Abstract:
:The Atg20 and Snx4/Atg24 proteins have been identified in a screen for mutants defective in a type of selective macroautophagy/autophagy. Both proteins are connected to the Atg1 kinase complex, which is involved in autophagy initiation, and bind phosphatidylinositol-3-phosphate. Atg20 and Snx4 contain putative BAR domains, suggesting a possible role in membrane deformation, but they have been relatively uncharacterized. Here we demonstrate that, in addition to its function in selective autophagy, Atg20 plays a critical role in the efficient induction of nonselective autophagy. Atg20 is a dynamic posttranslationally modified protein that engages both structurally stable (PX and BAR) and intrinsically disordered domains for its function. In addition to its PX and BAR domains, Atg20 uses a third membrane-binding module, a membrane-inducible amphipathic helix present in a previously undescribed location in Atg20 within the putative BAR domain. Taken together, these findings yield insights into the molecular mechanism of the autophagy machinery.
journal_name
Proc Natl Acad Sci U S Aauthors
Popelka H,Damasio A,Hinshaw JE,Klionsky DJ,Ragusa MJdoi
10.1073/pnas.1708367114subject
Has Abstractpub_date
2017-11-21 00:00:00pages
E10112-E10121issue
47eissn
0027-8424issn
1091-6490pii
1708367114journal_volume
114pub_type
杂志文章abstract::A simple model is described for calculating the electrostatic energy of lipid domains at the air-water interface, taking account of dipole-dipole repulsions between the lipid molecules themselves, as well as interactions between the molecular dipoles and image dipoles in the subphase. The model assumes that the molecu...
journal_title:Proceedings of the National Academy of Sciences of the United States of America
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doi:10.1073/pnas.92.19.8823
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