Amphipathic motifs in BAR domains are essential for membrane curvature sensing Export

@article{citeulike:5919956, abstract = {BAR (Bin/Amphiphysin/Rvs) domains and amphipathic -helices (AHs) are believed to be sensors of membrane curvature thus facilitating the assembly of protein complexes on curved membranes. Here, we used quantitative fluorescence microscopy to compare the binding of both motifs on single nanosized liposomes of different diameters and therefore membrane curvature. Characterization of members of the three BAR domain families showed surprisingly that the crescent-shaped BAR dimer with its positively charged concave face is not able to sense membrane curvature. Mutagenesis on BAR domains showed that membrane curvature sensing critically depends on the N-terminal AH and furthermore that BAR domains sense membrane curvature through hydrophobic insertion in lipid packing defects and not through electrostatics. Consequently, amphipathic motifs, such as AHs, that are often associated with BAR domains emerge as an important means for a protein to sense membrane curvature. Measurements on single liposomes allowed us to document heterogeneous binding behaviour within the ensemble and quantify the influence of liposome polydispersity on bulk membrane curvature sensing experiments. The latter results suggest that bulk liposome-binding experiments should be interpreted with great caution.}, author = {Bhatia, Vikram K. and Madsen, Kenneth L. and Bolinger, Pierre-Yves and Kunding, Andreas and Hedegard, Per and Gether, Ulrik and Stamou, Dimitrios}, citeulike-article-id = {5919956}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/emboj.2009.261}, citeulike-linkout-1 = {http://dx.doi.org/10.1038/emboj2009261a}, day = {08}, doi = {10.1038/emboj.2009.261}, issn = {0261-4189}, journal = {The EMBO Journal}, keywords = {bar, lipid, liposomes, snx}, month = {October}, number = {21}, pages = {3303--3314}, posted-at = {2009-11-04 13:19:52}, priority = {2}, publisher = {Nature Publishing Group}, title = {Amphipathic motifs in BAR domains are essential for membrane curvature sensing}, url = {http://dx.doi.org/10.1038/emboj.2009.261}, volume = {28}, year = {2009} }

TY - JOUR ID - citeulike:5919956 L3 - citeulike-article-id:5919956 N2 - BAR (Bin/Amphiphysin/Rvs) domains and amphipathic -helices (AHs) are believed to be sensors of membrane curvature thus facilitating the assembly of protein complexes on curved membranes. Here, we used quantitative fluorescence microscopy to compare the binding of both motifs on single nanosized liposomes of different diameters and therefore membrane curvature. Characterization of members of the three BAR domain families showed surprisingly that the crescent-shaped BAR dimer with its positively charged concave face is not able to sense membrane curvature. Mutagenesis on BAR domains showed that membrane curvature sensing critically depends on the N-terminal AH and furthermore that BAR domains sense membrane curvature through hydrophobic insertion in lipid packing defects and not through electrostatics. Consequently, amphipathic motifs, such as AHs, that are often associated with BAR domains emerge as an important means for a protein to sense membrane curvature. Measurements on single liposomes allowed us to document heterogeneous binding behaviour within the ensemble and quantify the influence of liposome polydispersity on bulk membrane curvature sensing experiments. The latter results suggest that bulk liposome-binding experiments should be interpreted with great caution. IS - 21 JF - The EMBO Journal SN - 0261-4189 EP - 3314 TI - Amphipathic motifs in BAR domains are essential for membrane curvature sensing PB - Nature Publishing Group VL - 28 SP - 3303 KW - bar KW - lipid KW - liposomes KW - snx AU - Bhatia, Vikram AU - Madsen, Kenneth AU - Bolinger, Pierre-Yves AU - Kunding, Andreas AU - Hedegard, Per AU - Gether, Ulrik AU - Stamou, Dimitrios PY - 2009/10/08/ UR - http://dx.doi.org/10.1038/emboj.2009.261 ER -