PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23321721-7 2013 In yeast, membrane binding by Atg5 is not required for its recruitment to the phagophore assembly site (PAS) but is essential for efficient promotion of autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway at a stage preceding Atg8 lipidation and autophagosome closure. Aminosalicylic Acid 104-107 Atg5p Saccharomyces cerevisiae S288C 30-34 30810528-2 2019 Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine. Aminosalicylic Acid 110-113 Atg5p Saccharomyces cerevisiae S288C 79-83 30810528-2 2019 Previous studies in yeast revealed that the autophagy-related E3 complex Atg12-Atg5-Atg16 is recruited to the PAS via Atg16 interaction with Atg21, which binds phosphatidylinositol 3-phosphate (PI3P) produced at the PAS, to stimulate conjugation of the ubiquitin-like protein Atg8 to phosphatidylethanolamine. Aminosalicylic Acid 216-219 Atg5p Saccharomyces cerevisiae S288C 79-83 30810528-3 2019 Here, we discover a novel mechanism for the PAS targeting of Atg12-Atg5-Atg16, which is mediated by the interaction of Atg12 with the Atg1 kinase complex that serves as a scaffold for PAS organization. Aminosalicylic Acid 44-47 Atg5p Saccharomyces cerevisiae S288C 67-71 25500271-6 2015 It is involved in a step downstream of PAS (phagophore assembly site) scaffold assembly, and upstream of the recruitment of Atg1, Atg14, Atg5 and Atg8. Aminosalicylic Acid 39-42 Atg5p Saccharomyces cerevisiae S288C 137-141 30810528-3 2019 Here, we discover a novel mechanism for the PAS targeting of Atg12-Atg5-Atg16, which is mediated by the interaction of Atg12 with the Atg1 kinase complex that serves as a scaffold for PAS organization. Aminosalicylic Acid 184-187 Atg5p Saccharomyces cerevisiae S288C 67-71 30810528-4 2019 While autophagy is partially defective without one of these mechanisms, cells lacking both completely lose the PAS localization of Atg12-Atg5-Atg16 and show no autophagic activity. Aminosalicylic Acid 111-114 Atg5p Saccharomyces cerevisiae S288C 137-141 30810528-5 2019 As with the PI3P-dependent mechanism, Atg12-Atg5-Atg16 recruited via the Atg12-dependent mechanism stimulates Atg8 lipidation, but also has the specific function of facilitating PAS scaffold assembly. Aminosalicylic Acid 178-181 Atg5p Saccharomyces cerevisiae S288C 44-48