title: Attachment of rod-like (BAR) proteins and membrane shape.
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.
authors.affiliation: Laboratory of Physics, Faculty of Electrical Engineering, University of Ljubljana, Tržaška 25, SI-1000 Ljubljana, Slovenia. doron.kabaso@fe.uni-lj.si
authors.forename: D
authors.initials: D
authors.lastname: Kabaso
authors.forename: E
authors.initials: E
authors.lastname: Gongadze
authors.forename: P
authors.initials: P
authors.lastname: Elter
authors.forename: U
authors.initials: U
authors.lastname: van Rienen
authors.forename: J
authors.initials: J
authors.lastname: Gimsa
authors.forename: V
authors.initials: V
authors.lastname: Kralj-Iglič
authors.forename: A
authors.initials: A
authors.lastname: Iglič
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry; D022081:Cell Surface Extensions / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D008051:Lipid Bilayers; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C075637:amphiphysin