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Titolo:
Regulated trafficking of the human dopamine transporter - Clathrin-mediated internalization and lysosomal degradation in response to phorbol esters
Autore:
Daniels, GM; Amara, SG;
Indirizzi:
Oregon Hlth Sci Univ, Dept Cell & Dev Biol, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 v Biol, Portland, OR 97201 USA Oregon Hlth Sci Univ, Howard Hughes Med Inst, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 d Inst, Portland, OR 97201 USA Oregon Hlth Sci Univ, Vollum Inst, Portland, OR 97201 USA Oregon Hlth Sci Univ Portland OR USA 97201 m Inst, Portland, OR 97201 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 50, volume: 274, anno: 1999,
pagine: 35794 - 35801
SICI:
0021-9258(199912)274:50<35794:RTOTHD>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; CELL-SURFACE EXPRESSION; DOWN-REGULATION; FUNCTIONAL REGULATION; NOREPINEPHRINE TRANSPORTER; RECEPTOR INTERNALIZATION; STRIATAL SYNAPTOSOMES; DILEUCINE MOTIF; XENOPUS-OOCYTES; COATED PITS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Amara, SG 3181 SW Sam Jackson Pk Rd L-474, Portland, OR 97201 USA 3181 SWSam Jackson Pk Rd L-474 Portland OR USA 97201 97201 USA
Citazione:
G.M. Daniels e S.G. Amara, "Regulated trafficking of the human dopamine transporter - Clathrin-mediated internalization and lysosomal degradation in response to phorbol esters", J BIOL CHEM, 274(50), 1999, pp. 35794-35801

Abstract

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 ofprotein 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 V-max 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.

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Documento generato il 29/09/20 alle ore 23:51:34