ArticleThe Journal of biological chemistry2011
An Atg13 protein-mediated self-association of the Atg1 protein kinase is important for the induction of autophagy.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 56 citations in OpenAlex.
- Atg23 prevents aberrant fusion of Atg9 vesicles during delivery to autophagosome formation sites.The EMBO journal · 2026Article
- The Role of Sigmar1 in Autophagy Regulation and Disease Therapy.International journal of molecular sciences · 2026Review
- The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Recruitment of Atg1 to the phagophore by Atg8 orchestrates autophagy machineries.Nature structural & molecular biology · 2025Article
- Structure and activation of the human autophagy-initiating ULK1C:PI3KC3-C1 supercomplex.Nature structural & molecular biology · 2025Article
- The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025Review
- Article
- The Multifaceted Interactions ofCells · 2024Article
- Article
- Cdc14 spatiotemporally dephosphorylates Atg13 to activate autophagy during meiotic divisions.The Journal of cell biology · 2022Article
- Article
- Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation.eLife · 2020Article
- Recruitment and Activation of the ULK1/Atg1 Kinase Complex in Selective Autophagy.Journal of molecular biology · 2020Review
- Mechanistic Insights into the Role of Atg11 in Selective Autophagy.Journal of molecular biology · 2020Review
- Article
- Autophagy plays an essential role in bone homeostasis.Journal of cellular physiology · 2019Review
- PP2C phosphatases promote autophagy by dephosphorylation of the Atg1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The dynamic Atg13-free conformation of the Atg1 EAT domain is required for phagophore expansion.Molecular biology of the cell · 2018Article
- Understanding and exploiting autophagy signaling in plants.Essays in biochemistry · 2017Review
- Proteins interacting with CreA and CreB in the carbon catabolite repression network in Aspergillus nidulans.Current genetics · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Autophagy pathways in eukaryotic cells mediate the turnover of a diverse set of cytoplasmic components, including damaged organelles and abnormal protein aggregates. Autophagy-mediated degradation is highly regulated, and defects in these pathways have been linked to a number of human disorders. The Atg1 protein kinase appears to be a key site of this control and is targeted by multiple signaling pathways to ensure the appropriate autophagic response to changing environmental conditions. Despite the importance of this kinase, relatively little is known about the molecular details of Atg1 activation. In this study we show that Atg13, an evolutionarily conserved regulator of Atg1, promotes the formation of a specific Atg1 self-interaction in the budding yeast, Saccharomyces cerevisiae. The appearance of this Atg1-Atg1 complex is correlated with the induction of autophagy, and conditions that disrupt this complex result in diminished levels of both autophagy and Atg1 kinase activity. Moreover, the addition of a heterologous dimerization domain to Atg1 resulted in elevated kinase activity both in vivo and in vitro. The formation of this complex appears to be an important prerequisite for the subsequent autophosphorylation of Thr-226 in the Atg1 activation loop. Previous work indicates that this modification is necessary and perhaps sufficient for Atg1 kinase activity. Interestingly, this Atg1 self-association does not require Atg17, suggesting that this second conserved regulator might activate Atg1 in a manner mechanistically distinct from that of Atg13. In all, this work suggests a model whereby this self-association stimulates the autophosphorylation of Atg1 within its activation loop.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.