Ras nanoclusters: Molecular structure and assembly

Daniel Abankwa, AA Gorfe, JF Hancock

Research output: Contribution to journalArticleScientificpeer-review

94 Citations (Scopus)

Abstract

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. (C) 2007 Elsevier Ltd. All rights reserved.
Original languageUndefined/Unknown
Pages (from-to)599–607
Number of pages9
JournalSeminars in Cell and Developmental Biology
Volume18
Issue number5
DOIs
Publication statusPublished - 2007
MoE publication typeA1 Journal article-refereed

Keywords

  • lipid-raft
  • MD simulations
  • nanocluster
  • Ras
  • structure

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