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Conventional protein kinase C isoforms regulate human dopamine transporter activity in Xenopus oocytes
Author(s) -
Doolen Suzanne,
Zahniser Nancy R
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02554-1
Subject(s) - xenopus , protein kinase c , gene isoform , dopamine transporter , microbiology and biotechnology , chemistry , protein kinase a , transporter , dopamine , phorbol , phosphorylation , biology , biochemistry , endocrinology , gene
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 Ca 2+ 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).