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dc.contributor.author
Mayer, Daniel
dc.contributor.author
Damberger, Fred F.
dc.contributor.author
Samarasimhareddy, Mamidi
dc.contributor.author
Feldmueller, Miki
dc.contributor.author
Vuckovic, Ziva
dc.contributor.author
Flock, Tilman
dc.contributor.author
Bauer, Brian
dc.contributor.author
Mutt, Eshita
dc.contributor.author
Zosel, Franziska
dc.contributor.author
Allain, Frédéric H.-T.
dc.contributor.author
Standfuss, Jörg
dc.contributor.author
Schertler, Gebhard F.X.
dc.contributor.author
Deupi, Xavier
dc.contributor.author
Sommer, Martha E.
dc.contributor.author
Hurevich, Mattan
dc.contributor.author
Friedler, Assaf
dc.contributor.author
Veprintsev, Dmitry B.
dc.date.accessioned
2019-04-01T14:19:45Z
dc.date.available
2019-03-30T01:49:06Z
dc.date.available
2019-04-01T14:19:45Z
dc.date.issued
2019
dc.identifier.other
10.1038/s41467-019-09204-y
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/334922
dc.identifier.doi
10.3929/ethz-b-000334922
dc.description.abstract
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.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2019-03-19
ethz.journal.title
Nature Communications
ethz.journal.volume
10
en_US
ethz.pages.start
1261
en_US
ethz.size
14 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2019-03-30T01:49:07Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2019-04-01T14:19:58Z
ethz.rosetta.lastUpdated
2019-04-01T14:19:58Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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