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Background: Microtubule-associated MAPILC3A constitute nearly half of the mass of all the microtubule associated proteins that copurify with brain microtubules. MAPILC3A is composed of a heavy chain and multiple light-chain subunits. The molecular machinery required for autophagy is highly conserved in all eukaryotes as seen by the high degree of conservation of proteins involved in the formation of the autophagosome membranes. Recently, both yeast Apg8p and its rat homologue LC3-II were identified as essential constituents of autophagosome membrane as a processed form. In addition, both the yeast and human proteins exist in two modified forms produced by a series of post-translational modifications including a critical C-terminal cleavage after a conserved Gly residue, and the smaller processed form is associated with the autophagosome membranes Results revealed different regulation of the three human isoforms of LC3-II and implicate that the three isoforms may have different physiological functions (1). 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. LC3-II is the first mammalian protein identified that specifically associates with autophagosome membranes (2).