Falcon (Edison) deep research synthesis for S. pombe atg16 (O94656 / SPBC405.05)
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Atg16 is the scaffold subunit of the Atg12-Atg5-Atg16 E3-like complex that promotes
Atg8 conjugation to phosphatidylethanolamine and helps determine where Atg8 lipidation
occurs on autophagic membranes; it is not itself the catalytic enzyme.
"Atg16 is the scaffold subunit of the **Atg12–Atg5–Atg16** complex, which functions as the **E3-like factor for Atg8 conjugation to phosphatidylethanolamine (PE)** and helps determine where Atg8 lipidation occurs on autophagic membranes."
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Atg16 functions as a scaffolding/targeting subunit that organizes the E3-like
machinery on the correct membrane surface rather than acting as a catalytic enzyme.
"**Atg16 is not the catalytic enzyme**, but a scaffolding/targeting subunit critical for organizing the E3-like machinery on the correct membrane surface"
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In S. pombe, Atg16 co-immunoprecipitates with Atg5 in both wild-type and atg12-deletion
cells, indicating Atg5 binding does not strictly require Atg12 conjugation.
"co-immunoprecipitation detected the Atg5–Atg16 interaction **both in wild type and atg12Δ cells**, indicating Atg5 binding does not strictly require Atg12"
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Atg18a is uniquely required to target the Atg12-Atg5-Atg16 complex to the PAS; this
is a distinctive fission-yeast feature with non-redundant Atg18 paralogs.
"Atg18a is uniquely required to target the Atg12–Atg5·Atg16 complex to the PAS"
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Atg16 localizes to the PAS (phagophore assembly site / pre-autophagosomal structure)
during starvation and colocalizes with CFP-Atg8.
"Atg16 localizes to the **PAS (phagophore assembly site / pre-autophagosomal structure)** during starvation and colocalizes with **CFP-Atg8**"
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Atg16 contains an N-terminal Atg5-binding region and a C-terminal coiled-coil domain.
"**N-terminal Atg5-binding region** plus a **C-terminal coiled-coil domain**"
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atg16-deletion cells are defective in CFP-Atg8 processing under nitrogen starvation,
a bulk-autophagy flux readout.
"**atg16Δ** cells are defective in CFP-Atg8 processing under nitrogen starvation"