Chemoproteogenomic stratification of the missense variant cysteinome

Cancer genomes are rife with genetic variants; one key outcome of this variation is widespread gain-of-cysteine mutations. These acquired cysteines can be both driver mutations and sites targeted by precision therapies. However, despite their ubiquity, nearly all acquired cysteines remain unidentified via chemoproteomics; identification is a critical step to enable functional analysis, including assessment of potential druggability and susceptibility to oxidation. Here, we pair cysteine chemoproteomics-a technique that enables proteome-wide pinpointing of functional, redox sensitive, and potentially druggable residues-with genomics to reveal the hidden landscape of cysteine genetic variation. Our chemoproteogenomics platform integrates chemoproteomic, whole exome, and RNA-seq data, with a customized two-stage false discovery rate (FDR) error controlled proteomic search, which is further enhanced with a user-friendly FragPipe interface. Chemoproteogenomics analysis reveals that cysteine acquisition is a ubiquitous feature of both healthy and cancer genomes that is further elevated in the context of decreased DNA repair. Reference cysteines proximal to missense variants are also found to be pervasive, supporting heretofore untapped opportunities for variant-specific chemical probe development campaigns. As chemoproteogenomics is further distinguished by sample-matched combinatorial variant databases and is compatible with redox proteomics and small molecule screening, we expect widespread utility in guiding proteoform-specific biology and therapeutic discovery.

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Publication Details

Journal
Nature Communications
Published
2024-10-28
DOI
https://doi.org/10.1038/s41467-024-53520-x
Citations
11
Primary Topic
Advanced biosensing and bioanalysis techniques
Type
article
Field-Weighted Citation Impact
2.57

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article

Chemoproteogenomic stratification of the missense variant cysteinome

Fengchao Yu, Heta S. Desai, Miranda Villanueva, Katrina H. Andrews et al.
11 citations
Nature Communications
Advanced biosensing and bioanalysis techniques
2.57
article

Chemoproteogenomic stratification of the missense variant cysteinome

Fengchao Yu, Heta S. Desai, Miranda Villanueva, Katrina H. Andrews, Keriann M. Backus, Mark A. Arbing, Samuel Ofori, Elaine F. Reed, Kristina V. Bergersen, Lisa M. Boatner, Flowreen Shikwana, Alexey I. Nesvizhskii, Nicholas Ung
article en
11 citations

Abstract

Cancer genomes are rife with genetic variants; one key outcome of this variation is widespread gain-of-cysteine mutations. These acquired cysteines can be both driver mutations and sites targeted by precision therapies. However, despite their ubiquity, nearly all acquired cysteines remain unidentified via chemoproteomics; identification is a critical step to enable functional analysis, including assessment of potential druggability and susceptibility to oxidation. Here, we pair cysteine chemoproteomics-a technique that enables proteome-wide pinpointing of functional, redox sensitive, and potentially druggable residues-with genomics to reveal the hidden landscape of cysteine genetic variation. Our chemoproteogenomics platform integrates chemoproteomic, whole exome, and RNA-seq data, with a customized two-stage false discovery rate (FDR) error controlled proteomic search, which is further enhanced with a user-friendly FragPipe interface. Chemoproteogenomics analysis reveals that cysteine acquisition is a ubiquitous feature of both healthy and cancer genomes that is further elevated in the context of decreased DNA repair. Reference cysteines proximal to missense variants are also found to be pervasive, supporting heretofore untapped opportunities for variant-specific chemical probe development campaigns. As chemoproteogenomics is further distinguished by sample-matched combinatorial variant databases and is compatible with redox proteomics and small molecule screening, we expect widespread utility in guiding proteoform-specific biology and therapeutic discovery.

Nature CommunicationsVol. 15(1)
University of California, Los Angeles (US), University of Michigan (US), UCLA Health (US), UCLA Medical Center (US), Abterra Biosciences (United States) (US), Broad Center (US)
U.S. Department of Energy, Arnold and Mabel Beckman Foundation, V Foundation for Cancer Research, National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, Jonsson Comprehensive Cancer Center
Openalex Percentile: Top 10%
Advanced biosensing and bioanalysis techniques
2.57
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