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      LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.

      The EMBO Journal

      Transfection, metabolism, Subcellular Fractions, Sequence Homology, Amino Acid, Rats, Protein Processing, Post-Translational, ultrastructure, Phagosomes, Molecular Sequence Data, genetics, Microtubule-Associated Proteins, Microscopy, Immunoelectron, Intracellular Membranes, Humans, HeLa Cells, Fungal Proteins, DNA Primers, Base Sequence, Animals, Amino Acid Sequence

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          Abstract

          Little is known about the protein constituents of autophagosome membranes in mammalian cells. Here we demonstrate that the rat microtubule-associated protein 1 light chain 3 (LC3), a homologue of Apg8p essential for autophagy in yeast, is associated to the autophagosome membranes after processing. Two forms of LC3, called LC3-I and -II, were produced post-translationally in various cells. LC3-I is cytosolic, whereas LC3-II is membrane bound. The autophagic vacuole fraction prepared from starved rat liver was enriched with LC3-II. Immunoelectron microscopy on LC3 revealed specific labelling of autophagosome membranes in addition to the cytoplasmic labelling. LC3-II was present both inside and outside of autophagosomes. Mutational analyses suggest that LC3-I is formed by the removal of the C-terminal 22 amino acids from newly synthesized LC3, followed by the conversion of a fraction of LC3-I into LC3-II. The amount of LC3-II is correlated with the extent of autophagosome formation. LC3-II is the first mammalian protein identified that specifically associates with autophagosome membranes.

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          Author and article information

          Journal
          10.1093/emboj/19.21.5720
          11060023
          305793

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