The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans.
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The primary worm study establishes association of WDR-23 with CUL-4/DDB-1 and regulation of SKN-1 abundance and activity.
"WDR-23, which interacts with the
CUL-4/DDB-1 ubiquitin ligase"
Nuclear and cytoplasmic WDR-23 isoforms mediate differential effects on GEN-1 and SKN-1 substrates.
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Primary worm isoform experiments show that compartment and regulatory outcome cannot be assigned independently of the N terminus.
"These opposing roles are mediated by two distinct isoforms: WDR-23A
in the cytoplasm and WDR-23B in the nucleus."
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The primary study identifies GEN-1 as a WDR-23 substrate; its DNA repair role does not make WDR-23 a nuclease.
"we identify
GEN-1, a Holliday junction resolvase, as an evolutionarily conserved WDR-23
substrate"
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The tested alternative N termini permit GEN-1 interaction, supporting a shared substrate-binding mechanism without establishing localization of the shorter target.
"the N-terminal domain of WDR-23B that mediates nuclear localization does not interfere with binding of GEN-1 in vitro."
WDR-23 exact-product sequence and repeat conservation
Reproducible comparison against the independently retrieved WDR-23B sequence
UniProt identification of the ribosome-related prediction donor
Frozen exact-input ProtNLM output and UniProt sequence for S6FN32