Atg13 is an essential regulatory scaffolding protein in the autophagy initiation complex in S. pombe. It contains an N-terminal HORMA domain that stabilizes through heterodimerization with Atg101, and a C-terminal intrinsically disordered region (IDR) that mediates multivalent interactions with Atg1, Atg17, and other autophagy factors. The protein serves as a molecular hub that bridges the Atg1 serine/threonine kinase to the Atg17 scaffold, enabling formation of the Atg1/ULK1 kinase complex. Atg13 is regulated by phosphorylation; under nutrient-rich conditions it is hyperphosphorylated by TOR, suppressing autophagy, while nitrogen starvation leads to dephosphorylation and autophagy induction. The HORMA domain recruits Atg9 vesicles to the phagophore assembly site (PAS), which is critical for autophagosome formation. Atg13 is required for macroautophagy, mitophagy, and normal sporulation under nitrogen starvation conditions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0019887 protein kinase regulator activity | IBA GO_REF:0000033 | MODIFY | Summary: This IBA annotation, phylogenetically inferred from S. cerevisiae Atg13, attributes "protein kinase regulator activity" to Atg13. In budding yeast and mammals, binding of dephosphorylated Atg13 to Atg1/ULK1 enhances kinase activity. However, fission-yeast-specific experimental data complicate this picture: Pan et al. (2020) showed that in S. pombe Atg1 kinase activity requires Atg11 (FIP200 ortholog) and does NOT require Atg13, Atg17, or Atg101. Thus in S. pombe Atg13 acts primarily as a scaffold/adaptor that organizes the Atg1 complex (bridging Atg1 to the Atg17 scaffold) rather than as an obligate Atg1-kinase activator. Reason: The falcon deep research and the underlying primary study (Pan et al. 2020, PMID:32909946) directly contradict the "kinase activator" reading of this term for S. pombe: Atg1 autophosphorylation persists in atg13-delta cells, and Atg11-mediated dimerization / cis-autophosphorylation, not Atg13 binding, drives Atg1 activation. The phylogenetic (IBA) inference from S. cerevisiae does not hold at the mechanistic level in fission yeast. Atg13's actual S. pombe molecular function is best captured as a molecular adaptor/scaffold that organizes the Atg1 initiation complex, so "molecular adaptor activity" (GO:0060090) is proposed as a more accurate replacement. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:28976798 Atg101 interacts with the HORMA domain of Atg13 and this enhances the stability of both proteins PMID:32909946 does not require Atg13, Atg17, or Atg101 file:SCHPO/atg13/atg13-deep-research-falcon.md Atg11** (FIP200 ortholog) rather than Atg13 is emphasized as required for normal Atg1 kinase activity file:SCHPO/atg13/atg13-deep-research-falcon.md it is primarily a **scaffold/adaptor protein** within the Atg1 initiation machinery. In fission yeast, Atg13 is described as a subunit of the Atg1 kinase complex and directly interacts with Atg1 and Atg17, supporting assembly/organization of the initiation complex |
| GO:0005776 autophagosome | IBA GO_REF:0000033 | ACCEPT | Summary: Atg13 is a core component of the autophagy initiation machinery and localizes to autophagosomes during their formation. The IBA annotation is supported by phylogenetic inference from orthologs across eukaryotes. Reason: Atg13 is recruited to the phagophore assembly site (PAS) where autophagosomes form. While the primary localization evidence in S. pombe is for the PAS (IDA), the autophagosome annotation is reasonable as Atg13 is present during autophagosome biogenesis. The IBA inference from multiple species including CGD and TAIR supports this conserved localization. Supporting Evidence: GO_REF:0000033 IBA annotation inferred from CGD:CAL0000176796, PANTHER:PTN001268151, TAIR:locus:2114623 |
| GO:0000407 phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: Atg13 localizes to the phagophore assembly site (PAS), a discrete cytoplasmic structure where autophagosome biogenesis is initiated. This IBA annotation is strongly supported by direct experimental evidence in S. pombe. Reason: This is a core localization for Atg13. Direct experimental evidence (IDA) in S. pombe confirms PAS localization (PMID:23950735, PMID:31941401). The IBA annotation is redundant with the IDA evidence but validates the phylogenetic conservation of this localization. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Under starvation conditions, Atg13 is recruited from a diffuse cytoplasmic distribution to discrete punctate structures that correspond to the phagophore assembly site (PAS) |
| GO:0000423 mitophagy | IBA GO_REF:0000033 | ACCEPT | Summary: Atg13 is involved in mitophagy (selective autophagy of mitochondria). This is supported by both phylogenetic inference (IBA) and direct experimental evidence (IMP) in S. pombe from PMID:27737912. Reason: Mitophagy is a core function of the autophagy machinery, and Atg13 is required for this process. The IBA annotation is validated by IMP evidence in S. pombe showing that Atg13 is required for autophagy of mitochondria under nitrogen starvation conditions. Supporting Evidence: PMID:27737912 in a distantly related fungal organism, the fission yeast Schizosaccharomyces pombe, autophagy of ER and mitochondria is induced by nitrogen starvation and is promoted by three Atg20- and Atg24-family proteins |
| GO:1990316 Atg1/ULK1 kinase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Atg13 is a core subunit of the Atg1/ULK1 kinase complex. This IBA annotation is strongly supported by direct experimental evidence (EXP) in S. pombe. Reason: This is a fundamental property of Atg13. The S. pombe Atg1 complex contains Atg1, Atg13, Atg17, and Atg101. Multiple experimental studies confirm Atg13 as a core component. The IBA annotation is validated by EXP evidence from PMID:34499173 and by structural studies (PMID:26030876, PMID:28976798). Supporting Evidence: PMID:28976798 Although the human ULK complex mediates phagophore initiation similar to the budding yeast Saccharomyces cerevisiae Atg1 complex, this complex contains ATG101 but not Atg29 and Atg31 PMID:26030876 Atg101 is an essential component of the autophagy-initiating ULK complex in higher eukaryotes PMID:35406650 pombe Atg1 complex has Atg1, Atg13, Atg17, and Atg11 subunits. file:SCHPO/atg13/atg13-deep-research-falcon.md the canonical core composition is described as **Atg1, Atg13, Atg17, and Atg11**, with **Atg101** as an additional Atg13-binding subunit that stabilizes Atg13 |
| GO:0034727 piecemeal microautophagy of the nucleus | IBA GO_REF:0000033 | UNDECIDED | Summary: This IBA annotation infers involvement in piecemeal microautophagy of the nucleus (PMN) from S. cerevisiae Atg13, where this process is well characterized. Reason: Piecemeal microautophagy of the nucleus (PMN) has been primarily characterized in S. cerevisiae. While the autophagy machinery is conserved, there is no direct evidence that this specific process occurs in S. pombe or that Atg13 is required for it in fission yeast. The IBA inference may be valid, but specific experimental validation in S. pombe is lacking. Supporting Evidence: GO_REF:0000033 IBA annotation inferred from PANTHER:PTN001268151 and SGD:S000006389 |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: Atg13 localizes to the cytosol under non-starving conditions, from which it is recruited to the PAS upon starvation. This is supported by HDA evidence from the S. pombe ORFeome localization study. Reason: Cytosolic localization is well supported. The deep research indicates that under starvation conditions, Atg13 is recruited from a diffuse cytoplasmic distribution to discrete punctate structures. The IBA is validated by HDA evidence from PMID:16823372. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Under starvation conditions, Atg13 is recruited from a diffuse cytoplasmic distribution to discrete punctate structures |
| GO:0034497 protein localization to phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: Atg13 plays a critical role in recruiting proteins to the phagophore assembly site. The HORMA domain of Atg13 is essential for recruiting Atg9 vesicles to the PAS, and Atg13 itself serves as a tethering point for other Atg proteins. Reason: This is a core function of Atg13. The deep research extensively documents that Atg13 is the primary determinant of Atg9 vesicle recruitment to the PAS and that it serves as a tethering point for other Atg proteins. The HORMA domain directly recruits Atg9 vesicles, and the C-terminal IDR mediates recruitment to Atg17. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md The N-terminal HORMA domain of Atg13 has been identified as the critical determinant for recruitment of Atg9 vesicles to the phagophore assembly site |
| GO:0000045 autophagosome assembly | IEA GO_REF:0000002 | ACCEPT | Summary: Atg13 is essential for autophagosome assembly as a core component of the autophagy initiation complex. This IEA annotation is derived from InterPro domain mapping (IPR040182). Reason: Autophagosome assembly is a core function of Atg13. The protein is essential for nucleating the autophagy initiation machinery at the PAS and for subsequent autophagosome formation. This IEA annotation is supported by IMP and ISO evidence for macroautophagy in S. pombe. Supporting Evidence: GO_REF:0000002 Gene Ontology annotation through association of InterPro records with GO terms |
| GO:0000407 phagophore assembly site | IEA GO_REF:0000120 | ACCEPT | Summary: This IEA annotation for PAS localization is derived from automated annotation pipelines. It is redundant with the IBA and IDA annotations for the same term. Reason: This annotation is correct but redundant with stronger IBA and IDA evidence for PAS localization. The automated annotation correctly captures this core localization of Atg13. Supporting Evidence: GO_REF:0000120 Combined Automated Annotation using Multiple IEA Methods |
| GO:0000422 autophagy of mitochondrion | IEA GO_REF:0000117 | ACCEPT | Summary: This IEA annotation for mitochondrial autophagy is derived from ARBA machine learning. It is essentially equivalent to the IBA and IMP annotations for mitophagy (GO:0000423). Reason: GO:0000422 (autophagy of mitochondrion) and GO:0000423 (mitophagy) are related terms. This annotation is consistent with the experimental evidence for Atg13's role in mitophagy from PMID:27737912. Supporting Evidence: GO_REF:0000117 Electronic Gene Ontology annotations created by ARBA machine learning models |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Atg13 is a cytoplasmic protein that localizes to the cytosol and is recruited to the PAS upon starvation. This IEA annotation is derived from UniProtKB subcellular location mapping. Reason: Cytoplasmic localization is accurate and supported by HDA evidence from PMID:16823372. This is a broader term than cytosol but correctly captures the general localization of Atg13. Supporting Evidence: GO_REF:0000044 Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping |
| GO:0006914 autophagy | IEA GO_REF:0000120 | ACCEPT | Summary: Atg13 is a core autophagy protein. This general autophagy annotation is derived from InterPro domain and UniProtKB keyword mapping. Reason: Autophagy is the fundamental biological process in which Atg13 functions. While more specific annotations (macroautophagy, mitophagy) exist with experimental evidence, this general term is also appropriate. The annotation correctly captures Atg13's central role in autophagy. Supporting Evidence: GO_REF:0000120 Combined Automated Annotation using Multiple IEA Methods |
| GO:0015031 protein transport | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: This annotation is derived from the UniProtKB keyword "Protein transport." While Atg13 is involved in recruiting proteins to the PAS, this term is overly general and does not capture the specific autophagy-related function. Reason: Atg13 does facilitate protein transport to the PAS and helps recruit Atg9 vesicles, but "protein transport" is too broad and does not accurately convey the autophagy-specific function. More specific terms like "protein localization to phagophore assembly site" (GO:0034497) better describe this role. However, the term is not incorrect per se. Supporting Evidence: GO_REF:0000043 Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping |
| GO:0016236 macroautophagy | IEA GO_REF:0000117 | ACCEPT | Summary: Atg13 is essential for macroautophagy. This IEA annotation is derived from ARBA and is supported by IMP evidence in S. pombe. Reason: Macroautophagy is a core function of Atg13. This IEA annotation is validated by IMP evidence from multiple publications including PMID:19778961 and PMID:23950735, which demonstrate that atg13 deletion impairs autophagy. Supporting Evidence: GO_REF:0000117 Electronic Gene Ontology annotations created by ARBA machine learning models |
| GO:0030435 sporulation resulting in formation of a cellular spore | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: This annotation is derived from the UniProtKB keyword "Sporulation." Atg13 is required for normal sporulation under nitrogen starvation, but this is an indirect effect of its autophagy function rather than a direct role in sporulation machinery. Reason: Autophagy is induced during nitrogen starvation to provide nitrogen for sporulation. Autophagy-deficient mutants undergo partial sporulation and autophagy supplies nitrogen for cellular adaptation including sporulation. The UniProt entry notes that atg13 is also required for glycogen storage during stationary phase and has a role in meiosis and sporulation. This is a secondary/pleiotropic effect of autophagy function, not a direct role in sporulation. Supporting Evidence: PMID:19778961 fission yeast may store sufficient intracellular nitrogen to allow partial sporulation under nitrogen-limiting conditions, although the majority of the nitrogen source is supplied by autophagy GO_REF:0000043 Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping |
| GO:0051321 meiotic cell cycle | IEA GO_REF:0000043 | REMOVE | Summary: This annotation is derived from the UniProtKB keyword "Meiosis." The gene was originally identified as mug78 (meiotically up-regulated gene 78). However, Atg13 is autophagy machinery, not meiotic machinery - it is upregulated during meiosis because autophagy is induced during the nitrogen starvation that triggers meiosis/sporulation. Reason: This is a clear over-annotation resulting from keyword mapping. Atg13 is an autophagy protein, not a meiotic cell cycle regulator. The gene name mug78 reflects its upregulation during meiosis, but this upregulation occurs because autophagy is induced during the nitrogen starvation that precedes meiosis/sporulation. The protein does not directly regulate the meiotic cell cycle - it provides recycled nutrients through autophagy that support the energy-intensive meiosis/sporulation process. The SPKW-to-GO mapping incorrectly conflates correlation with causation. Supporting Evidence: PMID:19778961 In budding yeast, autophagy-deficient mutants are known to be sterile, whereas in fission yeast we found that up to 30 % of autophagy-defective cells with amino acid auxotrophy were able to recover sporulation when an excess of required amino acids was supplied |
| GO:1990316 Atg1/ULK1 kinase complex | IEA GO_REF:0000120 | ACCEPT | Summary: This IEA annotation for Atg1/ULK1 kinase complex membership is redundant with the IBA and EXP annotations for the same term. Reason: This annotation is correct but redundant with stronger IBA and EXP evidence. Atg13 is unambiguously a core subunit of the Atg1 complex in S. pombe. Supporting Evidence: GO_REF:0000120 Combined Automated Annotation using Multiple IEA Methods |
| GO:0005515 protein binding | IPI PMID:26030876 Structure of the Atg101-Atg13 complex reveals essential role... | MODIFY | Summary: This IPI annotation indicates that Atg13 binds Atg101 (O13978), as demonstrated by the crystal structure of the Atg101-Atg13 complex. Reason: While the protein-protein interaction is experimentally validated, "protein binding" is an uninformative term that does not capture the specific nature of the interaction. The interaction with Atg101 via HORMA domain heterodimer formation is functionally important for stabilizing both proteins. A more specific term would better capture this regulatory interaction. Proposed replacements: protein-containing complex binding Supporting Evidence: PMID:26030876 Atg13 HORMA from higher eukaryotes possesses an inherently unstable fold, which is stabilized by Atg101 via interactions analogous to those between O-Mad2 and C-Mad2 |
| GO:0042594 response to starvation | NAS PMID:34499173 Visual detection of binary, ternary and quaternary protein i... | ACCEPT | Summary: Atg13 functions in the cellular response to nitrogen starvation by enabling autophagy induction. The NAS (non-traceable author statement) annotation from ComplexPortal reflects this role. Reason: Atg13 is dephosphorylated in response to nitrogen starvation, leading to assembly of the active Atg1 complex and autophagy induction. This is a core function. Autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen, thus ensuring that they can adapt and subsequently propagate PMID:35406650 fission yeast atg1, atg8, and atg13 deletion mutants lose viability during nitrogen starvation and exhibit a mating defect |
| GO:0000045 autophagosome assembly | ISO GO_REF:0000024 | ACCEPT | Summary: This ISO annotation for autophagosome assembly is derived from manual transfer from S. cerevisiae Atg13 (SGD:S000006389). Reason: Autophagosome assembly is a core function of Atg13. The ISO annotation from S. cerevisiae is appropriate given the high conservation of the autophagy machinery between these yeasts. This is supported by IMP evidence for macroautophagy in S. pombe. Supporting Evidence: GO_REF:0000024 Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity |
| GO:1990316 Atg1/ULK1 kinase complex | EXP PMID:34499173 Visual detection of binary, ternary and quaternary protein i... | ACCEPT | Summary: This EXP annotation provides direct experimental evidence that Atg13 is a component of the Atg1 kinase complex in S. pombe. Reason: This is the highest-quality evidence for Atg13's membership in the Atg1 complex. The Pil1 co-tethering assay and other interaction studies confirm that Atg13 directly interacts with Atg1 and Atg17 as part of this complex. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md The S. pombe Atg1 complex contains Atg1, Atg13, Atg17, and Atg101 PMID:35406650 the Atg1 complex functioning in bulk autophagy is composed of Atg1 serine/threonine protein kinase, the scaffold protein Atg13 file:SCHPO/atg13/atg13-deep-research-falcon.md directly interacts with Atg1 and Atg17, supporting assembly/organization of the initiation complex |
| GO:0000407 phagophore assembly site | IDA PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | ACCEPT | Summary: Direct experimental evidence demonstrates that Atg13 localizes to the phagophore assembly site (PAS) in S. pombe. Reason: This IDA annotation provides strong direct evidence for PAS localization of Atg13. The study used fluorescence microscopy to demonstrate PAS localization in the context of the Atg38-Atg8 feedback loop study. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Atg13 is recruited to the PAS early in the autophagy response through its interaction with Atg17, which is already present at the PAS even under nutrient-rich conditions file:SCHPO/atg13/atg13-deep-research-falcon.md Atg13 acts at the **autophagy initiation site** (often referred to as the phagophore assembly site, PAS) as a core component of the Atg1 complex architecture |
| GO:0000423 mitophagy | IMP PMID:27737912 Atg20- and Atg24-family proteins promote organelle autophagy... | ACCEPT | Summary: This IMP annotation demonstrates that Atg13 is required for mitophagy in S. pombe based on mutant phenotype analysis. Reason: Direct experimental evidence shows that Atg13 is required for selective autophagy of mitochondria (mitophagy) under nitrogen starvation conditions. This is a core function of the autophagy machinery. Supporting Evidence: PMID:27737912 in a distantly related fungal organism, the fission yeast Schizosaccharomyces pombe, autophagy of ER and mitochondria is induced by nitrogen starvation and is promoted by three Atg20- and Atg24-family proteins |
| GO:0005515 protein binding | IPI PMID:28976798 Conserved and unique features of the fission yeast core Atg1... | MODIFY | Summary: This IPI annotation indicates that Atg13 binds Atg1 (SPAC10F6.11c), Atg101 (SPAC25H1.03), itself (SPAC4F10.07c), and Atg17 (SPCC63.08c) based on coprecipitation experiments. Reason: While these protein-protein interactions are experimentally validated and functionally important, "protein binding" is an uninformative term. The study demonstrates specific interactions between Atg1 complex subunits. More informative terms would better capture the functional significance. Proposed replacements: protein-containing complex binding Supporting Evidence: PMID:28976798 Our pairwise coprecipitation experiments showed that while the interactions between Atg1, Atg13, and Atg17 are conserved, Atg101 does not bind Atg17 |
| GO:0016236 macroautophagy | IMP PMID:19778961 Autophagy-deficient Schizosaccharomyces pombe mutants underg... | ACCEPT | Summary: This IMP annotation demonstrates that Atg13 is required for macroautophagy in S. pombe. Deletion of atg13 results in autophagy defects and partial sporulation under nitrogen starvation. Reason: Direct experimental evidence shows that atg13 deletion impairs macroautophagy. The study found that autophagy-deficient S. pombe mutants undergo partial sporulation during nitrogen starvation. This is a core function of Atg13. Supporting Evidence: PMID:19778961 Using this marker, 13 Atg homologues were also found to be required for autophagy in fission yeast |
| GO:0000407 phagophore assembly site | IDA PMID:23950735 Global analysis of fission yeast mating genes reveals new au... | ACCEPT | Summary: Direct experimental evidence demonstrates PAS localization of Atg13 in S. pombe through the global analysis of mating genes. Reason: This IDA annotation provides direct evidence for Atg13 localization to the PAS. The study identified atg13 among genes required for autophagy and demonstrated its PAS localization. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Atg13 localizes to the phagophore assembly site (PAS), a discrete cytoplasmic location where autophagosome biogenesis is initiated |
| GO:0016236 macroautophagy | IMP PMID:23950735 Global analysis of fission yeast mating genes reveals new au... | ACCEPT | Summary: This IMP annotation demonstrates that Atg13 is required for macroautophagy based on mutant phenotype analysis from the global fission yeast screen. Reason: Direct experimental evidence confirms that atg13 is required for macroautophagy in S. pombe. The deletion of atg13 impairs Atg8 processing, a marker for autophagy. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Atg13 is essential for autophagosome assembly as a core component of the autophagy initiation complex |
| GO:0005737 cytoplasm | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: High-throughput localization study in S. pombe demonstrates cytoplasmic localization of Atg13. Reason: The ORFeome localization study provides direct evidence for cytoplasmic localization of Atg13. This is consistent with its role as a cytosolic protein that is recruited to the PAS upon starvation. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Under starvation conditions, Atg13 is recruited from a diffuse cytoplasmic distribution to discrete punctate structures |
| GO:0005829 cytosol | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: High-throughput localization study demonstrates cytosolic localization of Atg13 in S. pombe. Reason: The ORFeome study provides direct evidence for cytosolic localization. Under non-starving conditions, Atg13 has a diffuse cytoplasmic/cytosolic distribution before being recruited to the PAS upon starvation. Supporting Evidence: file:SCHPO/atg13/atg13-deep-research-perplexity.md Under starvation conditions, Atg13 is recruited from a diffuse cytoplasmic distribution to discrete punctate structures |
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Download this section (compressed HTML)Q: Does S. pombe undergo piecemeal microautophagy of the nucleus (PMN) similar to S. cerevisiae, and if so, is Atg13 required?
Q: Are there isoform-specific functions of Atg13 in S. pombe?
Q: What are the specific phosphorylation sites on S. pombe Atg13 that are regulated by TORC1?
Experiment: Systematic analysis of Atg13 phosphorylation sites in S. pombe using phosphoproteomics
Hypothesis: TORC1-regulated phosphorylation sites on Atg13 control autophagy induction
Experiment: Investigation of whether PMN occurs in S. pombe and the role of Atg13
Hypothesis: Piecemeal microautophagy of the nucleus may occur in S. pombe and require Atg13
Experiment: Structure determination of the complete S. pombe Atg1 complex to understand the architecture
Hypothesis: The complete Atg1 complex structure will reveal how Atg13 bridges Atg1 to the Atg17 scaffold
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