Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 39, Issue 2, Pages 82-90Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2013.12.003
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Funding
- European Research Council (ERC) [233312]
- Danish National Research Counsil
- Novo Nordisk Foundation
- Lundbeck Foundation
- Lundbeck Foundation [R54-2010-5637] Funding Source: researchfish
- European Research Council (ERC) [233312] Funding Source: European Research Council (ERC)
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Nutrients, biological waste-products, toxins, pathogens, and other ligands for endocytosis are typically captured by multidomain receptors with multiligand specificity. Upon internalization, the receptor-ligand complex segregates, followed by lysosomal degradation of the ligand and recycling of the receptor. Endosomal acidification and calcium efflux lead to the essential ligand-receptor affinity switch and separation. Recent data, including crystal structures of receptor-ligand complexes, now reveal how calcium, in different types of domain scaffolds, functions in a common way as a removable 'lynchpin' that stabilizes favorable positioning of ligand-attractive receptor residues. In addition to explaining how calcium depletion can cause ligand-receptor dissociation, the new data add further insight into how acidification contributes to dissociation through structural changes that affect the receptor calcium sites.
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