title: Cooperativity between individual transporter protomers: new data fuelling old complexes.
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.
authors.affiliation: Center for Physiology and Pharmacology, Institute of Pharmacology, Medical University Vienna, Vienna, Austria.
authors.forename: Harald H
authors.initials: HH
authors.lastname: Sitte
authors.forename: Gerhard J
authors.initials: GJ
authors.lastname: Schütz
authors.forename: Michael
authors.initials: M
authors.lastname: Freissmuth
mesh_terms: D000818:Animals; D009154:Mutation; D050479:Neurotransmitter Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism*
chemical_list: D050479:Neurotransmitter Transport Proteins; D021122:Protein Subunits