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Molecular Pharmacology

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Research ArticleArticle

Identification of RanBP 9/10 as Interacting Partners for Protein Kinase C (PKC) γ/δ and the D1 Dopamine Receptor: Regulation of PKC-Mediated Receptor Phosphorylation

Elizabeth B. Rex, Michele L. Rankin, Yu Yang, Quansheng Lu, Charles R. Gerfen, Pedro A. Jose and David R. Sibley
Molecular Pharmacology July 2010, 78 (1) 69-80; DOI: https://doi.org/10.1124/mol.110.063727
Elizabeth B. Rex
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Michele L. Rankin
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Yu Yang
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Quansheng Lu
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Charles R. Gerfen
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Pedro A. Jose
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David R. Sibley
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Abstract

We reported previously that ethanol treatment regulates D1 receptor phosphorylation and signaling in a protein kinase C (PKC) δ- and PKCγ-dependent fashion by a mechanism that may involve PKC isozyme-specific interacting proteins. Using a PKC isozyme-specific coimmunoprecipitation approach coupled to mass spectrometry, we report the identification of RanBP9 and RanBP10 as novel interacting proteins for both PKCγ and PKCδ. Both RanBP9 and RanBP10 were found to specifically coimmunoprecipitate with both PKCγ and PKCδ; however, this association did not seem to mediate the ethanol regulation of the PKCs. It is noteworthy that the D1 receptor was also found to specifically coimmunoprecipitate with RanBP9/10 from human embryonic kidney (HEK) 293T cells and with endogenous RanBP9 from rat kidney. RanBP9 and RanBP10 were also found to colocalize at the cellular level with the D1 receptor in both kidney and brain tissue. Although overexpression of RanBP9 or RanBP10 in HEK293T cells did not seem to alter the kinase activities of either PKCδ or PKCγ, both RanBP proteins regulated D1 receptor phosphorylation, signaling, and, in the case of RanBP9, expression. Specifically, overexpression of either RanBP9 or RanBP10 enhanced basal D1 receptor phosphorylation, which was associated with attenuation of D1 receptor-stimulated cAMP accumulation. Moreover, treatment of cells with select PKC inhibitors blocked the RanBP9/10-dependent increase in basal receptor phosphorylation, suggesting that phosphorylation of the receptor by PKC is regulated by RanBP9/10. These data support the idea that RanBP9 and RanBP10 may function as signaling integrators and dictate the efficient regulation of D1 receptor signaling by PKCδ and PKCγ.

Footnotes

  • ↵Embedded Image The online version of this article (available at http://molpharm.aspetjournals.org) contains supplemental material.

  • This research was supported by the National Institutes of Health National Heart, Lung, and Blood Institute [Grants R37-HL023081, P01-HL074940, P01-HL068686, R01-HL092196]; the National Institutes of Health National Institute of Diabetes and Digestive and Kidney Diseases [R01-DK039308]; and Intramural Research funds from the National Institutes of Health National Institute of Neurological Disorders and Stroke and the National Institutes of Health National Institute of Mental Health.

  • Article, publication date, and citation information can be found at http://molpharm.aspetjournals.org.

    doi:10.1124/mol.110.063727.

  • ABBREVIATIONS:

    PKC
    protein kinase C
    PKA
    protein kinase A
    GPCR
    G protein-coupled receptor
    HEK
    human embryonic kidney
    DA
    dopamine
    GFP
    green fluorescent protein
    PAGE
    polyacrylamide gel electrophoresis
    DMEM
    Dulbecco's modified essential medium
    FBS
    fetal bovine serum
    PVDF
    polyvinylidene difluoride
    EtOH
    ethanol
    mGluR
    metabotropic glutamate receptor
    MOR
    μ-opioid receptor
    GRK
    G protein-coupled receptor kinase
    PBS
    phosphate-buffered saline
    HA
    hemagglutinin
    MOPS
    3-(N-morpholino)propanesulfonic acid
    DAG
    diacylglycerol
    PS
    phosphatidyl serine
    coIP
    coimmunoprecipitation
    D1R
    dopamine 1 receptor
    EGFP
    enhanced green fluorescent protein
    Hsp-70
    70-kDa heat shock protein
    ERK
    extracellular signal-regulated kinase
    PICK1
    protein interacting with C kinase 1
    RACK
    receptor for activated C kinase
    SCH23390
    R-(+)-7-chloro-8-hydroxy-3-methyl-1-phenyl-2,3,4,5-tetrahydro-1H-3-benzazepine
    Gö6976
    12-(2-cyanoethyl)-6,7,12,13-tetrahydro-13-methyl-5-oxo-5H-indolo(2,3-a)pyrrolo(3,4-c)-carbazole
    Gö6983
    3-[1-[3-(dimethylamino)propyl]-5-methoxy-1H-indol-3-yl]-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dione
    Ro 20-1724
    4-[3-butoxy-4-methoxyphenyl)-methyl]-2-imidazolidinone.

  • Received January 22, 2010.
  • Accepted April 15, 2010.
  • U.S. Government work not protected by U.S. copyright
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Molecular Pharmacology: 78 (1)
Molecular Pharmacology
Vol. 78, Issue 1
1 Jul 2010
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Research ArticleArticle

Identification of RanBP 9/10 as Interacting Partners for Protein Kinase C (PKC) γ/δ and the D1 Dopamine Receptor: Regulation of PKC-Mediated Receptor Phosphorylation

Elizabeth B. Rex, Michele L. Rankin, Yu Yang, Quansheng Lu, Charles R. Gerfen, Pedro A. Jose and David R. Sibley
Molecular Pharmacology July 1, 2010, 78 (1) 69-80; DOI: https://doi.org/10.1124/mol.110.063727

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Research ArticleArticle

Identification of RanBP 9/10 as Interacting Partners for Protein Kinase C (PKC) γ/δ and the D1 Dopamine Receptor: Regulation of PKC-Mediated Receptor Phosphorylation

Elizabeth B. Rex, Michele L. Rankin, Yu Yang, Quansheng Lu, Charles R. Gerfen, Pedro A. Jose and David R. Sibley
Molecular Pharmacology July 1, 2010, 78 (1) 69-80; DOI: https://doi.org/10.1124/mol.110.063727
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