Abstract:
:Atg13 is an essential subunit of the Atg1 autophagy initiation complex in yeast and its mammalian counterpart, ATG13, is indispensable for autophagy induction by the ULK1 complex. The N terminus of the protein folds into a HORMA domain, an architecture that has been revealed by crystallography. 1-4 In human cells, the ATG13 HORMA domain interacts directly with ATG14, a subunit of the class III phosphatidylinositol 3-kinase complex. 5 In budding yeast, the HORMA domain of Atg13 recruits Atg14, but a direct interaction remains to be proven. 1 The amino acid sequence that follows the HORMA domain does not adopt any 3-dimensional structure on its own; therefore, it is termed an intrinsically disordered region (IDR). Here we discuss the results of 2 recent studies in light of previous reports on Atg13 from yeast. Together, they yield an insight into the molecular mechanism for the function of this intriguing protein, and reveal why Atg13, as well as the mammalian homolog ATG13, cannot have a structurally rigid architecture.
journal_name
Autophagyjournal_title
Autophagyauthors
Popelka H,Klionsky DJdoi
10.1080/15548627.2016.1277312subject
Has Abstractpub_date
2017-03-04 00:00:00pages
449-451issue
3eissn
1554-8627issn
1554-8635journal_volume
13pub_type
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