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Published Online November 26, 2003
Science DOI: 10.1126/science.1092586

Research Articles

Submitted on October 15, 2003
Accepted on November 18, 2003

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

Brian J. Peter 1, Helen M. Kent 1, Ian G. Mills 2, Yvonne Vallis 1, P. Jonathan G. Butler 1, Philip R. Evans 1*, Harvey T. McMahon 1*

1 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
2 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK; Present address: Department of Oncology, University of Cambridge, Hutchison/MRC Cancer Research Centre, Hills Road, Cambridge CB2 2XZ, UK.

* To whom correspondence should be addressed. E-mail: pre{at}mrc-lmb.cam.ac.uk, hmm{at}mrc-lmb.cam.ac.uk.

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 arfaptin2, which we find also binds and tubulates membranes. From this we predict BAR domains 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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The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy.
G. Ren, P. Vajjhala, J. S. Lee, B. Winsor, and A. L. Munn (2006)
Microbiol. Mol. Biol. Rev. 70, 37-120
   Abstract »    Full Text »    PDF »
Biogenesis of caveolae: a structural model for caveolin-induced domain formation..
R. G. Parton, M. Hanzal-Bayer, and J. F. Hancock (2006)
J. Cell Sci. 119, 787-796
   Abstract »    Full Text »    PDF »
Lipid Binding Regulates Synaptic Targeting of PICK1, AMPA Receptor Trafficking, and Synaptic Plasticity.
W. Jin, W.-P. Ge, J. Xu, M. Cao, L. Peng, W. Yung, D. Liao, S. Duan, M. Zhang, and J. Xia (2006)
J. Neurosci. 26, 2380-2390
   Abstract »    Full Text »    PDF »
Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals Roles for the Rvs Heterodimer In Vivo.
H. Friesen, C. Humphries, Y. Ho, O. Schub, K. Colwill, and B. Andrews (2006)
Mol. Biol. Cell 17, 1306-1321
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Extracellular Signal-regulated Kinase Regulates Clathrin-independent Endosomal Trafficking.
S. E. Robertson, S. R. G. Setty, A. Sitaram, M. S. Marks, R. E. Lewis, and M. M. Chou (2006)
Mol. Biol. Cell 17, 645-657
   Abstract »    Full Text »    PDF »
Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis.
K. Tsujita, S. Suetsugu, N. Sasaki, M. Furutani, T. Oikawa, and T. Takenawa (2006)
J. Cell Biol. 172, 269-279
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A genome-wide visual screen reveals a role for sphingolipids and ergosterol in cell surface delivery in yeast.
T. J. Proszynski, R. W. Klemm, M. Gravert, P. P. Hsu, Y. Gloor, J. Wagner, K. Kozak, H. Grabner, K. Walzer, M. Bagnat, et al. (2005)
PNAS 102, 17981-17986
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Involvement of Rac in actin cytoskeleton rearrangements induced by MIM-B.
G. Bompard, S. J. Sharp, G. Freiss, and L. M. Machesky (2005)
J. Cell Sci. 118, 5393-5403
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Loss of Bif-1 Suppresses Bax/Bak Conformational Change and Mitochondrial Apoptosis.
Y. Takahashi, M. Karbowski, H. Yamaguchi, A. Kazi, J. Wu, S. M. Sebti, R. J. Youle, and H.-G. Wang (2005)
Mol. Cell. Biol. 25, 9369-9382
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Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport.
J. G. Carlton, M. V. Bujny, B. J. Peter, V. M. J. Oorschot, A. Rutherford, R. S. Arkell, J. Klumperman, H. T. McMahon, and P. J. Cullen (2005)
J. Cell Sci. 118, 4527-4539
   Abstract »    Full Text »    PDF »
Marrying Immunotherapy with Chemotherapy: Why Say IDO?.
A. J. Muller and G. C. Prendergast (2005)
Cancer Res. 65, 8065-8068
   Abstract »    Full Text »    PDF »
Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors.
I. G. Mills, L. Gaughan, C. Robson, T. Ross, S. McCracken, J. Kelly, and D. E. Neal (2005)
J. Cell Biol. 170, 191-200
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