Semisynthetic lipidated LC3 protein mediates membrane fusion

Chembiochem. 2013 Jul 22;14(11):1296-300. doi: 10.1002/cbic.201300344. Epub 2013 Jul 8.

Abstract

All together: Lipidated LC3 has been synthesized by expressed protein ligation. A TEV-cleavable MBP tag was employed to facilitate ligation under folding conditions and to solubilize the lipidated protein. The synthetic LC3-phosphatidylethanolamine (PE) mediates membrane tethering and fusion at the physiological concentration of PE, and could be a useful tool for autophagy studies.

Keywords: LC3; autophagy; expressed protein ligation; lipidated proteins; membrane fusion; protein synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cysteine Endopeptidases / metabolism
  • Endopeptidases / metabolism
  • Humans
  • Light
  • Liposomes / metabolism*
  • Maltose-Binding Proteins / chemistry
  • Maltose-Binding Proteins / genetics
  • Maltose-Binding Proteins / metabolism
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism*
  • Phosphatidylethanolamines / chemistry*
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Scattering, Radiation

Substances

  • Liposomes
  • MAP1LC3A protein, human
  • Maltose-Binding Proteins
  • Microtubule-Associated Proteins
  • Phosphatidylethanolamines
  • Recombinant Fusion Proteins
  • phosphatidylethanolamine
  • Endopeptidases
  • TEV protease
  • Cysteine Endopeptidases