| http://purl.uniprot.org/citations/34193767 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34193767 | http://www.w3.org/2000/01/rdf-schema#comment | "Autophagy is an intracellular degradation system regulating cellular homeostasis. The two ubiquitin-like modification systems named the Atg8 system and the Atg12 system are essential for autophagy. Atg8 and Atg12 are ubiquitin-like proteins covalently conjugated with a phosphatidylethanolamine (PE) and Atg5, respectively, via enzymatic reactions. The Atg8-PE conjugate binds to autophagic membranes and recruits various proteins through direct interaction, whereas the Atg12-Atg5 conjugate recognizes Atg3, the E2 enzyme for Atg8, and facilitates Atg8-PE conjugation by functioning as the E3 enzyme. Although structural and biochemical analyses have well established the Atg8-family interacting motif (AIM), studies on the interacting sequence for Atg12 are rare (only one example for human ATG12-ATG3), thereby making it challenging to define a binding motif. Here we determined the crystal structure of the plant ATG12b as a complex with the ATG12b-binding region of ATG3 and revealed that ATG12b recognizes the aspartic acid (Asp)-methionine (Met) motif in ATG3 via a hydrophobic pocket and a basic residue, which we confirmed critical for the complex formation by mutational analysis. This recognition mode is similar to that reported between human ATG12 and ATG3, suggesting that the Asp-Met sequence is a conserved Atg12-interacting motif (AIM12). These data suggest that AIM12 mediates E2-E3 interaction during Atg8 lipidation and provide structural basis for developing chemicals that regulate autophagy by targeting Atg12-family proteins."xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.org/dc/terms/identifier | "doi:10.1248/bpb.b21-00439"xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/author | "Matoba K."xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/author | "Noda N.N."xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/name | "Biol Pharm Bull"xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/pages | "1337-1343"xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/title | "Atg12-Interacting Motif Is Crucial for E2-E3 Interaction in Plant Atg8 System."xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://purl.uniprot.org/core/volume | "44"xsd:string |
| http://purl.uniprot.org/citations/34193767 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/34193767 |
| http://purl.uniprot.org/citations/34193767 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/34193767 |
| http://purl.uniprot.org/uniprot/#_Q0WWQ1-mappedCitation-34193767 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/34193767 |
| http://purl.uniprot.org/uniprot/#_Q9LVK3-mappedCitation-34193767 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/34193767 |
| http://purl.uniprot.org/uniprot/Q9LVK3 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/34193767 |
| http://purl.uniprot.org/uniprot/Q0WWQ1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/34193767 |