Skip to main content
SpringerLink
Log in

Eisosome-driven plasma membrane organization is mediated by BAR domains

  • Brief Communication
  • Published:

From Nature Structural & Molecular Biology

View current issue Submit your manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Figure 1: Molecular structure of Lsp1 and Pil1.
Figure 2: Lsp1 and Pil1 belong to the superfamily of BAR domain–containing proteins.
Figure 3: The positively charged patch on the Pil1 concave surface is required for normal Pil1 localization and function.

Similar content being viewed by others

Accession codes

Primary accessions

Protein Data Bank

Referenced accessions

Protein Data Bank

References

  1. Simons, K. & Ikonen, E. Nature 387, 569–572 (1997).

    Article  CAS  Google Scholar 

  2. Lingwood, D. & Simons, K. Science 327, 46–50 (2010).

    Article  CAS  Google Scholar 

  3. Walther, T.C. et al. Nature 439, 998–1003 (2006).

    Article  CAS  Google Scholar 

  4. Grossmann, G., Opekarova, M., Malinsky, J., Weig-Meckl, I. & Tanner, W. EMBO J. 26, 1–8 (2007).

    Article  CAS  Google Scholar 

  5. Strádalová, V. et al. J. Cell Sci. 122, 2887–2894 (2009).

    Article  Google Scholar 

  6. Fröhlich, F. et al. J. Cell Biol. 185, 1227–1242 (2009).

    Article  Google Scholar 

  7. Minor, W., Cymborowski, M., Otwinowski, Z. & Chruszcz, M. Acta Crystallogr. D Biol. Crystallogr. 62, 859–866 (2006).

    Article  Google Scholar 

  8. Peter, B.J. et al. Science 303, 495–499 (2004).

    Article  CAS  Google Scholar 

  9. Tarricone, C. et al. Nature 411, 215–219 (2001).

    Article  CAS  Google Scholar 

  10. Masuda, M. & Mochizuki, N. Semin. Cell Dev. Biol. 21, 391–398 (2010).

    Article  CAS  Google Scholar 

Download references

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.

Author information

Authors and Affiliations

  1. Max Planck Institute of Biochemistry, Organelle Architecture and Dynamics, Martinsried, Germany

    Natasza E Ziółkowska, Lena Karotki & Michael Rehman

  2. Division of Structural Biology, Oxford Particle Imaging Centre, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK

    Juha T Huiskonen

  3. Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut, USA

    Tobias C Walther

Authors
  1. Natasza E Ziółkowska
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Lena Karotki
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Michael Rehman
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Juha T Huiskonen
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Tobias C Walther
    View author publications

    You can also search for this author in PubMed Google Scholar

Contributions

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.

Corresponding author

Correspondence to Tobias C Walther.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Supplementary information

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)

Rights and permissions

Reprints and permissions

About this article

Cite this article

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

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb.2080

  • Springer Nature America, Inc.

This article is cited by

Search

Navigation