In this section
@article{Liu:2024:glycob/cwae083,
author = {Liu, Y and Drickamer, K and Taylor, ME},
doi = {glycob/cwae083},
journal = {Glycobiology},
title = {Preformed mincle dimers stabilized by an interchain disulfide bond in the neck region},
url = {http://dx.doi.org/10.1093/glycob/cwae083},
year = {2024}
}
TY - JOUR
AB - The sugar-binding receptor mincle stimulates macrophages when it encounters surface glycans on pathogens, such as trehalose dimycolate glycolipid in the outer membrane of mycobacteria. Binding of oligosaccharide ligands to the extracellular C-type carbohydrate-recognition domain (CRD) in mincle initiates intracellular signaling through the common Fc receptor γ (FcRγ) adapter molecule associated with mincle. One potential mechanism for initiation of signaling involves clustering of receptors, so it is important to understand the oligomeric state of mincle. Affinity purification of mincle from transfected mammalian cells has been used to show that mincle exists as a pre-formed, disulfide-linked dimer. Deletion of cysteine residues and chemical crosslinking further demonstrate that the dimers of mincle are stabilized by a disulfide bond between cysteine residues in the neck sequence that links the CRD to the membrane. In contrast, cysteine residues in the transmembrane region of mincle are not required for dimer formation or association with FcRγ. A protocol has been developed for efficient production of a disulfide-linked extracellular domain fragment of mincle in a bacterial expression system by appending synthetic dimerization domains to guide dimer formation in the absence of the membrane anchor.
AU - Liu,Y
AU - Drickamer,K
AU - Taylor,ME
DO - glycob/cwae083
PY - 2024///
SN - 1460-2423
TI - Preformed mincle dimers stabilized by an interchain disulfide bond in the neck region
T2 - Glycobiology
UR - http://dx.doi.org/10.1093/glycob/cwae083
UR - http://hdl.handle.net/10044/1/115012
ER -
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