Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling

Prokineticin receptors are GPCRs involved in several physiological processes including the regulation of energy homeostasis, nociception, and reproductive function. PKRs are inhibited by the endogenous accessory protein MRAP2 which prevents them from trafficking to the plasma membrane. Very little i...

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Main Authors: Jissele A. Verdinez, Julien A. Sebag
Format: Article
Language:English
Published: Frontiers Media S.A. 2021-08-01
Series:Frontiers in Neuroscience
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fnins.2021.730417/full
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spelling doaj-56986f09b06345fab3c8e15d1f62bae12021-08-13T06:15:00ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2021-08-011510.3389/fnins.2021.730417730417Role of N-Linked Glycosylation in PKR2 Trafficking and SignalingJissele A. Verdinez0Jissele A. Verdinez1Jissele A. Verdinez2Julien A. Sebag3Julien A. Sebag4Julien A. Sebag5Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, IA, United StatesFraternal Order of Eagles Diabetes Research Center, University of Iowa, Iowa City, IA, United StatesIowa Neuroscience Institute, University of Iowa, Iowa City, IA, United StatesDepartment of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, IA, United StatesFraternal Order of Eagles Diabetes Research Center, University of Iowa, Iowa City, IA, United StatesIowa Neuroscience Institute, University of Iowa, Iowa City, IA, United StatesProkineticin receptors are GPCRs involved in several physiological processes including the regulation of energy homeostasis, nociception, and reproductive function. PKRs are inhibited by the endogenous accessory protein MRAP2 which prevents them from trafficking to the plasma membrane. Very little is known about the importance of post-translational modification of PKRs and their role in receptor trafficking and signaling. Here we identify 2 N-linked glycosylation sites within the N-terminal region of PKR2 and demonstrate that glycosylation of PKR2 at position 27 is important for its plasma membrane localization and signaling. Additionally, we show that glycosylation at position 7 results in a decrease in PKR2 signaling through Gαs without impairing Gαq/11 signaling.https://www.frontiersin.org/articles/10.3389/fnins.2021.730417/fullprokineticin receptorGPCRMRAP2traffickingglycosylation
collection DOAJ
language English
format Article
sources DOAJ
author Jissele A. Verdinez
Jissele A. Verdinez
Jissele A. Verdinez
Julien A. Sebag
Julien A. Sebag
Julien A. Sebag
spellingShingle Jissele A. Verdinez
Jissele A. Verdinez
Jissele A. Verdinez
Julien A. Sebag
Julien A. Sebag
Julien A. Sebag
Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling
Frontiers in Neuroscience
prokineticin receptor
GPCR
MRAP2
trafficking
glycosylation
author_facet Jissele A. Verdinez
Jissele A. Verdinez
Jissele A. Verdinez
Julien A. Sebag
Julien A. Sebag
Julien A. Sebag
author_sort Jissele A. Verdinez
title Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling
title_short Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling
title_full Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling
title_fullStr Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling
title_full_unstemmed Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling
title_sort role of n-linked glycosylation in pkr2 trafficking and signaling
publisher Frontiers Media S.A.
series Frontiers in Neuroscience
issn 1662-453X
publishDate 2021-08-01
description Prokineticin receptors are GPCRs involved in several physiological processes including the regulation of energy homeostasis, nociception, and reproductive function. PKRs are inhibited by the endogenous accessory protein MRAP2 which prevents them from trafficking to the plasma membrane. Very little is known about the importance of post-translational modification of PKRs and their role in receptor trafficking and signaling. Here we identify 2 N-linked glycosylation sites within the N-terminal region of PKR2 and demonstrate that glycosylation of PKR2 at position 27 is important for its plasma membrane localization and signaling. Additionally, we show that glycosylation at position 7 results in a decrease in PKR2 signaling through Gαs without impairing Gαq/11 signaling.
topic prokineticin receptor
GPCR
MRAP2
trafficking
glycosylation
url https://www.frontiersin.org/articles/10.3389/fnins.2021.730417/full
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