Calmodulin kinase II interacts with the dopamine transporter C terminus to regulate amphetamine-induced reverse transport

Research output: Contribution to journalJournal articleResearchpeer-review

  • Jacob U Fog
  • Habibeh Khoshbouei
  • Marion Holy
  • William A Owens
  • Christian Bjerggaard Vaegter
  • Namita Sen
  • Yelyzaveta Nikandrova
  • Erica Bowton
  • Douglas G McMahon
  • Roger J Colbran
  • Lynette C Daws
  • Harald H Sitte
  • Jonathan A Javitch
  • Aurelio Galli
  • Gether, Ulrik
Efflux of dopamine through the dopamine transporter (DAT) is critical for the psychostimulatory properties of amphetamines, but the underlying mechanism is unclear. Here we show that Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) plays a key role in this efflux. CaMKIIalpha bound to the distal C terminus of DAT and colocalized with DAT in dopaminergic neurons. CaMKIIalpha stimulated dopamine efflux via DAT in response to amphetamine in heterologous cells and in dopaminergic neurons. CaMKIIalpha phosphorylated serines in the distal N terminus of DAT in vitro, and mutation of these serines eliminated the stimulatory effects of CaMKIIalpha. A mutation of the DAT C terminus impairing CaMKIIalpha binding also impaired amphetamine-induced dopamine efflux. An in vivo role for CaMKII was supported by chronoamperometry measurements showing reduced amphetamine-induced dopamine efflux in response to the CaMKII inhibitor KN93. Our data suggest that CaMKIIalpha binding to the DAT C terminus facilitates phosphorylation of the DAT N terminus and mediates amphetamine-induced dopamine efflux.
Original languageEnglish
JournalNeuron
Volume51
Issue number4
Pages (from-to)417-429
Number of pages13
ISSN0896-6273
DOIs
Publication statusPublished - 2006

    Research areas

  • Amphetamines, Animals, Animals, Newborn, Benzylamines, Biological Transport, Blotting, Western, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Calcium-Calmodulin-Dependent Protein Kinases, Cells, Cultured, Central Nervous System Stimulants, Chromatography, High Pressure Liquid, Dopamine, Dopamine Plasma Membrane Transport Proteins, Enzyme Inhibitors, Humans, Immunohistochemistry, Immunoprecipitation, Membrane Potentials, Mesencephalon, Neurons, Patch-Clamp Techniques, Phosphorylation, Protein Binding, Protein Structure, Tertiary, Rats, Sulfonamides, Transfection

ID: 1200628