Evidence map›Paper›PMID 38838187›Full record

ArticleJournal of proteome research2024

Chemical Proteomic Profiling of Protein Dopaminylation in Colorectal Cancer Cells.

Nan Zhang, Shuaixin Gao, Haidong Peng, Jinghua Wu, Huapeng Li, Connor Gibson, Sophia Wu, Jiangjiang Zhu, Qingfei Zheng

Abstract read
In one paragraph

Article in Journal of proteome research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Biocompatible Chemistry: A Plug-and-Play Toolbox for Chemical Biology Research.Chembiochem : a European journal of chemical biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Nan ZhangDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.
Shuaixin GaoHuman Nutrition Program, Department of Human Sciences, College of Education and Human Ecology, The Ohio State University, Columbus, Ohio 43210, United States.
Haidong PengDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.
Jinghua WuDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0001-6198-2763
Huapeng LiDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.
Connor GibsonDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.
Sophia WuDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.
Jiangjiang ZhuCenter for Cancer Metabolism, James Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0002-4548-8949
Qingfei ZhengDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0002-8397-3507

Funding

Characterizing the Metabolome and Volatilome of Gut MicrobiomeR35GM133510 · NIGMS · OHIO STATE UNIVERSITY · PI ZHU, JIANGJIANG · 2019 to 2023
$2.2M
Development of a Chemical Biology Toolbox to Investigate Histone MonoaminylationR35GM150676 · NIGMS · PURDUE UNIVERSITY · PI Qingfei Zheng · 2023 to 2026
$1.6M
UHPLC-Trapped Ion Mobility-QTOF for ProteomicsS10OD026945 · OD · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2019 to 2019
$600k
NIGMS NIH HHS R35 GM133510NIGMS NIH HHS R35 GM150676NIH HHS S10 OD026945
6 · The paper itself

Abstract

Histone dopaminylation is a newly identified epigenetic mark that plays a role in the regulation of gene transcription, where an isopeptide bond is formed between the fifth amino acid of H3 (i.e., glutamine) and dopamine. Recently, we developed a chemical probe to specifically label and enrich histone dopaminylation via bioorthogonal chemistry. Given this powerful tool, we found that histone H3 glutamine 5 dopaminylation (H3Q5dop) was highly enriched in colorectal tumors, which could be attributed to the high expression level of its regulator, transglutaminase 2 (TGM2), in colon cancer cells. Due to the enzyme promiscuity of TGM2, nonhistone proteins have also been identified as dopaminylation targets; however, the dopaminylated proteome in cancer cells still remains elusive. Here, we utilized our chemical probe to enrich dopaminylated proteins from colorectal cancer cells in a bioorthogonal manner and performed the chemical proteomics analysis. Therefore, 425 dopaminylated proteins were identified, many of which are involved in nucleic acid metabolism and transcription pathways. More importantly, a number of dopaminylation sites were identified and attributed to the successful application of our chemical probe. Overall, these findings shed light on the significant association between cellular protein dopaminylation and cancer development, further suggesting that targeting these pathways may become a promising anticancer strategy.

Indexed as

Colorectal NeoplasmsHistonesProtein Glutamine gamma Glutamyltransferase 2ProteomicsCell Line, TumorEpigenesis, GeneticGlutamineGTP-Binding ProteinsHumansProtein Processing, Post-TranslationalProteomeTransglutaminasesGlutamineGTP-Binding ProteinsHistonesProtein Glutamine gamma Glutamyltransferase 2ProteomeTGM2 protein, humanTransglutaminasesbioorthogonal chemistrycell signalingchemical proteomicscolorectal cancerprotein dopaminylation

Identifiers

PMID38838187
PMCPMC13120854

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.