ArticleMolecular biology of the cell2000
Effects of I domain deletion on the function of the beta2 integrin lymphocyte function-associated antigen-1.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 46 citations in OpenAlex.
- Activation states of blood eosinophils in asthma.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2014Review
- CD11a polymorphisms regulate TH2 cell homing and TH2-related disease.The Journal of allergy and clinical immunology · 2014Article
- Integrin activation States and eosinophil recruitment in asthma.Frontiers in pharmacology · 2013Article
- Integrating receptor signal inputs that influence small Rho GTPase activation dynamics at the immunological synapse.Molecular and cellular biology · 2009Article
- Efalizumab binding to the LFA-1 alphaL I domain blocks ICAM-1 binding via steric hindrance.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Adhesion between human neutrophils and immobilized endothelial ligand vascular cell adhesion molecule 1: divalent ion effects.Biophysical journal · 2009Article
- Up-regulation and activation of eosinophil integrins in blood and airway after segmental lung antigen challenge.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- Aggregatibacter actinomycetemcomitans leukotoxin requires beta-sheets 1 and 2 of the human CD11a beta-propeller for cytotoxicity.Cellular microbiology · 2007Article
- The B cell antigen receptor controls integrin activity through Btk and PLCgamma2.The Journal of experimental medicine · 2003Article
- A novel form of integrin dysfunction involving beta1, beta2, and beta3 integrins.The Journal of clinical investigation · 2003Article
- An isolated, surface-expressed I domain of the integrin alphaLbeta2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Locking in alternate conformations of the integrin alphaLbeta2 I domain with disulfide bonds reveals functional relationships among integrin domains.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
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
A subset of integrin alpha subunits contain an I domain, which is important for ligand binding. We have deleted the I domain from the beta2 integrin lymphocyte function-asssociated antigen-1 (LFA-1) and expressed the resulting non-I domain-containing integrin (DeltaI-LFA-1) in an LFA-1-deficient T cell line. DeltaI-LFA-1 showed no recognition of LFA-1 ligands, confirming the essential role of the I domain in ligand binding. Except for I domain monoclonal antibodies (mAbs), DeltaI-LFA-1 was recognized by a panel of anti-LFA-1 mAbs similarly to wild-type LFA-1. However, DeltaI-LFA-1 had enhanced expression of seven mAb epitopes that are associated with beta2 integrin activation, suggesting that it exhibited an "active" conformation. In keeping with this characteristic, DeltaI-LFA-1 induced constitutive activation of alpha4beta1 and alpha5beta1, suggesting intracellular signaling to these integrins. This "cross-talk" was not due to an effect on beta1 integrin affinity. However, the enhanced activity was susceptible to inhibition by cytochalasin D, indicating a role for the cytoskeleton, and also correlated with clustering of beta1 integrins. Thus, removal of the I domain from LFA-1 created an integrin with the hallmarks of a constitutively active receptor mediating signals into the cell. These findings suggest a key role for the I domain in controlling integrin activity.
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