Journal
FEBS LETTERS
Volume 583, Issue 7, Pages 1078-1083Publisher
WILEY
DOI: 10.1016/j.febslet.2009.03.009
Keywords
Autophagy; Autophagosome; Ubiquitin-like protein; Phosphatidylethanolamine; Atg3; Atg8-PE
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [15002012, 19002015, 15GS0320]
- Grants-in-Aid for Scientific Research [15GS0320, 15002012, 19002015] Funding Source: KAKEN
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Autophagy is a bulk degradation process conserved among eukaryotes. In macro-autophagy, autophagosomes sequester cytoplasmic components and deliver their contents to lysosomes/vacuoles. Autophagosome formation requires the conjugation of Atg8, a ubiquitin-like protein, to phosphatidylethanolamine ( PE). Here we report that the amino (N)-terminal region of Atg3, an E2-like enzyme for Atg8, plays a crucial role in Atg8-PE conjugation. The conjugating activities of Atg3 mutants lacking the 7 N-terminal amino acid residues or containing a Leu-to-Asp mutation at position 6 were severely impaired both in vivo and in vitro. In addition, the amino-terminal region is critical for interaction with the substrate, PE.
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