Journal
AUTOPHAGY
Volume 8, Issue 6, Pages 883-892Publisher
LANDES BIOSCIENCE
DOI: 10.4161/auto.19652
Keywords
autophagy; ubiquitin-like proteins; deconjugation; Atg4; Atg8
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Funding
- National Key Basic Research Program of China [2011CB910100]
- National Natural Science Foundation of China [31171285, 30971441]
- National Institutes of Health grant [GM53396]
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Modification of target molecules by ubiquitin or ubiquitin-like (Ubl) proteins is generally reversible. Little is known, however, about the physiological function of the reverse reaction, deconjugation. Atg8 is a unique Ubl protein whose conjugation target is the lipid phosphatidylethanolamine (PE). Atg8 functions in the formation of double-membrane autophagosomes, a central step in the well-conserved intracellular degradation pathway of macroautophagy (hereafter autophagy). Here we show that the deconjugation of Atg8-PE by the cysteine protease Atg4 plays dual roles in the formation of autophagosomes. During the early stage of autophagosome formation, deconjugation releases Atg8 from non-autophagosomal membranes to maintain a proper supply of Atg8. At a later stage, the release of Atg8 from intermediate autophagosomal membranes facilitates the maturation of these structures into fusion-capable autophagosomes. These results provide new insights into the functions of Atg8-PE and its deconjugation.
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