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PMID:11100732

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Citation

Ichimura, Y, Kirisako, T, Takao, T, Satomi, Y, Shimonishi, Y, Ishihara, N, Mizushima, N, Tanida, I, Kominami, E, Ohsumi, M, Noda, T and Ohsumi, Y (2000) A ubiquitin-like system mediates protein lipidation. Nature 408:488-92

Abstract

Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole. Apg8/Aut7 is an essential factor for autophagy in yeast. We previously found that the carboxy-terminal arginine of nascent Apg8 is removed by Apg4/Aut2 protease, leaving a glycine residue at the C terminus. Apg8 is then converted to a form (Apg8-X) that is tightly bound to the membrane. Here we report a new mode of protein lipidation. Apg8 is covalently conjugated to phosphatidylethanolamine through an amide bond between the C-terminal glycine and the amino group of phosphatidylethanolamine. This lipidation is mediated by a ubiquitination-like system. Apg8 is a ubiquitin-like protein that is activated by an E1 protein, Apg7 (refs 7, 8), and is transferred subsequently to the E2 enzymes Apg3/Aut1 (ref. 9). Apg7 activates two different ubiquitin-like proteins, Apg12 (ref. 10) and Apg8, and assigns them to specific E2 enzymes, Apg10 (ref. 11) and Apg3, respectively. These reactions are necessary for the formation of Apg8-phosphatidylethanolamine. This lipidation has an essential role in membrane dynamics during autophagy.

Links

PubMed Online version:10.1038/35044114

Keywords

Amino Acid Sequence; Autophagy; Binding Sites; Cell Membrane/metabolism; Fungal Proteins/genetics; Fungal Proteins/metabolism; Microtubule-Associated Proteins/genetics; Microtubule-Associated Proteins/metabolism; Molecular Sequence Data; Phosphatidylethanolamines/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins; Ubiquitin-Conjugating Enzymes; Ubiquitins/metabolism

Significance

Annotations

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status


See also

References

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