title: Eisosome proteins assemble into a membrane scaffold.
abstract: 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.
authors: Organelle Architecture and Dynamics, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
authors: Lena
authors: L
authors: Karotki
authors: Juha T
authors: JT
authors: Huiskonen
authors: Christopher J
authors: CJ
authors: Stefan
authors: Natasza E
authors: NE
authors: Ziółkowska
authors: Robyn
authors: R
authors: Roth
authors: Michal A
authors: MA
authors: Surma
authors: Nevan J
authors: NJ
authors: Krogan
authors: Scott D
authors: SD
authors: Emr
authors: John
authors: J
authors: Heuser
authors: Kay
authors: K
authors: Grünewald
authors: Tobias C
authors: TC
authors: Walther
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: C487328:LSP1 protein, S cerevisiae; C487327:PIL1 protein, S cerevisiae; D010750:Phosphoproteins; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins