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Mini-Reviews in Medicinal Chemistry

Volume 11 Issue 4
ISSN: 1389-5575
eISSN: 1875-5607

 

   All Titles

  Attachment of Rod-Like (BAR) Proteins and Membrane Shape
  pp.272-282 (11) Authors: D. Kabaso, E. Gongadze, P. Elter, U. van Rienen, J. Gimsa, V. Kralj-Iglic, A. Iglic
 
 
      Abstract

Previous studies have shown that cellular function depends on rod-like membrane proteins, among them Bin/Amphiphysin/Rvs (BAR) proteins may curve the membrane leading to physiologically important membrane invaginations and membrane protrusions. The membrane shaping induced by BAR proteins has a major role in various biological processes such as cell motility and cell growth. Different models of binding of BAR domains to the lipid bilayer are described. The binding includes hydrophobic insertion loops and electrostatic interactions between basic amino acids at the concave region of the BAR domain and negatively charged lipids. To shed light on the elusive binding dynamics, a novel experiment is proposed to expand the technique of single-molecule AFM for the traction of binding energy of a single BAR domain.

 
  Keywords: AFM, attachment dynamics, curvature membrane proteins, membrane shape, rod-like, BAR, membrane invaginations, membrane protrusions, cell motility, cell growth, hydrophobic insertion loops, electrostatic interactions, BAR domain, binding energy
  Affiliation: Laboratory of Physics, Faculty of Electrical Engineering, University of Ljubljana, Trzaska 25, SI-1000 Ljubljana, Slovenia.
 
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