Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Gene Ontology annotations Inferred by Curator (IC) using at least one Inferred by Sequence Similarity (ISS) annotation to support the inference
Combined Automated Annotation using Multiple IEA Methods
Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial sporulation during nitrogen starvation.
-
Confirms Atg2 is required for macroautophagy
"autophagy-defective cells were also able to sporulate when a prototrophic strain was subjected to nitrogen starvation"
-
Shows autophagy supplies nutrients for sporulation but is not essential for meiosis per se
"fission yeast may store sufficient intracellular nitrogen to allow partial sporulation"
Global analysis of fission yeast mating genes reveals new autophagy factors.
-
Identifies atg2 as essential autophagy factor
"genes involved in starvation response, sexual reproduction, and macroautophagy are significantly enriched"
-
Shows atg2 deletion causes long-lasting Atg8 puncta indicating autophagosome assembly defects
"we found that Atg8 puncta in atg2delta cells were also long-lasting structures"
-
Confirms Atg2 localization to PAS
"Ctl1 became largely restricted to PAS in starved atg1delta or atg2delta cells"
Atg2 mediates direct lipid transfer between membranes for autophagosome formation.
-
Crystal structure of S. pombe Atg2 N-terminal region at 2.7 angstroms
"the conserved amino-terminal region of Schizosaccharomyces pombe Atg2 includes a lipid-transfer-protein-like hydrophobic cavity"
-
Demonstrates Atg2 is a lipid transfer protein with hydrophobic cavity
"Atg2 acts as a lipid-transfer protein that supplies phospholipids for autophagosome formation"
-
Shows Atg2 tethers ER to phagophore and transfers phospholipids
"Atg2 physically links the edge of the expanding IM with the endoplasmic reticulum (ER), a role that is essential for autophagosome formation"
Atg38-Atg8 interaction in fission yeast establishes a positive feedback loop to promote autophagy.
-
Confirms Atg2 localization to PAS
"PAS accumulation of Atg2, Atg18b, Atg24b, Atg5, Atg16, and Atg8 reduced by the Atg38 AIM mutation"
-
Shows Atg2 accumulation at PAS is affected by Atg38-Atg8 interaction
"the Atg38-Atg8 interaction establishes a positive feedback loop between Atg8 and the PtdIns3K complex I"
Inter-organelle lipid transfer: a channel model for Vps13 and chorein-N motif proteins.
-
Reviews Atg2 as a bridge-like lipid transfer protein
"they are not shuttles but instead are bridges between membranes, with lipids traversing the cytosol via the hydrophobic channel"
-
Describes channel model for lipid transfer through hydrophobic groove
"They feature an extended channel, most likely lined with hydrophobic residues"
A conserved membrane curvature-generating protein is crucial for autophagosome formation in fission yeast.
-
Confirms Atg2 localization to phagophores
"more than 80% of phagophores marked by mCh-Atg8 or Atg2-tdT contained Rop1-mNG"
-
Shows Rop1 colocalizes with Atg2 at phagophore rims
"Rop1-mNG and mCh-Atg8 are simultaneously appearing on phagophores"
ATG2 is a triglyceride transfer protein.
-
Demonstrates ATG2 transfers triglycerides in addition to phospholipids
"the neutral lipid triacylglycerol is also rapidly transported, with kinetics similar to those of phospholipid transport"
-
Shows stable ATG2 binding to lipid droplet monolayers
"the tight binding of ATG2 specifically to monolayers via its collection of COOH-terminal amphipathic helices"
Deep research summary for S. pombe atg2
Falcon (Edison) deep research report for S. pombe atg2
-
S. pombe atg2Δ blocks starvation-induced bulk autophagy in the CFP-Atg8 processing assay, and atg2Δ cells accumulate abnormally numerous, long-lived Atg8 puncta, indicating a defect in phagophore/autophagosome biogenesis dynamics (Sun et al. 2013, PLoS Genetics).
"atg2Δ** mutants fail to show CFP-Atg8 processing under nitrogen starvation, indicating blocked autophagy flux"
-
Atg2 is required for retrograde recycling of Atg9 and Ctl1 from the PAS in starved cells; Atg9 and Ctl1 physically co-immunoprecipitate, placing Atg2 in the Atg9/Ctl1 trafficking module at the PAS (Sun et al. 2013, PLoS Genetics).
"Atg9 recycling from PAS requires Atg1 and Atg2"
-
High-resolution APEX2 electron microscopy in S. pombe localizes Atg2 specifically to the tips/rims of cup-shaped phagophores, with ~80% of open phagophores showing rim labeling (Wang et al. 2023, Nature Communications).
"Atg2-APEX2 electron-dense precipitate concentrates at the tips/rims** of cup-shaped phagophores"
-
The conserved functional model places ATG2/Atg2 as a rod-like, bridge-like lipid transfer protein acting at phagophore-ER membrane contact sites, cooperating with the Atg9 scramblase to supply and equilibrate lipids for phagophore expansion (Duarte & Reggiori 2023; Choi et al. 2024).
"ATG2/Atg2 is a rod-like, bridge-like lipid transfer protein** that operates at **phagophore–ER membrane contact sites**"
-
In S. pombe, the Atg18-family member Atg18a (not Atg2 itself) promotes PAS targeting of Atg2, consistent with PI3P recognition being delegated to the Atg18 partner (Xu & Du 2022, Cells review).
"Atg18a promotes PAS targeting of Atg2"
UniProt entry for S. pombe Atg2 (O94649)