The Crystal Structure of Atg3, an Autophagy-related Ubiquitin Carrier Protein (E2) Enzyme that Mediates Atg8 Lipidation*
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Summary
The structure of Atg3 provides a molecular basis for understanding the unique lipidation reaction that Atg2 carries out and is reported here the crystal structure of Saccharomyces cerevisiae at 2.5-Å resolution.
- Type
- article
- Published
- 2007-03-16
- Cited by
- 148
- References
- 34
- Access
- Open access
- OpenAlex
- https://openalex.org/W1967413008
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:39186793
Keywords
ATG8, Lipid-anchored protein, Autophagy, Ubiquitin, ATG12
References
- NMRPipe: A multidimensional spectral processing system based on UNIX pipes
- The PyMOL Molecular Graphics System
- Three-dimensional structure of a ubiquitin-conjugating enzyme (E2).
- A ubiquitin-like system mediates protein lipidation
- The crystal structure of microtubule‐associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8
- Automated MAD and MIR structure solution
- Determinants of functionality in the ubiquitin conjugating enzyme family.
- Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import
- Escape of Intracellular Shigella from Autophagy
- The pre‐autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
- The ubiquitin system.
- A Giant Ubiquitin-conjugating Enzyme Related to IAP Apoptosis Inhibitors
- Crystallization and preliminary X-ray analysis of Atg3.
- The role of autophagy during the early neonatal starvation period
- Crystallography & NMR system: A new software suite for macromolecular structure determination.
- Loss of autophagy in the central nervous system causes neurodegeneration in mice
- Ubiquitin and ubiquitin-like proteins as multifunctional signals
- Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins.
- Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction.
- Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.
Cited by
- Role of Autophagy in the control of muscle mass
- Identification and characterization of the linear region of ATG3 that interacts with ATG7 in higher eukaryotes.
- The role of protein degradation in neuronal cell death
- The roles and regulation of ubiquitin/ubiquitin-like protein conjugation pathways in responses to oxidative stress in Schizosaccharomyces pombe
- Insights into membrane binding of PROPPINs and reconstitution of the mammalian autophagic conjugation systems.
- Depletion of autophagy-related genes ATG3 and ATG5 in Tenebrio molitor leads to decreased survivability against an intracellular pathogen, Listeria monocytogenes.
- Characterization of the ATG8-conjugation system in 2 Plasmodium species with special focus on the liver stage
- Posttranslationally-modified structures in the autophagy machinery: an integrative perspective
- Binding to E1 and E3 is mutually exclusive for the human autophagy E2 Atg3
- Protective effect of N-acetylcysteine against nicardipine hydrochloride-induced autophagic cell death of human vascular endothelial cells.
- New Targets for Acetylation in Autophagy
- Localization of Atg3 to autophagy‐related membranes and its enhancement by the Atg8‐family interacting motif to promote expansion of the membranes
- A PCR analysis of the ubiquitin-like conjugation systems in macroautophagy
- Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
- Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7–Atg3 and Atg7–Atg10 structures
- Clusterin facilitates stress-induced lipidation of LC3 and autophagosome biogenesis to enhance cancer cell survival
- Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast
- Autophagy in protists
- Autophagy-related Protein 8 (Atg8) Family Interacting Motif in Atg3 Mediates the Atg3-Atg8 Interaction and Is Crucial for the Cytoplasm-to-Vacuole Targeting Pathway*
- Structure of the autophagic E2 enzyme Atg10.
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