期刊
SCIENCE
卷 301, 期 5640, 页码 1720-1725出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1084174
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资金
- NCI NIH HHS [CA31798] Funding Source: Medline
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 (alpha(L)beta(2)) in living cells by measuring fluorescence resonance energy transfer between cyan fluorescent protein - fused and yellow fluorescent protein - fused alpha(L) and beta(2) 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.
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