FBXO22 is a promising E3 ubiquitin ligase for targeted protein degradation
4 affiliations
- 1Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
- 2Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA
- 3Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599, USA
- 4Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA
Abstract
Targeted protein degradation (TPD) is an exciting new strategy to destroy, rather than simply inhibit, therapeutic targets of interest. Degrader molecules function by recruiting protein targets to E3 ubiquitin ligases, resulting in target polyubiquitination and destruction. Although there are >600 E3s, relatively few, notably CRBN and VHL, are routinely used for TPD applications in either academic or clinical settings. An up-and-coming ligase on the TPD scene is FBXO22, which has multiple distinct features when compared to other commonly used E3s. Here, we highlight the native functions of FBXO22 and the chemical matter (degraders) used to repurpose FBXO22's ubiquitination activity. As FBXO22 is overexpressed in a variety of cancers, this may provide a therapeutic window to destroy targets selectively in cancer cells. Taken together, FBXO22 fulfills a necessary void in the TPD field and provides a new approach to develop novel cancer therapeutics.
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BibTeX
@article{liu2026fbxo22,
title = {{FBXO22 is a promising E3 ubiquitin ligase for targeted protein degradation}},
author = {Tongkun Liu and Kevin C. Robertson and Amanda S. McGowan and Reagan E. Thompson and Lindsey I. James and Nicholas G. Brown},
journal = {Current opinion in chemical biology},
year = {2026},
month = oct,
doi = {10.1016/j.cbpa.2026.102803},
url = {https://doi.org/10.1016/j.cbpa.2026.102803},
note = {CC BY},
}
RIS
TY - JOUR
TI - FBXO22 is a promising E3 ubiquitin ligase for targeted protein degradation
AU - Tongkun Liu
AU - Kevin C. Robertson
AU - Amanda S. McGowan
AU - Reagan E. Thompson
AU - Lindsey I. James
AU - Nicholas G. Brown
PY - 2026
DA - 2026/10/28
JO - Current opinion in chemical biology
DO - 10.1016/j.cbpa.2026.102803
UR - https://doi.org/10.1016/j.cbpa.2026.102803
AB - Targeted protein degradation (TPD) is an exciting new strategy to destroy, rather than simply inhibit, therapeutic targets of interest. Degrader molecules function by recruiting protein targets to E3 ubiquitin ligases, resulting in target polyubiquitination and destruction. Although there are >600 E3s, relatively few, notably CRBN and VHL, are routinely used for TPD applications in either academic or clinical settings. An up-and-coming ligase on the TPD scene is FBXO22, which has multiple distinct features when compared to other commonly used E3s. Here, we highlight the native functions of FBXO22 and the chemical matter (degraders) used to repurpose FBXO22's ubiquitination activity. As FBXO22 is overexpressed in a variety of cancers, this may provide a therapeutic window to destroy targets selectively in cancer cells. Taken together, FBXO22 fulfills a necessary void in the TPD field and provides a new approach to develop novel cancer therapeutics.
SN - 1367-5931
SN - 1879-0402
ER -