期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-09204-y
关键词
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资金
- Swiss National Science Foundation [135754, 159748, 310030_153145, 310030B_173335, SNF Sinergia CRSII3_141898]
- Israeli Science Foundation [939/14]
- Deutsche Forschungsgemeinschaft [SO1037/1-3]
- Berlin Institute of Health [BIH_PRO_314]
- ETH Zurich
- European Union [664786]
- Hebrew University
- Swiss National Science Foundation (SNF) [310030B_173335, 310030_153145] Funding Source: Swiss National Science Foundation (SNF)
Cellular functions of arrestins are determined in part by the pattern of phosphorylation on the G protein-coupled receptors (GPCRs) to which arrestins bind. Despite high-resolution structural data of arrestins bound to phosphorylated receptor C-termini, the functional role of each phosphorylation site remains obscure. Here, we employ a library of synthetic phosphopeptide analogues of the GPCR rhodopsin C-terminus and determine the ability of these peptides to bind and activate arrestins using a variety of biochemical and biophysical methods. We further characterize how these peptides modulate the conformation of arrestin 1 by nuclear magnetic resonance (NMR). Our results indicate different functional classes of phosphorylation sites: 'key sites' required for arrestin binding and activation, an 'inhibitory site' that abrogates arrestin binding, and 'modulator sites' that influence the global conformation of arrestin. These functional motifs allow a better understanding of how different GPCR phosphorylation patterns might control how arrestin functions in the cell.
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