Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms

Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms

The type 2 dopamine receptor D<sub>2</sub> (D<sub>2</sub>-R), member of the G protein-coupled receptor (GPCR) superfamily, exists in two isoforms, short (D<sub>2S</sub>-R) and long (D<sub>2L</sub>-R). They differ by an additional 29 amino acids (AA) in...

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Main Authors: Kaja Blagotinšek Cokan, Maša Mavri, Catrin Sian Rutland, Sanja Glišić, Milan Senćanski, Milka Vrecl, Valentina Kubale
Format: Article
Language:English
Published: MDPI AG 2020-09-01
Series:Biomolecules
Subjects:
D<sub>2</sub> dopamine receptor
intracellular trafficking
endoplasmic reticulum
retention motifs
ICL3
interacting partners
Online Access:https://www.mdpi.com/2218-273X/10/10/1355
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spelling doaj-a4dc4a35dfbf49e6ba91dfe286bcbefb2020-11-25T03:22:17ZengMDPI AGBiomolecules2218-273X2020-09-01101355135510.3390/biom10101355Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) IsoformsKaja Blagotinšek Cokan0Maša Mavri1Catrin Sian Rutland2Sanja Glišić3Milan Senćanski4Milka Vrecl5Valentina Kubale6Department of Anatomy, Histology with Embryology and Cytology, Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, SloveniaDepartment of Anatomy, Histology with Embryology and Cytology, Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, SloveniaSchool of Veterinary Medicine and Science, Medical Faculty, University of Nottingham, Sutton, Bonington Campus, Loughborough LE12 5RD, UKCenter for Multidisciplinary Research, Institute of Nuclear Sciences VINCA, University of Belgrade, Mike Petrovića Alasa 12-14, 11351 Vinča, Belgrade, SerbiaCenter for Multidisciplinary Research, Institute of Nuclear Sciences VINCA, University of Belgrade, Mike Petrovića Alasa 12-14, 11351 Vinča, Belgrade, SerbiaDepartment of Anatomy, Histology with Embryology and Cytology, Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, SloveniaDepartment of Anatomy, Histology with Embryology and Cytology, Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, SloveniaThe type 2 dopamine receptor D<sub>2</sub> (D<sub>2</sub>-R), member of the G protein-coupled receptor (GPCR) superfamily, exists in two isoforms, short (D<sub>2S</sub>-R) and long (D<sub>2L</sub>-R). They differ by an additional 29 amino acids (AA) in the third cytoplasmic loop (ICL3) of the D<sub>2L</sub>-R. These isoforms differ in their intracellular localization and trafficking functionality, as D<sub>2L</sub>-R possesses a larger intracellular pool, mostly in the endoplasmic reticulum (ER). This review focuses on the evolutionarily conserved motifs in the ICL3 of the D<sub>2</sub>-R and proteins interacting with the ICL3 of both isoforms, specifically with the 29 AA insert. These motifs might be involved in D<sub>2</sub>-R exit from the ER and have an impact on cell-surface and intracellular localization and, therefore, also play a role in the function of dopamine receptor signaling, ligand binding and possible homo/heterodimerization. Our recent bioinformatic data on potential new interaction partners for the ICL3 of D<sub>2</sub>-Rs are also presented. Both are highly relevant, and have clinical impacts on the pathophysiology of several diseases such as Parkinson’s disease, schizophrenia, Tourette’s syndrome, Huntington’s disease, manic depression, and others, as they are connected to a variety of essential motifs and differences in communication with interaction partners.https://www.mdpi.com/2218-273X/10/10/1355D<sub>2</sub> dopamine receptorintracellular traffickingendoplasmic reticulumretention motifsICL3interacting partners
collection DOAJ
language English
format Article
sources DOAJ
author Kaja Blagotinšek Cokan
Maša Mavri
Catrin Sian Rutland
Sanja Glišić
Milan Senćanski
Milka Vrecl
Valentina Kubale
spellingShingle Kaja Blagotinšek Cokan
Maša Mavri
Catrin Sian Rutland
Sanja Glišić
Milan Senćanski
Milka Vrecl
Valentina Kubale
Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms
Biomolecules
D<sub>2</sub> dopamine receptor
intracellular trafficking
endoplasmic reticulum
retention motifs
ICL3
interacting partners
author_facet Kaja Blagotinšek Cokan
Maša Mavri
Catrin Sian Rutland
Sanja Glišić
Milan Senćanski
Milka Vrecl
Valentina Kubale
author_sort Kaja Blagotinšek Cokan
title Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms
title_short Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms
title_full Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms
title_fullStr Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms
title_full_unstemmed Critical Impact of Different Conserved Endoplasmic Retention Motifs and Dopamine Receptor Interacting Proteins (DRIPs) on Intracellular Localization and Trafficking of the D<sub>2</sub> Dopamine Receptor (D<sub>2</sub>-R) Isoforms
title_sort critical impact of different conserved endoplasmic retention motifs and dopamine receptor interacting proteins (drips) on intracellular localization and trafficking of the d<sub>2</sub> dopamine receptor (d<sub>2</sub>-r) isoforms
publisher MDPI AG
series Biomolecules
issn 2218-273X
publishDate 2020-09-01
description The type 2 dopamine receptor D<sub>2</sub> (D<sub>2</sub>-R), member of the G protein-coupled receptor (GPCR) superfamily, exists in two isoforms, short (D<sub>2S</sub>-R) and long (D<sub>2L</sub>-R). They differ by an additional 29 amino acids (AA) in the third cytoplasmic loop (ICL3) of the D<sub>2L</sub>-R. These isoforms differ in their intracellular localization and trafficking functionality, as D<sub>2L</sub>-R possesses a larger intracellular pool, mostly in the endoplasmic reticulum (ER). This review focuses on the evolutionarily conserved motifs in the ICL3 of the D<sub>2</sub>-R and proteins interacting with the ICL3 of both isoforms, specifically with the 29 AA insert. These motifs might be involved in D<sub>2</sub>-R exit from the ER and have an impact on cell-surface and intracellular localization and, therefore, also play a role in the function of dopamine receptor signaling, ligand binding and possible homo/heterodimerization. Our recent bioinformatic data on potential new interaction partners for the ICL3 of D<sub>2</sub>-Rs are also presented. Both are highly relevant, and have clinical impacts on the pathophysiology of several diseases such as Parkinson’s disease, schizophrenia, Tourette’s syndrome, Huntington’s disease, manic depression, and others, as they are connected to a variety of essential motifs and differences in communication with interaction partners.
topic D<sub>2</sub> dopamine receptor
intracellular trafficking
endoplasmic reticulum
retention motifs
ICL3
interacting partners
url https://www.mdpi.com/2218-273X/10/10/1355
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