triggered de-sialylation controls glycolipid-lectin-driven endocytosis.Nature cell biology · 2025Article
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- Exploration into Galectin-3 Driven Endocytosis and Lattices.Biomolecules · 2024Article
- Integrin mechanosensing relies on a pivot-clip mechanism to reinforce cell adhesion.Biophysical journal · 2024Article
- Reducing Sialylation Enhances Electrotaxis of Corneal Epithelial Cells.International journal of molecular sciences · 2023Article
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- Vitamin D3 and its hydroxyderivatives as promising drugs against COVID-19: a computational study.Journal of biomolecular structure & dynamics · 2022Article
- Vitamin D and lumisterol derivatives can act on liver X receptors (LXRs).Scientific reports · 2021Article
- Sialylation of host proteins as targetable risk factor for COVID-19 susceptibility and spreading: A hypothesis.FASEB bioAdvances · 2021Article
- Site-Specific N- and O-Glycosylation Analysis of Human Plasma Fibronectin.Frontiers in chemistry · 2021Article
- Insight in Adhesion Protein Sialylation and Microgravity Dependent Cell Adhesion-An Omics Network Approach.International journal of molecular sciences · 2020Article
- Article
- Podocyte-Specific Sialylation-Deficient Mice Serve as a Model for Human FSGS.Journal of the American Society of Nephrology : JASN · 2019Article
- Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study.Protein science : a publication of the Protein Society · 2017Article
- Structural Insight for Roles of DR5 Death Domain Mutations on Oligomerization of DR5 Death Domain-FADD Complex in the Death-Inducing Signaling Complex Formation: A Computational Study.Journal of molecular modeling · 2016Article
- Role of UDP-N-acetylglucosamine2-epimerase/N-acetylmannosamine kinase (GNE) in β1-integrin-mediated cell adhesion.Molecular neurobiology · 2014Article
- An oncogenic protein Golgi phosphoprotein 3 up-regulates cell migration via sialylation.The Journal of biological chemistry · 2014Article
- Characterization of calmodulin-Fas death domain interaction: an integrated experimental and computational study.Biochemistry · 2014Article
- Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.Journal of virology · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-glycosylation of the I-like domain of beta1 integrin plays an essential role in integrin structure and function, and the altered sialylation of beta1 integrin regulates beta1 integrin binding to fibronectin. However, the structural basis underlying the effect of altered sialylation of the beta1 I-like domain on beta1 integrin binding to fibronectin remains largely unknown. In this study, we used a combination of molecular dynamics simulations and binding free energy analyses to investigate changes in binding thermodynamics and in conformation of the glycosylated beta1 I-like domain-FN-III(9-10) complex caused by altered sialylation of the beta1 I-like domain. Binding free energy analyses showed that desialylation of beta1 I-like domain increased beta1 integrin binding to fibronectin, consistent with experimental results. Interaction analyses showed that altered sialylation of the beta1 I-like domain resulted in significant changes in the interaction of the N-glycans of the I-like domain with both the I-like domain and fibronectin, and these changes could directly affect the allosteric regulation of the interaction between the I-like domain and fibronectin. Altered sialylation of the beta1 I-like domain caused significant conformational changes in key functional sites of both the beta1 I-like domain and fibronectin. In addition, altered sialylation of the beta1 I-like domain resulted in changes in the degree of correlated motions between residues in the I-like domain and residues in fibronectin, and in the degree of motion changes in fibronectin, which could affect beta1 integrin binding to fibronectin. We believe results from this study provide thermodynamic and structural evidence for a role of altered sialylation of beta1 integrin in regulating beta1 integrin binding to fibronectin and it's induced cellular activities.
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