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

Research output: Contribution to journalArticlepeer-review

  • External authors:
  • Svetlana Fomina
  • Tina D. Howard
  • Olivia K. Sleator
  • Marina Golovanova
  • Liam O'Ryan
  • Mark L. Leyland
  • J. Günter Grossmann
  • Richard F. Collins


The interaction of the extra-membranous domain of tetrameric inwardly rectifying Kir2.1 ion channels (Kir2.1NC4) 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 Kir2.1NC4: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. © 2011 Elsevier B.V. All rights reserved.

Bibliographical metadata

Original languageEnglish
Pages (from-to)2374-2389
Number of pages15
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number10
Publication statusPublished - Oct 2011