Self-directed assembly and clustering of the cytoplasmic domains of inwardly rectifying Kir2.1 potassium channels on association with PSD-95
- Resource Type
- Article
- Authors
- Fomina, Svetlana; Howard, Tina D.; Sleator, Olivia K.; Golovanova, Marina; O'Ryan, Liam; Leyland, Mark L.; Grossmann, J. Günter; Collins, Richard F.; Prince, Stephen M.
- Source
- BBA: Biomembranes. Oct2011, Vol. 1808 Issue 10, p2374-2389. 16p.
- Subject
- *POTASSIUM channels
*CYTOPLASM
*MOLECULAR self-assembly
*X-ray scattering
*PROTEIN kinases
*MASS spectrometry
*ESCHERICHIA coli
*ELECTRON microscopy
- Language
- ISSN
- 0005-2736
Abstract: 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 (Kir2.1NC4: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 &y& Elsevier]