title: Eisosome-driven plasma membrane organization is mediated by BAR domains.
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.
authors.affiliation: Max Planck Institute of Biochemistry, Organelle Architecture and Dynamics, Martinsried, Germany.
authors.forename: Natasza E
authors.initials: NE
authors.lastname: Ziółkowska
authors.forename: Lena
authors.initials: L
authors.lastname: Karotki
authors.forename: Michael
authors.initials: M
authors.lastname: Rehman
authors.forename: Juha T
authors.initials: JT
authors.lastname: Huiskonen
authors.forename: Tobias C
authors.initials: TC
authors.lastname: Walther
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D005810:Multigene Family; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D020539:Sequence Analysis, Protein
chemical_list: C487328:LSP1 protein, S cerevisiae; D008565:Membrane Proteins; C487327:PIL1 protein, S cerevisiae; D010750:Phosphoproteins; D029701:Saccharomyces cerevisiae Proteins