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FBXO16 is a CRL1/SCF substrate-recognition protein that drives K48-linked polyubiquitination and proteasomal degradation of select substrates, with prominent nuclear activity.
"**FBXO16 is a CRL1/SCF substrate-recognition protein that drives K48-linked polyubiquitination and proteasomal degradation of select substrates, with prominent nuclear activity.**"
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The FBXO16 F-box domain is required for ligase complex formation while its C-terminal region mediates substrate recognition (e.g. binding the hnRNPL RRM3 domain; C-terminus essential for beta-catenin binding).
"The **F-box domain** is required for **complex formation and ubiquitination function** (e.g., ΔF-box mutants fail to promote ubiquitination of targets or to form productive complexes)."
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FBXO16 targets the nuclear pool of beta-catenin for K48-linked polyubiquitination, suppressing Wnt/TCF transcriptional output.
"FBXO16 physically interacts with β-catenin and promotes **K48-linked polyubiquitination** and **proteasome-mediated degradation** of the **nuclear pool** of β-catenin, suppressing Wnt/TCF transcriptional output."
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FBXO16 acts as the substrate-recognition component of a PDLIM2-containing CRL1 complex that promotes nuclear p65/RELA polyubiquitination and degradation, limiting NF-kappa-B activation.
"Fbxo16 was identified as a substrate-recognition component in a **PDLIM2-containing CRL1 complex** that promotes p65 polyubiquitination and degradation in nuclear compartments, suppressing NF-κB activation."