期刊
ACS CHEMICAL BIOLOGY
卷 9, 期 11, 页码 2479-2484出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb5005806
关键词
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资金
- Deutsche Forschungsgemeinschaft [PI 405/5, SFB 944]
- European Community [223608]
Dimerization of transmembrane receptors is a key regulatory factor in cellular communication, which has remained challenging to study under well-defined conditions in vitro. We developed a novel strategy to explore membrane protein interactions in a controlled lipid environment requiring minute sample quantities. By rapid transfer of transmembrane proteins from mammalian cells into polymer-supported membranes, membrane proteins could be efficiently fluorescence labeled and reconstituted with very low background. Thus, differential ligand-induced dimerization of the type I interferon (IFN) receptor subunits IFNAR1 and IFNAR2 could be probed quantitatively at physiologically relevant concentrations by single molecule imaging. These measurements clearly support a regulatory role of the affinity of IFNs toward IFNAR1 for controlling the level of receptor dimerization.
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