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| Content Provider | PubMed Central |
|---|---|
| Author | Zoltan, Metlagel Otomo, Chinatsu Takaesu, Giichi Otomo, Takanori |
| Abstract | Autophagy-related (ATG)12 is a ubiquitin-like protein essential to autophagy. It has been known for years that ATG12 is conjugated to the structural protein ATG5 and that the resulting protein–protein conjugate acts like an E3 enzyme that facilitates the attachment of the LC3 ubiquitin-like protein to a lipid molecule, phosphatidylethanolamine. However, the exact role of ATG12 in the E3 complex and the significance of ATG12 being a ubiquitin-like protein have remained elusive. We show that ATG12 binds to a short peptide region of the E2 enzyme ATG3 and describe the structural details of this interaction. This work establishes ATG12 as the ATG3 recruitment factor and explains how ATG12 uses its ubiquitin-like fold for binding to the ATG3 peptide. |
| Related Links | http://dx.doi.org/10.1073/pnas.1314755110 |
| Ending Page | 18849 |
| Page Count | 6 |
| Starting Page | 18844 |
| File Format | |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 47 |
| Volume Number | 110 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2013-11-19 |
| Access Restriction | Open |
| Rights Holder | National Academy of Sciences |
| Subject Keyword | General Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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