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Mini-Reviews in Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 1389-5575
ISSN (Online): 1875-5607

Attachment of Rod-Like (BAR) Proteins and Membrane Shape

Author(s): D. Kabaso, E. Gongadze, P. Elter, U. van Rienen, J. Gimsa, V. Kralj-Iglic and A. Iglic

Volume 11, Issue 4, 2011

Page: [272 - 282] Pages: 11

DOI: 10.2174/138955711795305353

open access plus

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


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