Determination of Sec18-Lipid Interactions by Liposome-Binding Assay

Methods Mol Biol. 2019:1860:211-220. doi: 10.1007/978-1-4939-8760-3_13.

Abstract

Protein-lipid binding interactions play a key role in the regulation of peripheral membrane protein function. Liposome-binding assays are a simple and affordable means of screening for specific protein-lipid interactions. Liposomes are prepared by mixing phospholipid combinations of interest before drying and rehydration. Sonication of the lipid mixture produces small unilamellar vesicles (SUVs) which are incubated with a protein of interest to allow for any binding to occur. Liposomes and liposome-protein complexes are floated on a sucrose gradient by centrifugation to separate them from unbound protein. Bound protein levels are easily determined by SDS-PAGE and Western blotting. This approach provides a reliable means of assaying novel protein-lipid interactions in vitro. Here we use liposome floatation to show the binding of the SNARE-activating protein Sec18 (mammalian NSF) to phosphatidic acid.

Keywords: Liposome; Membrane fusion; Membrane trafficking; NSF; Phosphatidic acid; Phospholipids; SNARE; Sec18.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / isolation & purification
  • Adenosine Triphosphatases / metabolism*
  • Liposomes / chemistry
  • Liposomes / metabolism*
  • Membrane Fusion
  • Phospholipids / chemistry
  • Phospholipids / metabolism*
  • Protein Binding
  • SNARE Proteins / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / isolation & purification
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Vesicular Transport Proteins / chemistry
  • Vesicular Transport Proteins / isolation & purification
  • Vesicular Transport Proteins / metabolism*

Substances

  • Liposomes
  • Phospholipids
  • SNARE Proteins
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins
  • Adenosine Triphosphatases
  • SEC18 protein, S cerevisiae