Molecular determinants of orexin receptor-arrestinubiquitin complex formation

Molecular determinants of orexin receptor-arrestinubiquitin complex formation

Background and Purpose: The orexin system regulates a multitude of key physiological processes, particularly involving maintenance of metabolic homeostasis. Consequently, there is considerable potential for pharmaceutical development for the treatment of disorders from narcolepsy to metabolic syndro...

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Main Authors: Jaeger, Werner C, Seeber, Ruth M, Eidne, Karin A, Pfleger, Kevin DG
Format: Online
Language:English
Published: John Wiley & Sons Ltd 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3904257/
id pubmed-3904257
recordtype oai_dc
spelling pubmed-39042572014-12-08 Molecular determinants of orexin receptor-arrestinubiquitin complex formation Jaeger, Werner C Seeber, Ruth M Eidne, Karin A Pfleger, Kevin DG Themed Section: Orexin Receptors Background and Purpose: The orexin system regulates a multitude of key physiological processes, particularly involving maintenance of metabolic homeostasis. Consequently, there is considerable potential for pharmaceutical development for the treatment of disorders from narcolepsy to metabolic syndrome. It acts through the hormonal activity of two endogenous peptides, orexin A binding to orexin receptors 1 and 2 (OX1 and OX2) with similar affinity, and orexin B binding to OX2 with higher affinity than OX1 receptors. We have previously revealed data differentiating orexin receptor subtypes with respect to their relative stability in forming orexin receptor-arrestin-ubiquitin complexes measured by BRET. Recycling and cellular signalling distinctions were also observed. Here, we have investigated, using BRET, the molecular determinants involved in providing OX2 receptors with greater β-arrestin-ubiquitin complex stability. John Wiley & Sons Ltd 2014-01 2013-12-23 /pmc/articles/PMC3904257/ /pubmed/24206104 http://dx.doi.org/10.1111/bph.12481 Text en Copyright © 2014 The British Pharmacological Society http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Jaeger, Werner C
Seeber, Ruth M
Eidne, Karin A
Pfleger, Kevin DG
spellingShingle Jaeger, Werner C
Seeber, Ruth M
Eidne, Karin A
Pfleger, Kevin DG
Molecular determinants of orexin receptor-arrestinubiquitin complex formation
author_facet Jaeger, Werner C
Seeber, Ruth M
Eidne, Karin A
Pfleger, Kevin DG
author_sort Jaeger, Werner C
title Molecular determinants of orexin receptor-arrestinubiquitin complex formation
title_short Molecular determinants of orexin receptor-arrestinubiquitin complex formation
title_full Molecular determinants of orexin receptor-arrestinubiquitin complex formation
title_fullStr Molecular determinants of orexin receptor-arrestinubiquitin complex formation
title_full_unstemmed Molecular determinants of orexin receptor-arrestinubiquitin complex formation
title_sort molecular determinants of orexin receptor-arrestinubiquitin complex formation
description Background and Purpose: The orexin system regulates a multitude of key physiological processes, particularly involving maintenance of metabolic homeostasis. Consequently, there is considerable potential for pharmaceutical development for the treatment of disorders from narcolepsy to metabolic syndrome. It acts through the hormonal activity of two endogenous peptides, orexin A binding to orexin receptors 1 and 2 (OX1 and OX2) with similar affinity, and orexin B binding to OX2 with higher affinity than OX1 receptors. We have previously revealed data differentiating orexin receptor subtypes with respect to their relative stability in forming orexin receptor-arrestin-ubiquitin complexes measured by BRET. Recycling and cellular signalling distinctions were also observed. Here, we have investigated, using BRET, the molecular determinants involved in providing OX2 receptors with greater β-arrestin-ubiquitin complex stability.
publisher John Wiley & Sons Ltd
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3904257/
_version_ 1612051968485752832

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