All aglow about presynaptic receptor regulation of neurotransmitter transporters.
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.
Blakely
Randy D
RD
Department of Pharmacology, Center for Molecular Neuroscience, Vanderbilt University School of Medicine, Nashville, TN 37232-8548, USA. randy.blakely@vanderbilt.edu
DeFelice
Louis J
LJ
D048049:Extracellular Signal-Regulated MAP Kinases / Q000378:metabolism; D006801:Humans; D050479:Neurotransmitter Transport Proteins / Q000378:metabolism*; D011726:Pyridinium Compounds / Q000378:metabolism; D017661:Receptors, Presynaptic / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D050479:Neurotransmitter Transport Proteins; D011726:Pyridinium Compounds; D017661:Receptors, Presynaptic; C052247:4-(4-diethylaminostyryl)-N-methylpyridinium; D048049:Extracellular Signal-Regulated MAP Kinases