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A ubiquitin-like system mediates protein lipidation

Author

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  • Yoshinobu Ichimura

    (National Institute for Basic Biology
    School of Life Science, The Graduate University for Advanced Studies)

  • Takayoshi Kirisako

    (National Institute for Basic Biology
    School of Life Science, The Graduate University for Advanced Studies)

  • Toshifumi Takao

    (Institute for Protein Research, Osaka University)

  • Yoshinori Satomi

    (Institute for Protein Research, Osaka University)

  • Yasutsugu Shimonishi

    (Institute for Protein Research, Osaka University)

  • Naotada Ishihara

    (National Institute for Basic Biology)

  • Noboru Mizushima

    (National Institute for Basic Biology
    PRESTO, Japan Science and Technology Corporation (JST))

  • Isei Tanida

    (Juntendo University School of Medicine)

  • Eiki Kominami

    (Juntendo University School of Medicine)

  • Mariko Ohsumi

    (High Tech Research Center, Teikyo University of Science and Technology)

  • Takeshi Noda

    (National Institute for Basic Biology
    School of Life Science, The Graduate University for Advanced Studies)

  • Yoshinori Ohsumi

    (National Institute for Basic Biology
    School of Life Science, The Graduate University for Advanced Studies)

Abstract

Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole1,2. Apg8/Aut7 is an essential factor for autophagy in yeast3,4,5. We previously found that the carboxy-terminal arginine of nascent Apg8 is removed by Apg4/Aut2 protease, leaving a glycine residue at the C terminus6. Apg8 is then converted to a form (Apg8-X) that is tightly bound to the membrane6. 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 autophagy6.

Suggested Citation

  • Yoshinobu Ichimura & Takayoshi Kirisako & Toshifumi Takao & Yoshinori Satomi & Yasutsugu Shimonishi & Naotada Ishihara & Noboru Mizushima & Isei Tanida & Eiki Kominami & Mariko Ohsumi & Takeshi Noda &, 2000. "A ubiquitin-like system mediates protein lipidation," Nature, Nature, vol. 408(6811), pages 488-492, November.
    • Handle: RePEc:nat:nature:v:408:y:2000:i:6811:d:10.1038_35044114
    DOI: 10.1038/35044114
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    Citations

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    Cited by:

    1. Kai-Chih Hung & Hui-Ju Huang & Ming-Wei Lin & Yen-Ping Lei & Anya Maan-yuh Lin, 2014. "Roles of Autophagy in MPP+-Induced Neurotoxicity In Vivo: The Involvement of Mitochondria and α-Synuclein Aggregation," PLOS ONE, Public Library of Science, vol. 9(3), pages 1-9, March.
    2. Yuki Takakura & Moeka Machida & Natsumi Terada & Yuka Katsumi & Seika Kawamura & Kenta Horie & Maki Miyauchi & Tatsuya Ishikawa & Nobuko Akiyama & Takao Seki & Takahisa Miyao & Mio Hayama & Rin Endo &, 2024. "Mitochondrial protein C15ORF48 is a stress-independent inducer of autophagy that regulates oxidative stress and autoimmunity," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    3. Barbara Baldo & Rana Soylu & Åsa Petersén, 2013. "Maintenance of Basal Levels of Autophagy in Huntington’s Disease Mouse Models Displaying Metabolic Dysfunction," PLOS ONE, Public Library of Science, vol. 8(12), pages 1-15, December.
    4. M. O. Aremu & Hashim Ibrahim, 2017. "Dietary Phospholipids and Phytostrerols: A Review on Some Nigerian Vegetable Oils," International Journal of Sciences, Office ijSciences, vol. 6(09), pages 94-102, September.
    5. Hayden Weng Siong Tan & Guang Lu & Han Dong & Yik-Lam Cho & Auginia Natalia & Liming Wang & Charlene Chan & Dennis Kappei & Reshma Taneja & Shuo-Chien Ling & Huilin Shao & Shih-Yin Tsai & Wen-Xing Din, 2022. "A degradative to secretory autophagy switch mediates mitochondria clearance in the absence of the mATG8-conjugation machinery," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    6. Jongchan Woo & Seungmee Jung & Seongbeom Kim & Yurong Li & Hyunjung Chung & Tatiana V. Roubtsova & Honghong Zhang & Celine Caseys & Dan Kliebenstein & Kyung-Nam Kim & Richard M. Bostock & Yong-Hwan Le, 2024. "Attenuation of phytofungal pathogenicity of Ascomycota by autophagy modulators," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    7. Kuninori Suzuki & Shingo Nakamura & Mayumi Morimoto & Kiyonaga Fujii & Nobuo N Noda & Fuyuhiko Inagaki & Yoshinori Ohsumi, 2014. "Proteomic Profiling of Autophagosome Cargo in Saccharomyces cerevisiae," PLOS ONE, Public Library of Science, vol. 9(3), pages 1-9, March.

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