ArticleAutophagy2011
The identification and analysis of phosphorylation sites on the Atg1 protein kinase.
Article in Autophagy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- NADCells · 2025Review
- Autophagy in Disease Onset and Progression.Aging and disease · 2024Review
- The crucial role of the regulatory mechanism of the Atg1/ULK1 complex in fungi.Frontiers in microbiology · 2022Review
- Review
- Autophagy and autophagy-related proteins in cancer.Molecular cancer · 2020Review
- Two distinct mechanisms target the autophagy-related E3 complex to the pre-autophagosomal structure.eLife · 2019Article
- PP2C phosphatases promote autophagy by dephosphorylation of the Atg1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dephosphorylation of the Atg1 kinase complex by type 2C protein phosphatases.Molecular & cellular oncology · 2019Article
- Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Phosphoproteome-based kinase activity profiling reveals the critical role of MAP2K2 and PLK1 in neuronal autophagy.Autophagy · 2017Article
- An overview of macroautophagy in yeast.Journal of molecular biology · 2016Review
- Post-translationally-modified structures in the autophagy machinery: an integrative perspective.The FEBS journal · 2015Review
- Analysis of phosphorylation sites on autophagy proteins.Protein & cell · 2015Article
- Atg1 family kinases in autophagy initiation.Cellular and molecular life sciences : CMLS · 2015Review
- Biochemical characterization of FIKK8--A unique protein kinase from the malaria parasite Plasmodium falciparum and other apicomplexans.Molecular and biochemical parasitology · 2015Article
- Molecular interactions of the Saccharomyces cerevisiae Atg1 complex provide insights into assembly and regulatory mechanisms.Autophagy · 2015Article
- Structural biology of the macroautophagy machinery.Frontiers in biology · 2014Article
- The PhosphoGRID Saccharomyces cerevisiae protein phosphorylation site database: version 2.0 update.Database : the journal of biological databases and curation · 2013Article
- An Atg13 protein-mediated self-association of the Atg1 protein kinase is important for the induction of autophagy.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Autophagy is a conserved, degradative process that has been implicated in a number of human diseases and is a potential target for therapeutic intervention. It is therefore important that we develop a thorough understanding of the mechanisms regulating this trafficking pathway. The Atg1 protein kinase is a key element of this control as a number of signaling pathways target this enzyme and its associated protein partners. These studies have established that Atg1 activities are controlled, at least in part, by protein phosphorylation. To further this understanding, we used a combined mass spectrometry and molecular biology approach to identify and characterize additional sites of phosphorylation in the Saccharomyces cerevisiae Atg1. Fifteen candidate sites of phosphorylation were identified, including nine that had not been noted previously. Interestingly, our data suggest that the phosphorylation at one of these sites, Ser-34, is inhibitory for both Atg1 kinase activity and autophagy. This site is located within a glycine-rich loop that is highly conserved in protein kinases. Phosphorylation at this position in several cyclin-dependent kinases has also been shown to result in diminished enzymatic activity. In addition, these studies identified Ser-390 as the site of autophosphorylation responsible for the anomalous migration exhibited by Atg1 on SDS-polyacrylamide gels. Finally, a mutational analysis suggested that a number of the sites identified here are important for full autophagy activity in vivo. In all, these studies identified a number of potential sites of regulation within Atg1 and will serve as a framework for future work with this enzyme.
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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.