dc.contributor.author
Peterhans, Christian
dc.contributor.author
Lally, Ciara C. M.
dc.contributor.author
Ostermaier, Martin K.
dc.contributor.author
Sommer, Martha E.
dc.contributor.author
Standfuss, Joerg
dc.date.accessioned
2018-06-08T03:59:29Z
dc.date.available
2016-08-10T10:55:52.138Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/16364
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-20547
dc.description.abstract
Arrestins desensitize G protein-coupled receptors (GPCRs) and act as mediators
of signalling. Here we investigated the interactions of arrestin-1 with two
functionally distinct forms of the dim-light photoreceptor rhodopsin. Using
unbiased scanning mutagenesis we probed the individual contribution of each
arrestin residue to the interaction with the phosphorylated apo-receptor
(Ops-P) and the agonist-bound form (Meta II-P). Disruption of the polar core
or displacement of the C-tail strengthened binding to both receptor forms. In
contrast, mutations of phosphate-binding residues (phosphosensors) suggest the
phosphorylated receptor C-terminus binds arrestin differently for Meta II-P
and Ops-P. Likewise, mutations within the inter-domain interface, variations
in the receptor-binding loops and the C-edge of arrestin reveal different
binding modes. In summary, our results indicate that arrestin-1 binding to
Meta II-P and Ops-P is similarly dependent on arrestin activation, although
the complexes formed with these two receptor forms are structurally distinct.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Biological fluorescence
dc.subject
High-throughput screening
dc.subject
Protein design
dc.subject
Structural biology
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie
dc.title
Functional map of arrestin binding to phosphorylated opsin, with and without
agonist
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Scientific Reports. - 6 (2016), Artikel Nr. 28686
dcterms.bibliographicCitation.doi
10.1038/srep28686
dcterms.bibliographicCitation.url
http://www.nature.com/articles/srep28686
refubium.affiliation
Charité - Universitätsmedizin Berlin
de
refubium.mycore.fudocsId
FUDOCS_document_000000025062
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000006806
dcterms.accessRights.openaire
open access