NDLI: Distinct phosphorylation sites on the ghrelin receptor, GHSR1a, establish a code thatdetermines the functions of ß-arrestins

Content Provider	PubMed Central
Author	Monica, Bouzo-lorenzo Santo-zas, Icía Lodeiro, Maria Nogueiras, Rubén Casanueva, Felipe F. Castro, Marian Pazos, Yolanda Tobin, Andrew B. Butcher, Adrian J. Camiña, Jesús P.
Copyright Year	2016
Abstract	The growth hormone secretagogue receptor, GHSR1a, mediates the biological activitiesof ghrelin, which includes the secretion of growth hormone, as well as thestimulation of appetite, food intake and maintenance of energy homeostasis. Mappingphosphorylation sites on GHSR1a and knowledge of how these sites control specificfunctional consequences unlocks new strategies for the development of therapeuticagents targeting individual functions. Herein, we have identified thephosphorylation of different sets of sites within GHSR1a which engender distinctfunctionality of ß-arrestins. More specifically, theSer362, Ser363 and Thr366 residuesat the carboxyl-terminal tail were primarily responsible for ß-arrestin1 and 2 binding, internalization and ß-arrestin-mediated proliferationand adipogenesis. The Thr350 and Ser349 are notnecessary for ß-arrestin recruitment, but are involved in thestabilization of the GHSR1a-ß-arrestin complex in a manner thatdetermines the ultimate cellular consequences of ß-arrestin signaling.We further demonstrated that the mitogenic and adipogenic effect of ghrelin weremainly dependent on the ß-arrestin bound to the phosphorylated GHSR1a.In contrast, the ghrelin function on GH secretion was entirely mediated by G proteinsignaling. Our data is consistent with the hypothesis that the phosphorylationpattern on the C terminus of GHSR1a determines the signaling and physiologicaloutput.
Related Links	http://dx.doi.org/10.1038/srep22495
Starting Page	22495
File Format	PDF
ISSN	20452322
e-ISSN	20452322
Journal	Scientific Reports
Volume Number	6
Language	English
Publisher	Nature Publishing Group
Publisher Date	2016-03-01
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Science and technology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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