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Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins.

Science (New York, N.Y.) | Sep 19, 2003

http://www.ncbi.nlm.nih.gov/pubmed/14500982

Although critical for development, immunity, wound healing, and metastasis, integrins represent one of the few classes of plasma membrane receptors for which the basic signaling mechanism remains a mystery. We investigated cytoplasmic conformational changes in the integrin LFA-1 (alphaLbeta2) in living cells by measuring fluorescence resonance energy transfer between cyan fluorescent protein-fused and yellow fluorescent protein-fused alphaL and beta2 cytoplasmic domains. In the resting state these domains were close to each other, but underwent significant spatial separation upon either intracellular activation of integrin adhesiveness (inside-out signaling) or ligand binding (outside-in signaling). Thus, bidirectional integrin signaling is accomplished by coupling extracellular conformational changes to an unclasping and separation of the alpha and beta cytoplasmic domains, a distinctive mechanism for transmitting information across the plasma membrane.

Pubmed ID: 14500982 RIS Download

Mesh terms: Antibodies, Monoclonal | Antigens, CD11a | Antigens, CD18 | Bacterial Proteins | Cell Adhesion | Cell Membrane | Chemokine CXCL12 | Chemokines, CXC | Cytoplasm | Dimerization | Fluorescence Resonance Energy Transfer | Green Fluorescent Proteins | Humans | Intercellular Adhesion Molecule-1 | Ligands | Luminescent Proteins | Lymphocyte Function-Associated Antigen-1 | Protein Conformation | Protein Structure, Tertiary | Receptors, CXCR4 | Recombinant Fusion Proteins | Signal Transduction | Talin | Transfection | Tumor Cells, Cultured