Harnessing FBXO31 with terminal amide-functionalized molecules for targeted protein degradation

Targeted protein degradation (TPD) is a powerful strategy for controlling protein abundance. Here, we establish FBXO31 as a TPD-competent E3 ligase by exploiting its recognition of C-terminal amide-bearing degrons. Using an amidated Ala-Phe motif as a chemical recruiter, multiple small-molecule binders can be transformed into FBXO31-dependent degraders that induce rapid and potent target degradation. Mechanistic studies confirm FBXO31-mediated ternary complex formation and identify key residues in FBXO31 required for recruiter engagement and target degradation. We further show that an FBXO31-based multi-kinase degrader exhibits a distinct and broader degradation profile than a CRBN-based degrader, highlighting a potentially expanded degradable target space beyond CRBN.

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Publication Details

Journal
bioRxiv (Cold Spring Harbor Laboratory)
Published
2026-01-29
DOI
https://doi.org/10.64898/2026.01.28.702440
Primary Topic
Protein Degradation and Inhibitors
Type
article
Field-Weighted Citation Impact
0.00
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article

Harnessing FBXO31 with terminal amide-functionalized molecules for targeted protein degradation

Isabella A. Riha, Xiaokang Jin, Jamal M Martin, Chen Zhou et al.
bioRxiv (Cold Spring Harbor Laboratory)
Protein Degradation and Inhibitors
article

Harnessing FBXO31 with terminal amide-functionalized molecules for targeted protein degradation

Isabella A. Riha, Xiaokang Jin, Jamal M Martin, Chen Zhou, Xiaoyu Zhang, Chenlu Zhang
article en

Abstract

Targeted protein degradation (TPD) is a powerful strategy for controlling protein abundance. Here, we establish FBXO31 as a TPD-competent E3 ligase by exploiting its recognition of C-terminal amide-bearing degrons. Using an amidated Ala-Phe motif as a chemical recruiter, multiple small-molecule binders can be transformed into FBXO31-dependent degraders that induce rapid and potent target degradation. Mechanistic studies confirm FBXO31-mediated ternary complex formation and identify key residues in FBXO31 required for recruiter engagement and target degradation. We further show that an FBXO31-based multi-kinase degrader exhibits a distinct and broader degradation profile than a CRBN-based degrader, highlighting a potentially expanded degradable target space beyond CRBN.

bioRxiv (Cold Spring Harbor Laboratory)
Northwestern University (US)
Openalex Percentile: Top 73%
Protein Degradation and Inhibitors
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