Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 26, Issue 1, Pages 43-54Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E14-06-1050
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Funding
- National Institutes of Health [HL081062, U54 MH074425-03S2]
- Leukemia and Lymphoma Society Grant [7388-06]
- Oxnard Foundation
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Lymphocyte function-associated antigen 1 (LFA-1, CD11a/CD18, alpha L beta 2-integrin) and its ligands are essential for adhesion between T-cells and antigen-presenting cells, formation of the immunological synapse, and other immune cell interactions. LFA-1 function is regulated through conformational changes that include the modulation of ligand binding affinity and molecular extension. However, the relationship between molecular conformation and function is unclear. Here fluorescence resonance energy transfer (FRET) with new LFA-1-specific fluorescent probes showed that triggering of the pathway used for T-cell activation induced rapid unquenching of the FRET signal consistent with extension of the molecule. Analysis of the FRET quenching at rest revealed an unexpected result that can be interpreted as a previously unknown LFA-1 conformation.
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