Critical roles of non-histone protein lysine methylation in human tumorigenesis
Abstract
Several protein lysine methyltransferases and demethylases have been identified to have critical roles in histone modification. A large body of evidence has indicated that their dysregulation is involved in the development and progression of various diseases, including cancer, and these enzymes are now considered to be potential therapeutic targets. Although most studies have focused on histone methylation, many reports have revealed that these enzymes also regulate the methylation dynamics of non-histone proteins such as p53, RB1 and STAT3 (signal transducer and activator of transcription 3), which have important roles in human tumorigenesis. In this Review, we summarize the molecular functions of protein lysine methylation and its involvement in human cancer, with a particular focus on lysine methylation of non-histone proteins.
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The mechanisms that underpin adaptive responses and render epigenetic therapies ineffective are varied and include tumour-intrinsic mechanisms and heterogenous cellular and molecular effects of the drugs.
“The mechanisms that underpin these adaptive responses and render epigenetic therapies ineffective are varied and include tumour-intrinsic mechanisms and heterogenous cellular and molecular effects of the drugs 187 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [187]
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Self-citation
- Authors
- Hamamoto, R., Saloura, V., & Nakamura, Y.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Hamamoto, Ryuji
- Venue
- Nature Reviews Cancer
- Published
- 2015-01-23
- Volume
- 15
- Issue
- 2
- Pages
- 110-124
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W2036357556
- Cited by
- 376
- References
- 167
- Citations by year
- 2026: 14 · 2025: 20 · 2024: 27 · 2023: 29 · 2022: 36 · 2021: 30 · 2020: 39 · 2019: 38 · 2018: 33 · 2017: 38 · 2016: 49 · 2015: 22
- FWCI
- 4.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- carcinogenesis, p53, RB1, STAT3, lysine methyltransferase, demethylases, cancer therapy targets, histone modifications
- MeSH terms
- Cell Transformation, Neoplastic, Chromosomal Proteins, Non-Histone, Humans, Lysine, Methylation, Histone-Lysine N-Methyltransferase, Tumor Suppressor Protein p53, Retinoblastoma Protein, STAT3 Transcription Factor
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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