Role of N-Linked Glycosylation in PKR2 Trafficking and Signaling.
| Autor: | Verdinez JA; Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, IA, United States.; Fraternal Order of Eagles Diabetes Research Center, University of Iowa, Iowa City, IA, United States.; Iowa Neuroscience Institute, University of Iowa, Iowa City, IA, United States., Sebag JA; Department of Molecular Physiology and Biophysics, Carver College of Medicine, University of Iowa, Iowa City, IA, United States.; Fraternal Order of Eagles Diabetes Research Center, University of Iowa, Iowa City, IA, United States.; Iowa Neuroscience Institute, University of Iowa, Iowa City, IA, United States. |
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| Jazyk: | angličtina |
| Zdroj: | Frontiers in neuroscience [Front Neurosci] 2021 Aug 13; Vol. 15, pp. 730417. Date of Electronic Publication: 2021 Aug 13 (Print Publication: 2021). |
| DOI: | 10.3389/fnins.2021.730417 |
| Abstrakt: | 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 Gα Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (Copyright © 2021 Verdinez and Sebag.) |
| Databáze: | MEDLINE |
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