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Eisosome proteins assemble into a membrane scaffold.

Spatial organization of membranes into domains of distinct protein and lipid composition is a fundamental feature of biological systems. The plasma membrane is organized in such domains to efficiently orchestrate the many reactions occurring there simultaneously. Despite the almost universal presence of membrane domains, mechanisms of their formation are often unclear. Yeast cells feature prominent plasma membrane domain organization, which is at least partially mediated by eisosomes. Eisosomes are large protein complexes that are primarily composed of many subunits of two Bin-Amphiphysin-Rvs domain-containing proteins, Pil1 and Lsp1. In this paper, we show that these proteins self-assemble into higher-order structures and bind preferentially to phosphoinositide-containing membranes. Using a combination of electron microscopy approaches, we generate structural models of Pil1 and Lsp1 assemblies, which resemble eisosomes in cells. Our data suggest that the mechanism of membrane organization by eisosomes is mediated by self-assembly of its core components into a membrane-bound protein scaffold with lipid-binding specificity.

Pubmed ID: 22123866


  • Karotki L
  • Huiskonen JT
  • Stefan CJ
  • Ziółkowska NE
  • Roth R
  • Surma MA
  • Krogan NJ
  • Emr SD
  • Heuser J
  • Grünewald K
  • Walther TC


The Journal of cell biology

Publication Data

November 28, 2011

Associated Grants

  • Agency: Wellcome Trust, Id: 090532
  • Agency: Wellcome Trust, Id: 090895
  • Agency: NIGMS NIH HHS, Id: R01 GM084448

Mesh Terms

  • Cell Membrane
  • Phosphoproteins
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins