The role of NSD1, NSD2, and NSD3 histone methyltransferases in solid tumors.

Histone Methyltransferases Histone-Lysine N-Methyltransferase / metabolism Humans Neoplasms / genetics Nuclear Proteins / metabolism Repressor Proteins / metabolism
Cancer H3K36 methyltransferases Histone methylation NSD1/KMT3B NSD2/MMSET/WHSC1 NSD3/WHSC1L1 Solid tumors

Journal

Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402

Informations de publication

Date de publication:
09 May 2022
Historique:
received: 15 02 2022
accepted: 20 04 2022
revised: 19 04 2022
entrez: 9 5 2022
pubmed: 10 5 2022
medline: 12 5 2022
Statut: epublish

Résumé

NSD1, NSD2, and NSD3 constitute the nuclear receptor-binding SET Domain (NSD) family of histone 3 lysine 36 (H3K36) methyltransferases. These structurally similar enzymes mono- and di-methylate H3K36, which contribute to the maintenance of chromatin integrity and regulate the expression of genes that control cell division, apoptosis, DNA repair, and epithelial-mesenchymal transition (EMT). Aberrant expression or mutation of members of the NSD family is associated with developmental defects and the occurrence of some types of cancer. In this review, we discuss the effect of alterations in NSDs on cancer patient's prognosis and response to treatment. We summarize the current understanding of the biological functions of NSD proteins, focusing on their activities and the role in the formation and progression in solid tumors biology, as well as how it depends on tumor etiologies. This review also discusses ongoing efforts to develop NSD inhibitors as a promising new class of cancer therapeutic agents.

Identifiants

DOI: 10.1007/s00018-022-04321-2 PMID: 35532818 PMC: PMC9520630
pubmed: 35532818
doi: 10.1007/s00018-022-04321-2
pii: 10.1007/s00018-022-04321-2
pmc: PMC9520630
mid: NIHMS1837961
doi:

Substances chimiques

Nuclear Proteins 0
Repressor Proteins 0
Histone Methyltransferases EC 2.1.1.-
Histone-Lysine N-Methyltransferase EC 2.1.1.43
NSD1 protein, human EC 2.1.1.43
NSD2 protein, human EC 2.1.1.43
NSD3 protein, human EC 2.1.1.43

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

285

Subventions

Organisme : Feinberg School of Medicine
ID : Translational Bridge Award
Organisme : NIDCR NIH HHS
ID : P50 DE030707
Pays : United States
Organisme : U.S. Army Medical Research Acquisition Activity
ID : W81XWH2110487
Organisme : NCI NIH HHS
ID : R01 CA218802
Pays : United States
Organisme : NIH HHS
ID : 1P50 DE030707-01
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA060553
Pays : United States
Organisme : U.S. Department of Defense
ID : W81XWH-17-1-0578
Organisme : U.S. Department of Defense
ID : W81XWH-17-1-0405
Organisme : NIH HHS
ID : R01 CA218802
Pays : United States
Organisme : NIDCR NIH HHS
ID : R01 DE027809
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA006927
Pays : United States
Organisme : Prostate Cancer Foundation
ID : 2017CHAL2008
Organisme : NIH HHS
ID : R01CA227918
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA227918
Pays : United States

Informations de copyright

© 2022. The Author(s), under exclusive licence to Springer Nature Switzerland AG.

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Auteurs

Iuliia Topchu (I)

Division of Hematology/Oncology, Department of Medicine, Robert H. Lurie Comprehensive Cancer Center, Feinberg School of Medicine, Northwestern University, 303 E. Superior Street, Chicago, IL, 60611, USA.

Rajendra P Pangeni (RP)

Division of Hematology/Oncology, Department of Medicine, Robert H. Lurie Comprehensive Cancer Center, Feinberg School of Medicine, Northwestern University, 303 E. Superior Street, Chicago, IL, 60611, USA.
Department of Natural and Applied Sciences, Nexus Institute of Research and Innovation (NIRI), Sitapakha, Mahalaxmi-4, Lalitpur, Bagmati, 44700, Nepal.

Igor Bychkov (I)

Division of Hematology/Oncology, Department of Medicine, Robert H. Lurie Comprehensive Cancer Center, Feinberg School of Medicine, Northwestern University, 303 E. Superior Street, Chicago, IL, 60611, USA.

Sven A Miller (SA)

Molecular Therapeutics Program, Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA, 19111, USA.

Evgeny Izumchenko (E)

Department of Medicine, Section of Hematology and Oncology, University of Chicago, Chicago, IL, 60637, USA.

Jindan Yu (J)

Department of Medicine-Hematology/Oncology and Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, 303 E. Superior Street, Chicago, IL, 60611, USA.

Erica Golemis (E)

Molecular Therapeutics Program, Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA, 19111, USA.
Department of Cancer and Cellular Biology, Lewis Katz School of Medicine at Temple University, 3500 North Broad St, Philadelphia, PA, 19140, USA.

John Karanicolas (J)

Molecular Therapeutics Program, Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA, 19111, USA.
Moulder Center for Drug Discovery Research, Temple University School of Pharmacy, Philadelphia, PA, 19140, USA.

Yanis Boumber (Y)

Division of Hematology/Oncology, Department of Medicine, Robert H. Lurie Comprehensive Cancer Center, Feinberg School of Medicine, Northwestern University, 303 E. Superior Street, Chicago, IL, 60611, USA. yanis.boumber@northwestern.edu.
Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University, ul. 74 Karl Marks, Kazan, 420012, Russia. yanis.boumber@northwestern.edu.
ORCID: 0000-0001-5003-248X

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Classifications MeSH

questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Protein Methyltransferases › Histone méthyltransférases › The role of NSD1, NSD2, and NSD3 histone...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › One-carbon group transferases › Methyltransferases › Protein Methyltransferases › Histone méthyltransférases › Histone-lysine N-methyltransferase › The role of NSD1, NSD2, and NSD3 histone...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › The role of NSD1, NSD2, and NSD3 histone...
questionsmedicales.fr › Tumeurs › The role of NSD1, NSD2, and NSD3 histone...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines nucléaires › The role of NSD1, NSD2, and NSD3 histone...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Protéines de répression › The role of NSD1, NSD2, and NSD3 histone...