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Titolo:
Membrane trafficking regulates the activity of the human dopamine transporter
Autore:
Melikian, HE; Buckley, KM;
Indirizzi:
Harvard Univ, Sch Med, Dept Neurobiol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 ed, Dept Neurobiol, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 18, volume: 19, anno: 1999,
pagine: 7699 - 7710
SICI:
0270-6474(19990915)19:18<7699:MTRTAO>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; HUMAN NOREPINEPHRINE TRANSPORTER; FUNCTIONAL REGULATION; NEUROTRANSMITTER TRANSPORTERS; GABA TRANSPORTER; SEROTONIN TRANSPORTERS; STRIATAL SYNAPTOSOMES; TRANSFERRIN RECEPTOR; SURFACE EXPRESSION; XENOPUS-OOCYTES;
Keywords:
dopamine; endocytosis; trafficking; transporter; regulation; protein kinase C; recycling;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Buckley, KM Harvard Univ, Sch Med, Dept Neurobiol, 220 Longwood Ave, Boston, MA 02115 USA Harvard Univ 220 Longwood Ave Boston MA USA 02115 MA 02115 USA
Citazione:
H.E. Melikian e K.M. Buckley, "Membrane trafficking regulates the activity of the human dopamine transporter", J NEUROSC, 19(18), 1999, pp. 7699-7710

Abstract

The trafficking of synaptic proteins is unquestionably a major determinantof the properties of synaptic transmission. Here, we present a detailed analysis of the downregulation and intracellular trafficking of the cocaine- and amphetamine-sensitive dopamine transporter (DAT), a presynaptic plasma membrane protein responsible for the regulation of extracellular DA concentrations. Using PC12 cells stably transfected with human DAT cDNA, we observe that phorbol ester activation of protein kinase C (PKC) results in decreased transporter capacity and a parallel decrease in the amount of DAT on the cell surface that is attributable to intracellular transporter sequestration. After internalization, DAT diverges to the recycling, as opposed to the degradative, arm of the endocytic pathway. This study demonstrates, for the first time, DAT endocytosis, establishes the pathways through which DAT traffics both at steady state and in response to PKC activation, and suggests that DAT recycling is likely to occur.

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Documento generato il 20/09/20 alle ore 06:50:48