期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 29, 期 -, 页码 143-151出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.07.006
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资金
- Swiss National Science Foundation (SNSF) [310030_153145, 31003A_141235]
- Swiss National Science Foundation (SNF) [310030_153145] Funding Source: Swiss National Science Foundation (SNF)
The past years have seen tremendous progress towards understanding how arrestins recognize phosphorylated G protein-coupled receptors (GPCRs). Two arrestin crystal structures, one of a pre-activated splice variant and one bound to a GPCR phosphopeptide, provided insights into the conformational changes upon phosphate recognition. Scanning mutagenesis and spectroscopic studies complete the picture of arrestin activation and receptor binding. Most perspicuous is the C-tail exchange mechanism, by which the C-tail of arrestin is released from its basal conformation and replaced by the phosphorylated GPCR C-terminus. Three positively charged clusters could act as conserved arrestin phosphosensors. Variations in the pattern of phosphorylation in a GPCR and variations within the C-terminus of different GPCRs may encode specificity to arrestin subtypes and particular physiological responses.
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