期刊
NATURE REVIEWS IMMUNOLOGY
卷 6, 期 9, 页码 693-698出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nri1916
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资金
- MRC [G0400007] Funding Source: UKRI
- Medical Research Council [G0400007] Funding Source: researchfish
- Medical Research Council [G1000133, G0400007] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Members of the Toll family of single-pass transmembrane receptors are key mediators of innate immunity in both vertebrates and invertebrates. They respond to various pathogen-associated stimuli and transduce the complex signalling responses that are required for inflammation and for the subsequent development of adaptive immunity. Here, we propose a molecular mechanism for signalling by the Toll and Toll-like receptors that involves a series of protein conformational changes initiated by dimerization of their extracellular domains. The initial dimerization event, which is triggered by the interaction of the receptor with its ligand, might disrupt a pre-formed but non-functional dimer. Formation of a stable receptor-ligand complex then relieves constitutive autoinhibition, enabling receptor-receptor association of the extracellular juxtamembrane regions and cytoplasmic signalling domains. This activation process constitutes a tightly regulated, unidirectional molecular switch.
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