ArticleBiophysical journal2009
LFA-1 binding destabilizes the JAM-A homophilic interaction during leukocyte transmigration.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 70 citations in OpenAlex.
- A novel epigenetic regulation of JAM-A by EZH2-DNMT3A cascade contributes to T cell adhesion via the activation of Rap1a in lupus patients.Journal of translational autoimmunity · 2026Article
- The role of Junctional Adhesion Molecule-A (JAM-A) in breast cancer metastasis.Molecular biology reports · 2026Review
- JAM-A: Adhesion Receptor and Signaling Regulator in Atherosclerosis.Current atherosclerosis reports · 2025Review
- ADTnorm: robust integration of single-cell protein measurement across CITE-seq datasets.Nature communications · 2025Article
- SubvertingBiology · 2024Review
- Pathophysiology in Brain Arteriovenous Malformations: Focus on Endothelial Dysfunctions and Endothelial-to-Mesenchymal Transition.Biomedicines · 2024Review
- Thy-1 (CD90)-regulated cell adhesion and migration of mesenchymal cells: insights into adhesomes, mechanical forces, and signaling pathways.Frontiers in cell and developmental biology · 2023Review
- Dissecting the molecular control of immune cell accumulation in the inflamed joint.JCI insight · 2022Article
- Understanding the Role of LFA-1 in Leukocyte Adhesion Deficiency Type I (LAD I): Moving towards Inflammation?International journal of molecular sciences · 2022Review
- The Roles of Junctional Adhesion Molecules (JAMs) in Cell Migration.Frontiers in cell and developmental biology · 2022Review
- The F11 Receptor (F11R)/Junctional Adhesion Molecule-A (JAM-A) (F11R/JAM-A) in cancer progression.Molecular and cellular biochemistry · 2022Review
- Astrocytic junctional adhesion molecule-A regulates T-cell entry past the glia limitans to promote central nervous system autoimmune attack.Brain communications · 2022Article
- Targeting Opposing Immunological Roles of the Junctional Adhesion Molecule-A in Autoimmunity and Cancer.Frontiers in immunology · 2020Review
- Analysis of leukocyte transepithelial migration using an in vivo murine colonic loop model.JCI insight · 2018Article
- Junctional adhesion molecule-A: functional diversity through molecular promiscuity.Cellular and molecular life sciences : CMLS · 2018Review
- Review
- Astrocytic tight junctions control inflammatory CNS lesion pathogenesis.The Journal of clinical investigation · 2017Article
- Tension on JAM-A activates RhoA via GEF-H1 and p115 RhoGEF.Molecular biology of the cell · 2016Article
- N-glycosylation controls the function of junctional adhesion molecule-A.Molecular biology of the cell · 2015Article
- Investigation of the monocyte diapedesis-related LFA-1 and JAM-A gene variants in Turkish coronary heart disease patients.Meta gene · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Leukocyte transendothelial migration into inflamed areas is regulated by the integrity of endothelial cell junctions and is stabilized by adhesion molecules including junctional adhesion molecule-A (JAM-A). JAM-A has been shown to participate in homophilic interactions with itself and in heterophilic interactions with leukocyte function-associated antigen-1 (LFA-1) via its first and second immunoglobulin domains, respectively. Using competitive binding assays in conjunction with atomic force microscopy adhesion measurements, we provide compelling evidence that the second domain of JAM-A stabilizes the homophilic interaction because its deletion suppresses the dynamic strength of the JAM-A homophilic interaction. Moreover, binding of the LFA-1 inserted domain to the second domain of JAM-A reduces the dynamic strength of the JAM-A homophilic interaction to the level measured with the JAM-A domain 2 deletion mutant. This finding suggests that LFA-1 binding cancels the stabilizing effects of the second immunoglobulin domain of JAM-A. Finally, our atomic force microscopy measurements reveal that the interaction of JAM-A with LFA-1 is stronger than the JAM-A homophilic interaction. Taken together, these results suggest that LFA-1 binding to JAM-A destabilizes the JAM-A homophilic interaction. In turn, the greater strength of the LFA-1/JAM-A complex permits it to support the tension needed to disrupt the JAM-A homophilic interaction, thus allowing transendothelial migration to proceed.
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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.