Eisosome proteins assemble into a membrane scaffold. Academic Article uri icon

Overview

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.

publication date

  • November 28, 2011

Research

keywords

  • Cell Membrane
  • Phosphoproteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins

Identity

PubMed Central ID

  • PMC3257569

Scopus Document Identifier

  • 84855882640

Digital Object Identifier (DOI)

  • 10.1083/jcb.201104040

PubMed ID

  • 22123866

Additional Document Info

volume

  • 195

issue

  • 5