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    Biochim Biophys Acta. 2011 Oct;1808(10):2374-89. doi: 10.1016/j.bbamem.2011.06.021. Epub 2011 Jul 5.

    Self-directed assembly and clustering of the cytoplasmic domains of inwardly rectifying Kir2.1 potassium channels on association with PSD-95.

    Fomina S, Howard TD, Sleator OK, Golovanova M, O'Ryan L, Leyland ML, Grossmann JG, Collins RF, Prince SM.

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    University of Manchester, Manchester Interdisciplinary Biocentre, Manchester M1 7DN, UK.

    Abstract

    The interaction of the extra-membranous domain of tetrameric inwardly rectifying Kir2.1 ion channels (Kir2.1NC(4)) with the membrane associated guanylate kinase protein PSD-95 has been studied using Transmission Electron Microscopy in negative stain. Three types of complexes were observed in electron micrographs corresponding to a 1:1 complex, a large self-enclosed tetrad complex and extended chains of linked channel domains. Using models derived from small angle X-ray scattering experiments in which high resolution structures from X-ray crystallographic and Nuclear Magnetic Resonance studies are positioned, the envelopes from single particle analysis can be resolved as a Kir2.1NC(4):PSD-95 complex and a tetrad of this unit (Kir2.1NC(4):PSD-95)(4). The tetrad complex shows the close association of the Kir2.1 cytoplasmic domains and the influence of PSD-95 mediated self-assembly on the clustering of these channels.

    Copyright © 2011 Elsevier B.V. All rights reserved.

    PMID:
    21756874
    [PubMed - indexed for MEDLINE]

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