Abstract
Plasma membranes are organized into domains of different protein and lipid composition. Eisosomes are key complexes for yeast plasma membrane organization, containing primarily Pil1 and Lsp1. Here we show that both proteins consist mostly of a banana-shaped BAR domain common to membrane sculpting proteins, most similar to the ones of amphiphysin, arfaptin 2 and endophilin 2. Our data reveal a previously unrecognized family of BAR-domain proteins involved in plasma membrane organization.
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Acknowledgements
We would like to thank P. de Camilli, E. Conti, F. Förster, T. Keil, W. Minor, S. Schuck, S. Suppmann, A. Wlodawer and the MPI-B Crystallization Facility for discussion and help with experiments and the German Research Foundation (N.E.Z. and T.C.W.), Academy of Finland (grant 130750, J.T.H.) and Boehringer Ingelheim fellowships (L.K.) for funding.
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All authors contributed to design and execution of experiments. N.E.Z. produced the protein, grew crystals, solved the structure of Lsp1 and performed the confocal microscopy. N.E.Z. and T.C.W. wrote the manuscript.
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The authors declare no competing financial interests.
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Supplementary Text and Figures
Supplementary Figures 1–8, Supplementary Tables 1–2 and Supplementary Methods (PDF 1412 kb)
Supplementary Video 1
Pil1-GFP R126E in the pil1Δ lsp1Δ strain forms long rods traversing the cytoplasm. Ylr413w-RFPmars is used as a membrane staining marker. z-stack images collected at 0.2-μm distances. (AVI 88 kb)
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Ziółkowska, N., Karotki, L., Rehman, M. et al. Eisosome-driven plasma membrane organization is mediated by BAR domains. Nat Struct Mol Biol 18, 854–856 (2011). https://doi.org/10.1038/nsmb.2080
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DOI: https://doi.org/10.1038/nsmb.2080
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