1. Phosphorylation of mitophagy and pexophagy receptors coordinates their interaction with Atg8 and Atg11
- Author
-
Sarah F. Burnett, Jean-Claude Farré, Aaron Burkenroad, and Suresh Subramani
- Subjects
Scaffold protein ,Saccharomyces cerevisiae Proteins ,Microtubule-associated protein ,ATG8 ,Molecular Sequence Data ,Vesicular Transport Proteins ,Autophagy-Related Proteins ,Receptors, Cytoplasmic and Nuclear ,Receptors, Cell Surface ,Plasma protein binding ,Saccharomyces cerevisiae ,Biology ,Biochemistry ,Pichia ,Gene Knockout Techniques ,Mitophagy ,Consensus Sequence ,Protein Interaction Mapping ,Genetics ,Autophagy ,Protein Interaction Domains and Motifs ,Amino Acid Sequence ,Phosphorylation ,Receptor ,Molecular Biology ,Binding Sites ,Sequence Homology, Amino Acid ,Scientific Reports ,Autophagy-Related Protein 8 Family ,Cell biology ,Microtubule-Associated Proteins ,Protein Processing, Post-Translational ,Protein Binding - Abstract
The selective autophagy receptors Atg19 and Atg32 interact with two proteins of the core autophagic machinery: the scaffold protein Atg11 and the ubiquitin-like protein Atg8. We found that the Pichia pastoris pexophagy receptor, Atg30, also interacts with Atg8. Both Atg30 and Atg32 interactions are regulated by phosphorylation close to Atg8-interaction motifs. Extending this finding to Saccharomyces cerevisiae, we confirmed phosphoregulation for the mitophagy and pexophagy receptors, Atg32 and Atg36. Each Atg30 molecule must interact with both Atg8 and Atg11 for full functionality, and these interactions occur independently and not simultaneously, but rather in random order. We present a common model for the phosphoregulation of selective autophagy receptors.
- Published
- 2013