Abstract 2552 Characterization of two novel peptides capable of inducing targeted degradation by a proteasome-independent mechanism

Targeted degradation by recruitment of biomolecules has therapeutic applications, but in order to be effective, targeted degradation requires moieties capable of inducing a degradation pathway. The moiety used affects degradation efficiency or which substrates can be targeted (proteins, organelles, etc.). Therefore, the discovery of new factors capable of degradation may open new possibilities in targeted degradation therapies. Using a high-throughput screen, we identified two RING finger containing peptides, HLTF;zf-C3HC4 and RO52;zf-C3HC4, capable of inducing degradation when recruited to a protein.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.110009
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
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Abstract 2552 Characterization of two novel peptides capable of inducing targeted degradation by a proteasome-independent mechanism

Carley Schwartz, Grace E. Boyum, Sarah L. Kendall, Gaelen T. Hess et al.
Journal of Biological Chemistry
Ubiquitin and proteasome pathways
article

Abstract 2552 Characterization of two novel peptides capable of inducing targeted degradation by a proteasome-independent mechanism

Carley Schwartz, Grace E. Boyum, Sarah L. Kendall, Gaelen T. Hess, Elizabeth E Wacker
article en

Abstract

Targeted degradation by recruitment of biomolecules has therapeutic applications, but in order to be effective, targeted degradation requires moieties capable of inducing a degradation pathway. The moiety used affects degradation efficiency or which substrates can be targeted (proteins, organelles, etc.). Therefore, the discovery of new factors capable of degradation may open new possibilities in targeted degradation therapies. Using a high-throughput screen, we identified two RING finger containing peptides, HLTF;zf-C3HC4 and RO52;zf-C3HC4, capable of inducing degradation when recruited to a protein.

Journal of Biological ChemistryVol. 301(5)
University of Wisconsin–Madison (US)
Zero hunger
Openalex Percentile: Top 88%
Ubiquitin and proteasome pathways
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