A ubiquitin-like system mediates protein lipidation

Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole 1 , 2 . Apg8/Aut7 is an essential factor for autophagy in yeast 3 , 4 , 5 . We previously found that the carboxy-terminal arginine of nascent Apg8 is removed by Apg4/Aut2 protease, leaving a glycine resid...

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Published in	Nature (London) Vol. 408; no. 6811; pp. 488 - 492
Main Authors	Ichimura, Yoshinobu, Kirisako, Takayoshi, Takao, Toshifumi, Satomi, Yoshinori, Shimonishi, Yasutsugu, Ishihara, Naotada, Mizushima, Noboru, Tanida, Isei, Kominami, Eiki, Ohsumi, Mariko, Noda, Takeshi, Ohsumi, Yoshinori
Format	Journal Article
Language	English
Published	London Nature Publishing Group UK 23.11.2000 Nature Publishing Nature Publishing Group
Subjects	Amino Acid Sequence Apg10 protein Apg12 protein Apg3 protein Apg7 protein Apg8 protein Aut1 protein Aut7 protein Autophagy Autophagy-Related Protein 12 Autophagy-Related Protein 7 Autophagy-Related Protein 8 Family Autophagy-Related Proteins Binding Sites Biodegradation Biological and medical sciences Cell Membrane - metabolism Cellular biology Conformational dynamics in molecular biology Enzymes Fundamental and applied biological sciences. Psychology Fungal Proteins - genetics Fungal Proteins - metabolism Humanities and Social Sciences letter Lipids Membranes Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Molecular biophysics Molecular Sequence Data Molecules multidisciplinary phosphatidylethanolamine Phosphatidylethanolamines - metabolism Proteins Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Science Science (multidisciplinary) ubiquitin Ubiquitin-Conjugating Enzymes Ubiquitins - metabolism Yeasts Fungi Ubiquitin Phosphatidylethanolamine Conformational dynamics Ascomycetes Biomembrane Saccharomyces cerevisiae Protein Thallophyta
Online Access	Get full text
ISSN	0028-0836 1476-4687
DOI	10.1038/35044114

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Abstract	Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole 1 , 2 . Apg8/Aut7 is an essential factor for autophagy in yeast 3 , 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 terminus 6 . Apg8 is then converted to a form (Apg8-X) that is tightly bound to the membrane 6 . 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 6 .
AbstractList	Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole. 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. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole 1 , 2 . Apg8/Aut7 is an essential factor for autophagy in yeast 3 , 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 terminus 6 . Apg8 is then converted to a form (Apg8-X) that is tightly bound to the membrane 6 . 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 6 . 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. 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.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. 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, and is transferred subsequently to the E2 enzymes Apg3/Aut1. Apg7 activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. These reactions are necessary for the formation of Apg8-phosphatidylethanolamine. This lipidation has an essential role in membrane dynamics during autophagy.
Audience	Academic
Author	Ohsumi, Yoshinori Ishihara, Naotada Noda, Takeshi Satomi, Yoshinori Mizushima, Noboru Tanida, Isei Ohsumi, Mariko Takao, Toshifumi Shimonishi, Yasutsugu Kominami, Eiki Ichimura, Yoshinobu Kirisako, Takayoshi
Author_xml	– sequence: 1 givenname: Yoshinobu surname: Ichimura fullname: Ichimura, Yoshinobu organization: Department of Cell Biology, National Institute for Basic Biology, Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies – sequence: 2 givenname: Takayoshi surname: Kirisako fullname: Kirisako, Takayoshi organization: Department of Cell Biology, National Institute for Basic Biology, Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies – sequence: 3 givenname: Toshifumi surname: Takao fullname: Takao, Toshifumi organization: Institute for Protein Research, Osaka University – sequence: 4 givenname: Yoshinori surname: Satomi fullname: Satomi, Yoshinori organization: Institute for Protein Research, Osaka University – sequence: 5 givenname: Yasutsugu surname: Shimonishi fullname: Shimonishi, Yasutsugu organization: Institute for Protein Research, Osaka University – sequence: 6 givenname: Naotada surname: Ishihara fullname: Ishihara, Naotada organization: Department of Cell Biology, National Institute for Basic Biology – sequence: 7 givenname: Noboru surname: Mizushima fullname: Mizushima, Noboru organization: Department of Cell Biology, National Institute for Basic Biology, PRESTO, Japan Science and Technology Corporation (JST) – sequence: 8 givenname: Isei surname: Tanida fullname: Tanida, Isei organization: Department of Biochemistry, Juntendo University School of Medicine – sequence: 9 givenname: Eiki surname: Kominami fullname: Kominami, Eiki organization: Department of Biochemistry, Juntendo University School of Medicine – sequence: 10 givenname: Mariko surname: Ohsumi fullname: Ohsumi, Mariko organization: Department of Biosciences, High Tech Research Center, Teikyo University of Science and Technology – sequence: 11 givenname: Takeshi surname: Noda fullname: Noda, Takeshi organization: Department of Cell Biology, National Institute for Basic Biology, Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies – sequence: 12 givenname: Yoshinori surname: Ohsumi fullname: Ohsumi, Yoshinori email: yohsumi@nibb.ac.jp organization: Department of Cell Biology, National Institute for Basic Biology, Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies
BackLink	http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=884273$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/11100732$$D View this record in MEDLINE/PubMed
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Keywords	Fungi Ubiquitin Phosphatidylethanolamine Conformational dynamics Ascomycetes Biomembrane Saccharomyces cerevisiae Protein Thallophyta
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Snippet	Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole 1 , 2 . Apg8/Aut7 is an essential factor for autophagy in yeast... 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... Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole. We previously found that the carboxy-terminal arginine of...
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SubjectTerms	Amino Acid Sequence Apg10 protein Apg12 protein Apg3 protein Apg7 protein Apg8 protein Aut1 protein Aut7 protein Autophagy Autophagy-Related Protein 12 Autophagy-Related Protein 7 Autophagy-Related Protein 8 Family Autophagy-Related Proteins Binding Sites Biodegradation Biological and medical sciences Cell Membrane - metabolism Cellular biology Conformational dynamics in molecular biology Enzymes Fundamental and applied biological sciences. Psychology Fungal Proteins - genetics Fungal Proteins - metabolism Humanities and Social Sciences letter Lipids Membranes Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Molecular biophysics Molecular Sequence Data Molecules multidisciplinary phosphatidylethanolamine Phosphatidylethanolamines - metabolism Proteins Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Science Science (multidisciplinary) ubiquitin Ubiquitin-Conjugating Enzymes Ubiquitins - metabolism Yeasts
Title	A ubiquitin-like system mediates protein lipidation
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