Structural characteristics of BAR domain superfamily to sculpt the membrane

Semin Cell Dev Biol. 2010 Jun;21(4):391-8. doi: 10.1016/j.semcdb.2010.01.010. Epub 2010 Jan 18.

Abstract

Membrane dynamics is an essential process for cell locomotion, cytokinesis, vesicular transport and organelle morphogenesis. Formation of tubes or buds from a nearly flat membrane is a widely spread feature of the membrane shape changes. The BAR (Bin/Amphiphysin/Rvs-homology) domain dimers exhibit long extended curved shapes and appear to be outstandingly suitable modules for this purpose. So far, crystal structures of 18 independent BAR domains including inverse-BAR domains and FCH-BAR domains have been reported. These atomic models show a vast variation of dimer shapes on a common and simple basic framework. Comparison of the structural variations with respect to differences in membrane sculpting properties provide useful clues about the mechanisms for modifying the framework into a particular dimer that generates and/or senses a distinct curvature set of the membrane.

Publication types

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

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Adaptor Proteins, Signal Transducing / genetics
  • Amino Acid Sequence
  • Animals
  • Cell Membrane* / chemistry
  • Cell Membrane* / ultrastructure
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Protein Multimerization
  • Protein Structure, Quaternary
  • Protein Structure, Secondary*
  • Protein Structure, Tertiary*

Substances

  • Adaptor Proteins, Signal Transducing
  • Nerve Tissue Proteins
  • amphiphysin