Shape matters in protein mobility within membranes

Proc Natl Acad Sci U S A. 2014 Apr 8;111(14):5083-7. doi: 10.1073/pnas.1321054111. Epub 2014 Mar 24.

Abstract

The lateral mobility of proteins within cell membranes is usually thought to be dependent on their size and modulated by local heterogeneities of the membrane. Experiments using single-particle tracking on reconstituted membranes demonstrate that protein diffusion is significantly influenced by the interplay of membrane curvature, membrane tension, and protein shape. We find that the curvature-coupled voltage-gated potassium channel (KvAP) undergoes a significant increase in protein mobility under tension, whereas the mobility of the curvature-neutral water channel aquaporin 0 (AQP0) is insensitive to it. Such observations are well explained in terms of an effective friction coefficient of the protein induced by the local membrane deformation.

Keywords: Brownian motion; Saffman–Delbrück; drag force; internal membrane structure; micropipette aspiration.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aquaporins / metabolism
  • Cell Shape*
  • Eye Proteins / metabolism
  • Lipid Bilayers
  • Membrane Proteins / metabolism*
  • Potassium Channels, Voltage-Gated / metabolism
  • Protein Transport

Substances

  • Aquaporins
  • Eye Proteins
  • Lipid Bilayers
  • Membrane Proteins
  • Potassium Channels, Voltage-Gated
  • aquaporin 0