Eisosome-driven plasma membrane organization is mediated by BAR domains

Nat Struct Mol Biol. 2011 Jun 19;18(7):854-6. doi: 10.1038/nsmb.2080.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / metabolism*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology
  • Multigene Family
  • Phosphoproteins / chemistry*
  • Phosphoproteins / metabolism
  • Phosphoproteins / physiology
  • Phylogeny
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / physiology
  • Sequence Analysis, Protein

Substances

  • LSP1 protein, S cerevisiae
  • Membrane Proteins
  • PIL1 protein, S cerevisiae
  • Phosphoproteins
  • Saccharomyces cerevisiae Proteins

Associated data

  • PDB/3PLT