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Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein. / Marion, S; Urs, NM; Peterson, SM; Sotnikova, TD; Beaulieu, JM; Gainetdinov, RR; Caron, MG.

In: Journal of Biological Chemistry, 2014.

Research output: Contribution to journalArticle

Harvard

Marion, S, Urs, NM, Peterson, SM, Sotnikova, TD, Beaulieu, JM, Gainetdinov, RR & Caron, MG 2014, 'Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein.', Journal of Biological Chemistry.

APA

Marion, S., Urs, NM., Peterson, SM., Sotnikova, TD., Beaulieu, JM., Gainetdinov, RR., & Caron, MG. (2014). Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein. Journal of Biological Chemistry.

Vancouver

Marion S, Urs NM, Peterson SM, Sotnikova TD, Beaulieu JM, Gainetdinov RR et al. Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein. Journal of Biological Chemistry. 2014.

Author

Marion, S ; Urs, NM ; Peterson, SM ; Sotnikova, TD ; Beaulieu, JM ; Gainetdinov, RR ; Caron, MG. / Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein. In: Journal of Biological Chemistry. 2014.

BibTeX

@article{47dee1a3f9dc44ad9c568ee270ecfe66,
title = "Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein.",
abstract = "Striatal dopamine D2 receptor (D2R) relies upon G protein- and β-arrestin-dependent signaling pathways to convey its action on motor control and behavior. Considering that D2R activation inhibits Akt in the striatum and that huntingtin physiological functions are affected by Akt phosphorylation, we sought to investigate whether D2R-mediated signaling could regulate huntingtin phosphorylation. We demonstrate that D2R activation decreases huntingtin phosphorylation on its Akt site. This dephosphorylation event depends upon the Gαi-dependent engagement of specific members of the protein phosphatase metallo-dependent (PPM/PP2C) family and is independent of β-arrestin 2. These observations identify the PPM/PP2C family as a mediator of G protein-coupled receptor signaling and thereby suggest a novel mechanism of dopaminergic signaling.",
keywords = "Akt, Arrestin, Dopamine D2 Receptor, Dopamine Receptors, G Protein-coupled Receptors (GPCR), G Proteins, Huntingtin, PP2C, Phosphatase",
author = "S Marion and NM Urs and SM Peterson and TD Sotnikova and JM Beaulieu and RR Gainetdinov and MG. Caron",
year = "2014",
language = "не определен",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",

}

RIS

TY - JOUR

T1 - Dopamine D2 receptor relies upon PPM/PP2C protein phosphatases to dephosphorylate huntingtin protein.

AU - Marion, S

AU - Urs, NM

AU - Peterson, SM

AU - Sotnikova, TD

AU - Beaulieu, JM

AU - Gainetdinov, RR

AU - Caron, MG.

PY - 2014

Y1 - 2014

N2 - Striatal dopamine D2 receptor (D2R) relies upon G protein- and β-arrestin-dependent signaling pathways to convey its action on motor control and behavior. Considering that D2R activation inhibits Akt in the striatum and that huntingtin physiological functions are affected by Akt phosphorylation, we sought to investigate whether D2R-mediated signaling could regulate huntingtin phosphorylation. We demonstrate that D2R activation decreases huntingtin phosphorylation on its Akt site. This dephosphorylation event depends upon the Gαi-dependent engagement of specific members of the protein phosphatase metallo-dependent (PPM/PP2C) family and is independent of β-arrestin 2. These observations identify the PPM/PP2C family as a mediator of G protein-coupled receptor signaling and thereby suggest a novel mechanism of dopaminergic signaling.

AB - Striatal dopamine D2 receptor (D2R) relies upon G protein- and β-arrestin-dependent signaling pathways to convey its action on motor control and behavior. Considering that D2R activation inhibits Akt in the striatum and that huntingtin physiological functions are affected by Akt phosphorylation, we sought to investigate whether D2R-mediated signaling could regulate huntingtin phosphorylation. We demonstrate that D2R activation decreases huntingtin phosphorylation on its Akt site. This dephosphorylation event depends upon the Gαi-dependent engagement of specific members of the protein phosphatase metallo-dependent (PPM/PP2C) family and is independent of β-arrestin 2. These observations identify the PPM/PP2C family as a mediator of G protein-coupled receptor signaling and thereby suggest a novel mechanism of dopaminergic signaling.

KW - Akt

KW - Arrestin

KW - Dopamine D2 Receptor

KW - Dopamine Receptors

KW - G Protein-coupled Receptors (GPCR)

KW - G Proteins

KW - Huntingtin

KW - PP2C

KW - Phosphatase

M3 - статья

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -

ID: 5835623