BAR domains as sensors of membrane curvature: the amphiphysin BAR structure

Brian J Peter; Helen M Kent; Ian G Mills; Yvonne Vallis; P Jonathan G Butler; Philip R Evans; Harvey T McMahon

doi:10.1126/science.1092586

BAR domains as sensors of membrane curvature: the amphiphysin BAR structure

Brian J Peter, Helen M Kent, Ian G Mills, Yvonne Vallis, P Jonathan G Butler, Philip R Evans, Harvey T McMahon

School of Medicine, Dentistry and Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

1427 Citations (Scopus)

Abstract

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 find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.

Original language	English
Pages (from-to)	495-9
Number of pages	5
Journal	Science
Volume	303
Issue number	5657
DOIs	https://doi.org/10.1126/science.1092586
Publication status	Published - 23 Jan 2004

Keywords

ADP-Ribosylation Factors
Adaptor Proteins, Signal Transducing
Amino Acid Sequence
Animals
COP-Coated Vesicles
Carrier Proteins
Cell Membrane
Clathrin
Clathrin-Coated Vesicles
Coated Vesicles
Crystallography, X-Ray
Cytoskeletal Proteins
Dimerization
Drosophila
Drosophila Proteins
GTPase-Activating Proteins
Liposomes
Models, Molecular
Molecular Sequence Data
Mutation
Nerve Tissue Proteins
Nuclear Proteins
Phosphoproteins
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary

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title = "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure",

abstract = "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 find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.",

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author = "Peter, {Brian J} and Kent, {Helen M} and Mills, {Ian G} and Yvonne Vallis and Butler, {P Jonathan G} and Evans, {Philip R} and McMahon, {Harvey T}",

year = "2004",

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doi = "10.1126/science.1092586",

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AU - Peter, Brian J

AU - Kent, Helen M

AU - Mills, Ian G

AU - Vallis, Yvonne

AU - Butler, P Jonathan G

AU - Evans, Philip R

AU - McMahon, Harvey T

PY - 2004/1/23

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N2 - 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 find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.

AB - 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 find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.

KW - ADP-Ribosylation Factors

KW - Adaptor Proteins, Signal Transducing

KW - Amino Acid Sequence

KW - Animals

KW - COP-Coated Vesicles

KW - Carrier Proteins

KW - Cell Membrane

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KW - Clathrin-Coated Vesicles

KW - Coated Vesicles

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KW - Cytoskeletal Proteins

KW - Dimerization

KW - Drosophila

KW - Drosophila Proteins

KW - GTPase-Activating Proteins

KW - Liposomes

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Mutation

KW - Nerve Tissue Proteins

KW - Nuclear Proteins

KW - Phosphoproteins

KW - Protein Binding

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

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DO - 10.1126/science.1092586

M3 - Article

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SN - 0036-8075

VL - 303

SP - 495

EP - 499

JO - Science

JF - Science

IS - 5657

ER -

BAR domains as sensors of membrane curvature: the amphiphysin BAR structure

Abstract

Keywords

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