Faculty, Staff and Student Publications

Publication Date

8-31-2023

Journal

Cell

Abstract

Post-translational modifications (PTMs) play key roles in regulating cell signaling and physiology in both normal and cancer cells. Advances in mass spectrometry enable high-throughput, accurate, and sensitive measurement of PTM levels to better understand their role, prevalence, and crosstalk. Here, we analyze the largest collection of proteogenomics data from 1,110 patients with PTM profiles across 11 cancer types (10 from the National Cancer Institute's Clinical Proteomic Tumor Analysis Consortium [CPTAC]). Our study reveals pan-cancer patterns of changes in protein acetylation and phosphorylation involved in hallmark cancer processes. These patterns revealed subsets of tumors, from different cancer types, including those with dysregulated DNA repair driven by phosphorylation, altered metabolic regulation associated with immune response driven by acetylation, affected kinase specificity by crosstalk between acetylation and phosphorylation, and modified histone regulation. Overall, this resource highlights the rich biology governed by PTMs and exposes potential new therapeutic avenues.

Keywords

Humans, Acetylation, Histones, Neoplasms, Phosphorylation, Protein Processing, Post-Translational, Proteomics, Post-translational modifications, Pan-Cancer, Genomics, Transcriptomics, Mass Spectrometry, Proteomics, DNA Damage Response, Metabolism, CPTAC

DOI

10.1016/j.cell.2023.07.013

PMID

37582358

PMCID

PMC10680287

PubMedCentral® Posted Date

8-31-2024

PubMedCentral® Full Text Version

Author MSS

nihms-1925596-f0007.jpg (200 kB)
Graphical Abstract

Published Open-Access

yes

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