Cooperativity between individual transporter protomers: new data fuelling old complexes.

Neurotransmitter transporters are arranged in an oligomeric quaternary structure as evidenced by crosslinking or fluorescence resonance energy transfer (FRET)-microscopy. In a study by Zhen and colleagues highlighted by this Editorial in the current issue of Journal of Neurochemistry, the combination of mutant and wild-type dopamine transporter (DAT) has been used to establish the cooperation between transporter protomers; the DAT mutant version has an altered affinity for the radiolabelled inhibitor [³H]CFT. Zhen and colleagues predict how saturation-binding curves ought to look, if the two binding sites (i.e. of the wild type and the mutant DAT) operated independently. The results are clear-cut: the experimental observations are inconsistent with curves obtained by mixing independent binding sites. Thus, by definition, the binding sites cooperate. Read the full article 'Dopamine transporter oligomerization: impact of combining protomers with differential cocaine analog binding affinities' on page 167. © 2015 International Society for Neurochemistry.

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Harald H Sitte, Gerhard J Schütz, Michael Freissmuth. Cooperativity between individual transporter protomers: new data fuelling old complexes. Journal of neurochemistry. 2015 Apr;133(2):163-6

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PMID: 25772534

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