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

Autor: Svetlana Fomina, Mark L. Leyland, Olivia K. Sleator, Tina D. Howard, Richard F. Collins, Stephen M. Prince, Marina Golovanova, J. Günter Grossmann, Liam O'Ryan
Jazyk: angličtina
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - Biomembranes. (10):2374-2389
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2011.06.021
Popis: 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.
Databáze: OpenAIRE