A ubiquitin-like system mediates protein lipidation

Yoshinobu Ichimura, Takayoshi Kirisako, Toshifumi Takao, Yoshinori Satomi, Yasutsugu Shimonishi, Naotada Ishihara, Noboru Mizushima, Isei Tanida, Eiki Kominami, Mariko Ohsumi, Takeshi Noda and Yoshinori Ohsumi ()
Additional contact information
Yoshinobu Ichimura: National Institute for Basic Biology
Takayoshi Kirisako: National Institute for Basic Biology
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
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
Yoshinori Ohsumi: National Institute for Basic Biology

Nature, 2000, vol. 408, issue 6811, 488-492

Abstract: 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.

Date: 2000
References: Add references at CitEc
Citations: View citations in EconPapers (8)

Downloads: (external link)
https://www.nature.com/articles/35044114 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:408:y:2000:i:6811:d:10.1038_35044114

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/35044114

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().