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lüll The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy Protein modifications: beyond the usual suspects review series Geng J; Klionsky DJEMBO Rep 2008[Sep]; 9 (9): 859-64As a lysosomal/vacuolar degradative pathway that is conserved in eukaryotic organisms, autophagy mediates the turnover of long-lived proteins and excess or aberrant organelles. The main characteristic of autophagy is the formation of a double-membrane vesicle, the autophagosome, which envelops part of the cytoplasm and delivers it to the lysosome/vacuole for breakdown and eventual recycling of the degradation products. Among the approximately 30 autophagy-related (Atg) genes identified so far, there are two ubiquitin-like proteins, Atg12 and Atg8. Analogous to ubiquitination, Atg12 is conjugated to Atg5 by Atg7--an E1-like protein--and Atg10--an E2-like protein. Similarly, Atg7 and Atg3 are the respective E1-like and E2-like proteins that mediate the conjugation of Atg8 to phosphatidylethanolamine. Both Atg12-Atg5 and Atg8 localize to the developing autophagosome. The Atg12-Atg5 conjugate facilitates the lipidation of Atg8 and directs its correct subcellular localization. Atg8-phosphatidylethanolamine is probably a scaffold protein that supports membrane expansion and the amount present correlates with the size of autophagosomes.|Animals[MESH]|Autophagy/*physiology[MESH]|Humans[MESH]|Models, Biological[MESH]|Models, Molecular[MESH]|Protein Isoforms/chemistry/metabolism/physiology[MESH]|Protein Processing, Post-Translational[MESH]|Protein Structure, Secondary[MESH]|Ubiquitin/chemistry/metabolism/*physiology[MESH] |