Cooperativity between individual transporter protomers: new data fuelling old complexes

Journal of Neurochemistry
H H SitteMichael Freissmuth

Abstract

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.

References

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Dec 30, 2014·Trends in Pharmacological Sciences·Harald H Sitte, Michael Freissmuth

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Citations

Jan 26, 2017·The Journal of Physical Chemistry. B·Mert GurIvet Bahar
Jan 20, 2017·Nature Communications·Andreas AnderluhGerhard J Schütz
Jun 7, 2017·The Journal of Biological Chemistry·Mary Hongying ChengIvet Bahar

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