Formation and expansion of the pre-autophagosomal structure in yeast requires the attachment of the ubiquitin-like protein Atg8 via its C-terminal glycine to the amino group of phosphatidylethanolamine (PE), enabling its anchoring to the isolation membrane of the autophagosome. In mammals, Atg8 is represented by at least six orthologs that fall into two subgroups, LC3- and GABARAP-like proteins and the free and PE linked versions of these proteins are often referred to as LC3-I and LC3-II respectively.
Whilst the specific roles for each individual protein have yet to be fully elucidated they have been shown to be involved in binding and selection of ubiqitinated autophagy substrate proteins, via ubiquitin / LC3 binding receptor proteins such as p62, in addition to their role in autophagosome biogenesis. Release of LC3 / GABARAP proteins via their cleavage from the mature autophagosome structure by Atg4 proteases facilitates their recycling and may be a requirement for autophagosome-lysosome fusion to take place.
应用类型
免疫原
Peptide derived from N-terminal region of human LC3A protein
