Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 39, Issue 10, Pages 487-495Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2014.08.006
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Funding
- MRC [U105192713]
- Medical Research Council [MC_U105184273, MC_U105192713] Funding Source: researchfish
- MRC [MC_U105184273, MC_U105192713] Funding Source: UKRI
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A key mechanism for guarding against inappropriate activation of signaling molecules is their weak affinity for effectors, which prevents them from undergoing accidental signal-transducing interactions due to fluctuations in their cellular concentration. The molecular devices that overcome these weak affinities are the signalosomes: dynamic clusters of transducing molecules assembled typically at signal-activated receptors. Signalosomes contain high local concentrations of protein-binding sites, and thus have a high avidity for their low-affinity ligands that generate signal responses. This review focuses on three domains - DIX (dishevelled and axin), PB1 (Phox and Bem1), and SAM (sterile alpha motif) - that undergo dynamic head-to-tail polymerization to assemble signalosomes and similar particles that require transient high local concentrations of protein-binding sites.
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