title: Semisynthetic lipidated LC3 protein mediates membrane fusion.
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.
authors.affiliation: Department of Chemical Biology, Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
authors.forename: Aimin
authors.initials: A
authors.lastname: Yang
authors.forename: Yanping
authors.initials: Y
authors.lastname: Li
authors.forename: Supansa
authors.initials: S
authors.lastname: Pantoom
authors.forename: Gemma
authors.initials: G
authors.lastname: Triola
authors.forename: Yao-Wen
authors.initials: YW
authors.lastname: Wu
mesh_terms: D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D008027:Light; D008081:Liposomes / Q000378:metabolism*; D058619:Maltose-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010714:Phosphatidylethanolamines / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D012542:Scattering, Radiation
chemical_list: D008081:Liposomes; C477012:MAP1LC3A protein, human; D058619:Maltose-Binding Proteins; D008869:Microtubule-Associated Proteins; D010714:Phosphatidylethanolamines; D011993:Recombinant Fusion Proteins; C483858:phosphatidylethanolamine; D010450:Endopeptidases; C099488:TEV protease; D003546:Cysteine Endopeptidases
keywords: LC3; autophagy; expressed protein ligation; lipidated proteins; membrane fusion; protein synthesis