The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Several key reactions performed by these proteins have been described, but a comprehensive understanding of the overall network is still lacki...
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| Published in | The EMBO journal Vol. 20; no. 21; pp. 5971 - 5981 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
01.11.2001
Nature Publishing Group UK Springer Nature B.V Oxford University Press |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Several key reactions performed by these proteins have been described, but a comprehensive understanding of the overall network is still lacking. Based on Apg protein localization, we have identified a novel structure that functions in autophagosome formation. This pre‐autophagosomal structure, containing at least five Apg proteins, i.e. Apg1p, Apg2p, Apg5p, Aut7p/Apg8p and Apg16p, is localized in the vicinity of the vacuole. Analysis of
apg
mutants revealed that the formation of both a phosphatidylethanolamine‐conjugated Aut7p and an Apg12p–Apg5p conjugate is essential for the localization of Aut7p to the pre‐autophagosomal structure. Vps30p/Apg6p and Apg14p, components of an autophagy‐ specific phosphatidylinositol 3‐kinase complex, Apg9p and Apg16p are all required for the localization of Apg5p and Aut7p to the structure. The Apg1p protein kinase complex functions in the late stage of autophagosome formation. Here, we present the classification of Apg proteins into three groups that reflect each step of autophagosome formation. |
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| AbstractList | Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Several key reactions performed by these proteins have been described, but a comprehensive understanding of the overall network is still lacking. Based on Apg protein localization, we have identified a novel structure that functions in autophagosome formation. This pre-autophagosomal structure, containing at least five Apg proteins, i.e. Apg1p, Apg2p, Apg5p, Aut7p/Apg8p and Apg16p, is localized in the vicinity of the vacuole. Analysis of apg mutants revealed that the formation of both a phosphatidylethanolamine-conjugated Aut7p and an Apg12p- Apg5p conjugate is essential for the localization of Aut7p to the pre- autophagosomal structure. Vps30p/Apg6p and Apg14p, components of an autophagy- specific phosphatidylinositol 3-kinase complex, Apg9p and Apg16p are all required for the localization of Apg5p and Aut7p to the structure. The Apg1p protein kinase complex functions in the late stage of autophagosome formation. Here, we present the classification of Apg proteins into three groups that reflect each step of autophagosome formation. Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Several key reactions performed by these proteins have been described, but a comprehensive understanding of the overall network is still lacking. Based on Apg protein localization, we have identified a novel structure that functions in autophagosome formation. This pre-autophagosomal structure, containing at least five Apg proteins, i.e. Apg1p, Apg2p, Apg5p, Aut7p/Apg8p and Apg16p, is localized in the vicinity of the vacuole. Analysis of apg mutants revealed that the formation of both a phosphatidylethanolamine-conjugated Aut7p and an Apg12p– Apg5p conjugate is essential for the localization of Aut7p to the pre-autophagosomal structure. Vps30p/Apg6p and Apg14p, components of an autophagy- specific phosphatidylinositol 3-kinase complex, Apg9p and Apg16p are all required for the localization of Apg5p and Aut7p to the structure. The Apg1p protein kinase complex functions in the late stage of autophagosome formation. Here, we present the classification of Apg proteins into three groups that reflect each step of autophagosome formation. Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Several key reactions performed by these proteins have been described, but a comprehensive understanding of the overall network is still lacking. Based on Apg protein localization, we have identified a novel structure that functions in autophagosome formation. This pre-autophagosomal structure, containing at least five Apg proteins, i.e. Apg1p, Apg2p, Apg5p, Aut7p/Apg8p and Apg16p, is localized in the vicinity of the vacuole. Analysis of apg mutants revealed that the formation of both a phosphatidylethanolamine-conjugated Aut7p and an Apg12p- Apg5p conjugate is essential for the localization of Aut7p to the pre-autophagosomal structure. Vps30p/Apg6p and Apg14p, components of an autophagy- specific phosphatidylinositol 3-kinase complex, Apg9p and Apg16p are all required for the localization of Apg5p and Aut7p to the structure. The Apg1p protein kinase complex functions in the late stage of autophagosome formation. Here, we present the classification of Apg proteins into three groups that reflect each step of autophagosome formation.Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Several key reactions performed by these proteins have been described, but a comprehensive understanding of the overall network is still lacking. Based on Apg protein localization, we have identified a novel structure that functions in autophagosome formation. This pre-autophagosomal structure, containing at least five Apg proteins, i.e. Apg1p, Apg2p, Apg5p, Aut7p/Apg8p and Apg16p, is localized in the vicinity of the vacuole. Analysis of apg mutants revealed that the formation of both a phosphatidylethanolamine-conjugated Aut7p and an Apg12p- Apg5p conjugate is essential for the localization of Aut7p to the pre-autophagosomal structure. Vps30p/Apg6p and Apg14p, components of an autophagy- specific phosphatidylinositol 3-kinase complex, Apg9p and Apg16p are all required for the localization of Apg5p and Aut7p to the structure. The Apg1p protein kinase complex functions in the late stage of autophagosome formation. Here, we present the classification of Apg proteins into three groups that reflect each step of autophagosome formation. |
| Author | Ohsumi, Yoshinori Noda, Takeshi Kamada, Yoshiaki Mizushima, Noboru Suzuki, Kuninori Kirisako, Takayoshi |
| AuthorAffiliation | 1 Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki 444-8585, 2 Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies and 3 PRESTO, Japan Science and Technology Corporation, Japan 4 Corresponding author e-mail: yohsumi@nibb.ac.jp |
| AuthorAffiliation_xml | – name: 1 Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki 444-8585, 2 Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies and 3 PRESTO, Japan Science and Technology Corporation, Japan 4 Corresponding author e-mail: yohsumi@nibb.ac.jp |
| Author_xml | – sequence: 1 givenname: Kuninori surname: Suzuki fullname: Suzuki, Kuninori organization: Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki, 444-8585, Japan – sequence: 2 givenname: Takayoshi surname: Kirisako fullname: Kirisako, Takayoshi organization: Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki, 444-8585, Japan – sequence: 3 givenname: Yoshiaki surname: Kamada fullname: Kamada, Yoshiaki organization: Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki, 444-8585, Japan – sequence: 4 givenname: Noboru surname: Mizushima fullname: Mizushima, Noboru organization: Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki, 444-8585, Japan – sequence: 5 givenname: Takeshi surname: Noda fullname: Noda, Takeshi organization: Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki, 444-8585, Japan – sequence: 6 givenname: Yoshinori surname: Ohsumi fullname: Ohsumi, Yoshinori email: yohsumi@nibb.ac.jp organization: Department of Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Myodaiji-cho, Okazaki, 444-8585, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11689437$$D View this record in MEDLINE/PubMed |
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| Title | The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation |
| URI | https://api.istex.fr/ark:/67375/WNG-QZ0819HP-B/fulltext.pdf https://link.springer.com/article/10.1093/emboj/20.21.5971 https://onlinelibrary.wiley.com/doi/abs/10.1093%2Femboj%2F20.21.5971 https://www.ncbi.nlm.nih.gov/pubmed/11689437 https://www.proquest.com/docview/195264546 https://www.proquest.com/docview/18124306 https://www.proquest.com/docview/49376453 https://www.proquest.com/docview/72252444 https://pubmed.ncbi.nlm.nih.gov/PMC125692 |
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