Journal
CELL STRUCTURE AND FUNCTION
Volume 41, Issue 1, Pages 13-20Publisher
JAPAN SOC CELL BIOLOGY
DOI: 10.1247/csf.15013
Keywords
Autophagy; Atg101; Atg13; HORMA
Categories
Funding
- Japan Society for the Promotion of Science (JSPS) [25111001, 25111004, 25111005]
- CREST, Japan Science and Technology Agency
- Grants-in-Aid for Scientific Research [25111004, 25111001] Funding Source: KAKEN
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The Saccharomyces cerevisiae autophagy-initiation complex, Atg1 kinase complex, consists of Atg1, Atg13, Atg17, Atg29, and Atg31, while the corresponding complex in most other eukaryotes, including mammals, is composed of ULK1 (or ULK2), Atg13, FIP200 (also known as RB1CC1), and Atg101. ULKs are homologs of Atg1, and FIP200 is partially homologous to Atg17. However, the sequence of Atg101 is not similar to that of Atg29 or Atg31. Although Atg101 is essential for autophagy and widely conserved in eukaryotes, its precise function and structure have remained largely unknown. Now, structural and cell biological analysis of Atg101 together with its binding partner Atg13 reveal that Atg101 is required for stabilization of uncapped Atg13 in most eukaryotes and also for recruitment of downstream Atg proteins through the newly identified WF motif. By contrast, S. cerevisiae has stable capped Atg13, which does not require Atg101 for its stabilization. Possible roles for other binding partners such as Atg29, Atg31, and Atg28 in different organisms are also discussed.
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