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FRET detection of lymphocyte function–associated antigen-1 conformational extension

Lymphocyte function–associated antigen 1 (LFA-1, CD11a/CD18, αLβ2-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...

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Detalles Bibliográficos
Autores principales: Chigaev, Alexandre, Smagley, Yelena, Haynes, Mark K., Ursu, Oleg, Bologa, Cristian G., Halip, Liliana, Oprea, Tudor, Waller, Anna, Carter, Mark B., Zhang, Yinan, Wang, Wei, Buranda, Tione, Sklar, Larry A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279228/
https://www.ncbi.nlm.nih.gov/pubmed/25378583
http://dx.doi.org/10.1091/mbc.E14-06-1050
Descripción
Sumario:Lymphocyte function–associated antigen 1 (LFA-1, CD11a/CD18, αLβ2-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.