MolPharm xPharm- The Comprehensive Pharmacology Reference

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


Molecular Pharmacology Fast Forward
First published on February 28, 2007; DOI: 10.1124/mol.107.035493


0026-895X/07/7105-1206-1208$20.00
Mol Pharmacol 71:1206-1208, 2007

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Related Article
Right arrow All Versions of this Article:
mol.107.035493v1
71/5/1206    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Related articles in MolPharm
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Blakely, R. D.
Right arrow Articles by DeFelice, L. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Blakely, R. D.
Right arrow Articles by DeFelice, L. J.
Perspective

All Aglow about Presynaptic Receptor Regulation of Neurotransmitter Transporters

Randy D. Blakely, and Louis J. DeFelice

Departments of Pharmacology (R.D.B., L.J.D.) and Psychiatry (R.D.B.), and Center for Molecular Neuroscience (R.D.B., L.J.D.), Vanderbilt University School of Medicine, Nashville, Tennessee

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 D2 receptors regulate DATs.


Received February 26, 2007; accepted February 27, 2007

Address correspondence to: Dr. Randy D. Blakely, Allan D. Bass Professor of Pharmacology & Psychiatry, Director, Vanderbilt Center for Molecular Neuroscience, Nashville, TN 37232-8548. E-mail: randy.blakely{at}vanderbilt.edu


Related articles in MolPharm:

D2 Receptors Regulate Dopamine Transporter Function via an Extracellular Signal-Regulated Kinases 1 and 2-Dependent and Phosphoinositide 3 Kinase-Independent Mechanism
Elizabeth A. Bolan, Bronwyn Kivell, Vanaja Jaligam, Murat Oz, Lankupalle D. Jayanthi, Yang Han, Namita Sen, Eneki Urizar, Ivone Gomes, Lakshmi A. Devi, Sammanda Ramamoorthy, Jonathan A. Javitch, Agustin Zapata, and Toni S. Shippenberg
MolPharm 2007 71: 1222-1232. [Abstract] [Full Text]  






Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
All ASPET Journals Molecular Pharmacology Pharmacological Reviews
 Molecular Interventions Drug Metabolism and Disposition

Copyright © 2007 by the American Society for Pharmacology and Experimental Therapeutics