A GIPC1-palmitate switch modulates dopamine drd3 receptor trafficking and signaling

Basit Öğe Kaydı
dc.authorid0000-0001-5950-3436
dc.contributor.authorArango-Lievano, Margarita
dc.contributor.authorŞensoy, Özge
dc.contributor.authorBorie, Amelie
dc.contributor.authorCorbani, Maithe
dc.contributor.authorGuillon, Gilles
dc.contributor.authorSokoloff, Pierre
dc.contributor.authorWeinstein, Harel
dc.contributor.authorJeanneteau, Freddy
dc.date.accessioned10.07.201910:49:13
dc.date.accessioned2019-07-10T20:01:48Z
dc.date.available10.07.201910:49:13
dc.date.available2019-07-10T20:01:48Z
dc.date.issued2016
dc.departmentİstanbul Medipol Üniversitesi, Mühendislik ve Doğa Bilimleri Fakültesi, Bilgisayar Mühendisliği Bölümü
dc.descriptionWOS: 000372330700014
dc.descriptionPubMed ID: 26787837
dc.description.abstractPalmitoylation is involved in several neuropsychiatric and movement disorders for which a dysfunctional signaling of the dopamine D3 receptor (Drd3) is hypothesized. Computational modeling of Drd3's homologue, Drd2, has shed some light on the putative role of palmitoylation as a reversible switch for dopaminergic receptor signaling. Drd3 is presumed to be palmitoylated, based on sequence homology with Drd2, but the functional attributes afforded by Drd3 palmitoylation have not been studied. Since these receptors are major targets of antipsychotic and anti-Parkinsonian drugs, a better characterization of Drd3 signaling and posttranslational modifications, like palmitoylation, may improve the prospects for drug development. Using molecular dynamics simulations, we evaluated in silico how Drd3 palmitoylation could elicit significant remodeling of the C-terminal cytoplasmic domain to expose docking sites for signaling proteins. We tested this model in cellulo by using the interaction of Drd3 with the G-alpha interacting protein (GAIP) C terminus 1 (GIPC1) as a template. From a series of biochemical studies, live imaging, and analyses of mutant proteins, we propose that Drd3 palmitoylation acts as a molecular switch for Drd3-biased signaling via a GIPC1-dependent route, which is likely to affect the mode of action of antipsychotic drugs.
dc.description.sponsorshipFondation pour la recherche medicale; French ministry of research; Fondation de Franceen_US
dc.description.sponsorshipFondation pour la recherche medicale provided funding to Pierre Sokoloff and Freddy Jeanneteau. French ministry of research provided funding to Freddy Jeanneteau. Fondation de France provided funding to Margarita Arango-Lievano and Freddy Jeanneteau.en_US
dc.identifier.citationArango Lievano, M., Şensoy, Ö., Borie, A., Corbani, M., Guillon, G., Sokoloff, P. ... Jeanneteau, F. (2016). A GIPC1-palmitate switch modulates dopamine drd3 receptor trafficking and signaling. Molecular And Cellular Biology, 36(6), 1019-1031. https://dx.doi.org/10.1128/MCB.00916-15
dc.identifier.doi10.1128/MCB.00916-15
dc.identifier.endpage1031
dc.identifier.issn0270-7306
dc.identifier.issn1098-5549
dc.identifier.issue6
dc.identifier.scopusqualityQ1
dc.identifier.startpage1019
dc.identifier.urihttps://dx.doi.org/10.1128/MCB.00916-15
dc.identifier.urihttps://hdl.handle.net/20.500.12511/3451
dc.identifier.volume36
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherAmer Soc Microbiology
dc.relation.ispartofMolecular And Cellular Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleA GIPC1-palmitate switch modulates dopamine drd3 receptor trafficking and signaling
dc.typeArticle

Dosyalar

Orijinal paket
Listeleniyor 1 - 1 / 1
Küçük Resim
İsim:
Sensoy-Ozge 2016.pdf
Boyut:
5.18 MB
Biçim:
Adobe Portable Document Format
Açıklama:
Tam Metin / Full Text
İndir

Koleksiyon

Scopus İndeksli Yayınlar Koleksiyonu
Makale Koleksiyonu
PubMed İndeksli Yayınlar Koleksiyonu
WoS İndeksli Yayınlar Koleksiyonu