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Department of Biomedicine

Christian Brix Folsted Andersen

How calcium makes endocytic receptors attractive

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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How calcium makes endocytic receptors attractive. / Andersen, Christian B F ; Moestrup, Søren K.

In: Trends in Biochemical Sciences, 03.01.2014.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Vancouver

Andersen CBF , Moestrup SK. How calcium makes endocytic receptors attractive. Trends in Biochemical Sciences. 2014 Jan 3. doi: 10.1016/j.tibs.2013.12.003

Author

Andersen, Christian B F ; Moestrup, Søren K. / How calcium makes endocytic receptors attractive. In: Trends in Biochemical Sciences. 2014.

Bibtex

@article{a7cc4152d086445c9b24219d89cbb9dd,

title = "How calcium makes endocytic receptors attractive",

abstract = "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.",

author = "Andersen, {Christian B F} and Moestrup, {S{\o}ren K}",

year = "2014",

month = jan,

day = "3",

doi = "10.1016/j.tibs.2013.12.003",

language = "English",

journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - How calcium makes endocytic receptors attractive

AU - Andersen, Christian B F

AU - Moestrup, Søren K

PY - 2014/1/3

Y1 - 2014/1/3

N2 - 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.

AB - 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.

U2 - 10.1016/j.tibs.2013.12.003

DO - 10.1016/j.tibs.2013.12.003

M3 - Journal article

C2 - 24393667

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

ER -