All aglow about presynaptic receptor regulation of neurotransmitter transporters.

Blakely RD, DeFelice LJ
Mol Pharmacol. 2007 71 (5): 1206-8

PMID: 17329498 · DOI:10.1124/mol.107.035493

Mounting evidence supports the idea that neurotransmitter transporters are subject to many forms of post-translational regulation typically associated with receptors and ion channels, including receptor and kinase-mediated changes in transporter phosphorylation, cell surface trafficking, and/or catalytic activation. Although hints of this regulation can be achieved with traditional radiolabeled substrate flux techniques, higher resolution methods are needed that can localize transporter function in situ as well as permit real-time monitoring of transport function without confounds associated with coincident receptor activation. The elegant study by Bolan et al. (p. 1222) capitalizes on the fluorescent properties of a recently introduced substrate for the dopamine (DA) transporter (DAT), termed 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP+), to illuminate a pertussis toxin-sensitive, extracellular signal-regulated kinase (ERK1/2)-dependent pathway by which presynaptic DA D(2) receptors regulate DATs.

MeSH Terms (6)

Extracellular Signal-Regulated MAP Kinases Humans Neurotransmitter Transport Proteins Pyridinium Compounds Receptors, Presynaptic Spectrometry, Fluorescence

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