Atg101: Not Just an Accessory Subunit in the Autophagy-initiation Complex

Access this Article

Author(s)

Abstract

The <i>Saccharomyces cerevisiae</i> 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, <i>S. cerevisiae</i> 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.

Journal

  • Cell Structure and Function

    Cell Structure and Function 41(1), 13-20, 2016

    Japan Society for Cell Biology

Codes

  • NII Article ID (NAID)
    130005126756
  • NII NACSIS-CAT ID (NCID)
    AA0060007X
  • Text Lang
    ENG
  • ISSN
    0386-7196
  • NDL Article ID
    028100137
  • NDL Call No.
    Z53-V38
  • Data Source
    NDL  J-STAGE 
Page Top