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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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 |
work_keys_str_mv |
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