Influence of the lipidation motif on the partitioning and association of N-ras in model membrane subdomains

  • Weise, K.
  • Triola, G.
  • Brunsveld, L.
  • Waldmann, H.
  • Winter, R.
Publication date
January 2009

Abstract

In a combined chemical biological and biophysical approach using time-lapse tapping-mode atomic force microscopy, we studied the partitioning of differently lipidated N-Ras proteins with various membrane-localization motifs into lipid domains of canonical model raft mixtures. The results provide direct evidence that partitioning of N-Ras occurs preferentially into liquid-disordered lipid domains, independent of the lipid anchor system. N-Ras proteins bearing at least one farnesyl group have a comparable membrane partitioning behavior and show diffusion of the protein into the liquid-disordered/liquid-ordered phase boundary region, thus leading to a decrease of the unfavorable line tension between domains. In addition, except for the monofar...

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