Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 11 September 2007
Vol. 2007, Issue 403, p. tw326
[DOI: 10.1126/stke.4032007tw326]


Neurotransmitter Transport The Molecular Machinery of Mood Swings

Gilbert Chin

Science, AAAS, Washington, DC 20005, USA

The action of monoamine neurotransmitters that serve as signaling molecules in mood and motivation begins when they are released from the presynaptic nerve terminal and ends when they are transported from the extracellular space back into the cytoplasm via dedicated sodium-dependent plasma membrane transporters. Zhou et al. describe the crystal structure of a bacterial homolog (LeuT) of the mammalian monoamine transporters in complex with its substrate (leucine) and an inhibitor of norepinephrine transport (the antidepressant desipramine). On the basis of homology modeling of the human transporters for serotonin, norepinephrine, and dopamine (hSERT, hNET, and hDAT), they construct mutants of hSERT and hDAT and show that these exhibit the predicted sensitivity of serotonin and dopamine uptake to desipramine inhibition.

Z. Zhou, J. Zhen, N. K. Karpowich, R. M. Goetz, C. J. Law, M. E. A. Reith, D.-N. Wang, LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake. Science 317, 1390-1393 (2007). [Abstract] [Full Text]

Citation: G. Chin, The Molecular Machinery of Mood Swings. Sci. STKE 2007, tw326 (2007).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882