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J Biol Chem, Vol. 274, Issue 50, 35794-35801, December 10, 1999
From the The dopamine transporter plays an essential role
in the modulation of dopaminergic neurotransmission by mediating the
reuptake of dopamine into presynaptic neurons. In cells expressing the dopamine transporter, activation of protein kinase C by phorbol esters
results in a significant reduction in dopamine uptake. This phorbol
ester-mediated inhibition of dopamine transport is associated with a
decrease in Vmax, although the apparent
affinity of the transporter for dopamine remains unchanged. Using a
green fluorescent protein-tagged dopamine transporter stably expressed in Madin-Darby canine kidney cells, we show in live cells that the
decrease in transporter activity is caused by the rapid internalization of carriers from the plasma membrane. This redistribution of the transporter is specific to phorbol ester activation and is unaffected by the presence of either substrates or inhibitors of the carrier. Upon
the addition of phorbol esters, transporters at the cell surface are
rapidly endocytosed through a clathrin-mediated and dynamin-dependent mechanism into early endosomes, where
they colocalize with transferrin. The internalized carrier is targeted
to the endosomal/lysosomal pathway and is completely degraded within 2 h of protein kinase C activation. Phorbol ester-mediated
alterations in the trafficking of the dopamine transporter may serve as
a mechanism for controlling extracellular dopamine levels in the central nervous system.
Regulated Trafficking of the Human Dopamine Transporter
CLATHRIN-MEDIATED INTERNALIZATION AND LYSOSOMAL DEGRADATION IN
RESPONSE TO PHORBOL ESTERS*
§ and§¶
Department of Cell and Developmental
Biology, ¶ Howard Hughes Medical Institute, and the
§ Vollum Institute, Oregon Health Science University,
Portland, Oregon 97201
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: 3181 S. W. Sam Jackson Park Rd. L-474, Portland, OR 97201-3098. Tel.:
503-494-6723; Fax: 503-494-8230; E-mail: amaras@ohsu.edu.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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