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Cooperativity between individual transporter protomers: new data fuelling old complexes.
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- Author(s): Sitte HH;Sitte HH; Schütz GJ; Freissmuth M
- Source:
Journal of neurochemistry [J Neurochem] 2015 Apr; Vol. 133 (2), pp. 163-6. Date of Electronic Publication: 2015 Mar 15.
- Publication Type:
Editorial; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Wiley on behalf of the International Society for Neurochemistry Country of Publication: England NLM ID: 2985190R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1471-4159 (Electronic) Linking ISSN: 00223042 NLM ISO Abbreviation: J Neurochem Subsets: MEDLINE
- Publication Information:
Publication: 2001- : Oxford, UK : Wiley on behalf of the International Society for Neurochemistry
Original Publication: New York : Raven Press
- Subject Terms:
- 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.
(© 2015 International Society for Neurochemistry.)
- Accession Number:
0 (Neurotransmitter Transport Proteins)
0 (Protein Subunits)
- Publication Date:
Date Created: 20150317 Date Completed: 20150612 Latest Revision: 20150410
- Publication Date:
20221213
- Accession Number:
10.1111/jnc.13086
- Accession Number:
25772534
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