Eisosome-driven plasma membrane organization is mediated by BAR domains

Natasza E. Ziółkowska, Lena Karotki, Michael Rehman, Juha T. Huiskonen, Tobias C. Walther

Research output: Contribution to journalArticle

44 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)854-856
Number of pages3
JournalNature Structural and Molecular Biology
Volume18
Issue number7
DOIs
Publication statusPublished - Jul 2011

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Cell Membrane
Musa
Membrane Proteins
Yeasts
Lipids
Proteins
Protein Domains
amphiphysin

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Ziółkowska, N. E., Karotki, L., Rehman, M., Huiskonen, J. T., & Walther, T. C. (2011). Eisosome-driven plasma membrane organization is mediated by BAR domains. Nature Structural and Molecular Biology, 18(7), 854-856. https://doi.org/10.1038/nsmb.2080

Eisosome-driven plasma membrane organization is mediated by BAR domains. / Ziółkowska, Natasza E.; Karotki, Lena; Rehman, Michael; Huiskonen, Juha T.; Walther, Tobias C.

In: Nature Structural and Molecular Biology, Vol. 18, No. 7, 07.2011, p. 854-856.

Research output: Contribution to journalArticle

Ziółkowska, NE, Karotki, L, Rehman, M, Huiskonen, JT & Walther, TC 2011, 'Eisosome-driven plasma membrane organization is mediated by BAR domains', Nature Structural and Molecular Biology, vol. 18, no. 7, pp. 854-856. https://doi.org/10.1038/nsmb.2080
Ziółkowska, Natasza E. ; Karotki, Lena ; Rehman, Michael ; Huiskonen, Juha T. ; Walther, Tobias C. / Eisosome-driven plasma membrane organization is mediated by BAR domains. In: Nature Structural and Molecular Biology. 2011 ; Vol. 18, No. 7. pp. 854-856.
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