Conventional protein kinase C isoforms regulate human dopamine transporter activity in Xenopus oocytes

FEBS Letters

Doolen, Suzanne¹  Zahniser, Nancy R¹ 

[1] Department of Pharmacology and Neuroscience Program, C-236, University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, CO 80262, USA

关键词: Electrophysiology;    Neurotransmitter;    Transporter regulation;    Trafficking;    BIS;    bisindolylmaleimide;    cPKC;    conventional PKC;    DA;    dopamine;    DAT;    DA transporter;    EGTA;    ethylenebis(oxyethylenenitrilo)tetraacetic acid;    FRB;    frog Ringer's buffer;    GABA;    γ-aminobutyric acid;    hDAT;    human DAT;    PKC;    protein kinase C;    nPKC;    novel PKC;    PMA;    β-phorbol 12-myristate 13-acetate;    RACK;    receptors for activated C kinase;   

DOI  :  10.1016/S0014-5793(02)02554-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The hypothesis that specific protein kinase C (PKC) isoforms regulate dopamine transporter (DAT) function was tested in Xenopus laevis oocytes expressing human (h)DAT. Activation of conventional PKCs (cPKCs) and novel PKCs (nPKCs) using 10 nM phorbol 12-myristate 13-acetate (PMA) significantly inhibited DAT-associated transport currents. This effect was reversed by isoform-non-selective PKC inhibitors, selective inhibitors of cPKCs and δPKC, and by Ca²⁺ chelation. By contrast, the ϵPKC translocation inhibitor peptide had no effect on PMA-induced inhibition of hDAT transport-associated currents. Thus, the primary mechanism by which PMA regulates hDAT expressed in oocytes appears to be by activating cPKC(s).

【 授权许可】

Unknown