ArticleInternational journal of molecular sciences2021
Role of Site-Specific Glycosylation in the I-Like Domain of Integrin β1 in Small Extracellular Vesicle-Mediated Malignant Behavior and FAK Activation.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Systemic health impact of cancer-associated extracellular vesicles and particles.Nature reviews. Cancer · 2026Review
- Post-translational modifications of integrins: molecular mechanisms and pathological implications.Cellular and molecular life sciences : CMLS · 2026Review
- Small extracellular vesicles as system-level regulators and predictive biomarkers in breast cancer progression and chemoresistance.Frontiers in pharmacology · 2026Review
- N-Glycosylation as a Key Requirement for the Positive Interaction of Integrin and uPAR in Glioblastoma.International journal of molecular sciences · 2025Article
- Sialylation on vesicular integrin β1 determined endocytic entry of small extracellular vesicles into recipient cells.Cellular & molecular biology letters · 2024Article
- Deciphering the Functional Status of Breast Cancers through the Analysis of Their Extracellular Vesicles.International journal of molecular sciences · 2023Review
- Extracellular vesicles in the breast cancer brain metastasis: physiological functions and clinical applications.Frontiers in human neuroscience · 2023Review
- Review
- Site-specificiScience · 2021Article
- Regulation of Flowering Timing by ABA-NnSnRK1 Signaling Pathway in Lotus.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Integrin β1 plays an essential role in the crosstalk between tumor cells and their microenvironment. Aberrant N-glycosylation of integrin β1 was documented to alter integrin β1 expression, dimerization, and biological function. However, the biological function of site-specific N-glycosylation of integrin β1 on extracellular vesicles is not fully understood. In this study, we mutated putative N-glycosylation sites in different domains of integrin β1. Removal of the N-glycosylation sites on the I-like domain of integrin β1 (termed the Δ4-6 β1 mutant) suppressed focal adhesion kinase (FAK) signaling, cell migration, and adhesion compared with other β1 mutants. Cell adhesion, migration, and activation of FAK were suppressed in recipient MCF7 cells co-cultured with Δ4-6 mutant cells and treated with small extracellular vesicles (sEVs) from Δ4-6 mutant cells. Notably, the wild-type and β1 mutant were both present in sEVs, and could be transferred to recipient cells via sEVs, resulting in changes of cell behavior. Our findings demonstrate the important roles of N-glycosylation of the I-like domain of integrin β1. Moreover, the vesicular Δ4-6 β1 mutant can regulate integrin-mediated functions in recipient cells via sEVs.
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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.