BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure

  title={BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure},
  author={Brian Jon Peter and Helen M. Kent and Ian G. Mills and Yvonne Vallis and Peter J Butler and Philip R. Evans and Harvey T. McMahon},
  pages={495 - 499}
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we… 

The crystal structure of the BAR domain from human Bin1/amphiphysin II and its implications for molecular recognition.

The crystal structure of the BAR domain from the human Bin1 protein at 2.0 A resolution is reported and calculations indicate that the Bin1BAR domain contains two potential sites for protein-protein interactions on the convex face of the dimer.

Amphipathic motifs in BAR domains are essential for membrane curvature sensing

BAR (Bin/Amphiphysin/Rvs) domains and amphipathic α‐helices (AHs) are believed to be sensors of membrane curvature thus facilitating the assembly of protein complexes on curved membranes. Here, we

Endophilin BAR domain drives membrane curvature by two newly identified structure‐based mechanisms

It is proposed that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino‐terminal amphipathic helix.

Structural insights into the cooperative remodeling of membranes by amphiphysin/BIN1

This study indicates that the H0 helix and the BAR tip are necessary for efficient and organized self-assembly of amphiphysin/N-BAR.



Amphiphysin 2 (Bin1) and T-Tubule Biogenesis in Muscle

Findings support a role of the bilayer-deforming properties of amphiphysin at T-tubules and, more generally, a physiological role of amphphysin in membrane deformation.

Tuba, a Novel Protein Containing Bin/Amphiphysin/Rvs and Dbl Homology Domains, Links Dynamin to Regulation of the Actin Cytoskeleton*

The properties of Tuba provide new evidence for a close functional link between dynamin, Rho GTPase signaling, and the actin cytoskeleton.

Amphiphysins: Raising the BAR for Synaptic Vesicle Recycling and Membrane Dynamics

Genetic studies reveal pleiotropic functions for amphiphysins in clathrin‐mediated endocytosis and the regulation of membrane dynamics, perhaps through the actin cytoskeleton.

Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis

Results show that amphiphysin binds lipid bilayers, indicate a potential function for amphiphYSin in the changes in bilayer curvature that accompany vesicle budding, and imply a close functional partnership between amphiphisin and dynamin in endocytosis.

A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals.

A specific, SH3 domain-mediated, interaction between amphiphysin and dynamin is demonstrated by gel overlay and affinity chromatography and it is shown that the two proteins are colocalized in nerve terminals and are coprecipitated from brain extracts consistent with their interactions in situ.

Identification and Characterization of a Nerve Terminal-enriched Amphiphysin Isoform*

The characterization of a novel amphiphysin isoform (termed amphiphYSin II) that was identified through a homology search of the data base of expressed sequence tags suggests that amphphysin II may participate with amphiphyn I in the regulation of synaptic vesicle endocytosis.

Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis.

It is proposed that it is an amphiphysin heterodimer that drives the recruitment of dynamin to clathrin-coated pits in endocytosing nerve terminals and activates dynamin's GTPase activity in vitro.

Bin2, a functionally nonredundant member of the BAR adaptor gene family.

BAR family proteins are implicated in diverse cellular processes, including synaptic vesicle endocytosis, actin regulation, differentiation, cell survival, and tumorigenesis, and Bin2 appears to encode a nonredundant function in the BAR adaptor gene family.

Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila.

It is proposed that muscle amphiphysin is not involved in clathrin-mediated endocytosis, but in the structural organization of the membrane-bound compartments of the excitation-contraction coupling machinery of muscles.

Structure of the Sec23/24–Sar1 pre-budding complex of the COPII vesicle coat

The structural basis for GTP-dependent recruitment of a vesicular coat complex is established, and for uncoating through coat-controlled GTP hydrolysis is established.