Ras nanoclusters: molecular structure and assembly.
H-, N- and K-ras4B are lipid-anchored, peripheral membrane guanine nucleotide binding proteins. Recent work has shown that Ras proteins are laterally segregated into non-overlapping, dynamic domains of the plasma membrane called nanoclusters. This lateral segregation is important to specify Ras interactions with membrane-associated proteins, effectors and scaffolding proteins and is critical for Ras signal transduction. Here we review biological, in vitro and structural data that provide insight into the molecular basis of how palmitoylated Ras proteins are anchored to the plasma membrane. We explore possible mechanisms for how the interactions of H-ras with a lipid bilayer may drive nanocluster formation.
Abankwa
Daniel
D
Institute for Molecular Bioscience, University of Queensland, Brisbane 4072, Australia.
Gorfe
Alemayehu A
AA
Hancock
John F
JF
D001665:Binding Sites; D002462:Cell Membrane / Q000737:chemistry* / Q000502:physiology; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D008051:Lipid Bilayers / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D021962:Membrane Microdomains / Q000737:chemistry* / Q000502:physiology; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D018631:ras Proteins / Q000737:chemistry* / Q000502:physiology
D008051:Lipid Bilayers; D018631:ras Proteins