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

Iuliia Topchu; Rajendra P. Pangeni; Igor Bychkov; Sven A. Miller; Evgeny Izumchenko; Jindan Yu; Erica Golemis; John Karanicolas; Yanis Boumber

doi:10.1007/s00018-022-04321-2

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

Iuliia Topchu, Rajendra P. Pangeni, Igor Bychkov, Sven A. Miller, Evgeny Izumchenko, Jindan Yu, Erica Golemis, John Karanicolas, Yanis Boumber^*

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

31 Scopus citations

Abstract

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.

Original language	English (US)
Article number	285
Journal	Cellular and Molecular Life Sciences
Volume	79
Issue number	6
DOIs	https://doi.org/10.1007/s00018-022-04321-2
State	Published - Jun 2022

Funding

Figures 1 , 3 , and 4 were created with BioRender.com.

Keywords

Cancer
H3K36 methyltransferases
Histone methylation
NSD1/KMT3B
NSD2/MMSET/WHSC1
NSD3/WHSC1L1
Solid tumors

ASJC Scopus subject areas

Molecular Medicine
Molecular Biology
Pharmacology
Cellular and Molecular Neuroscience
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1007/s00018-022-04321-2

Cite this

@article{a2b75bc1cb0f4360a9170e07ff84ba1c,

title = "The role of NSD1, NSD2, and NSD3 histone methyltransferases in solid tumors",

abstract = "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{\textquoteright}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.",

keywords = "Cancer, H3K36 methyltransferases, Histone methylation, NSD1/KMT3B, NSD2/MMSET/WHSC1, NSD3/WHSC1L1, Solid tumors",

author = "Iuliia Topchu and Pangeni, {Rajendra P.} and Igor Bychkov and Miller, {Sven A.} and Evgeny Izumchenko and Jindan Yu and Erica Golemis and John Karanicolas and Yanis Boumber",

note = "Publisher Copyright: {\textcopyright} 2022, The Author(s), under exclusive licence to Springer Nature Switzerland AG.",

year = "2022",

month = jun,

doi = "10.1007/s00018-022-04321-2",

language = "English (US)",

volume = "79",

journal = "Cellular and Molecular Life Sciences",

issn = "1420-682X",

publisher = "Springer Science and Business Media Deutschland GmbH",

number = "6",

}

TY - JOUR

T1 - The role of NSD1, NSD2, and NSD3 histone methyltransferases in solid tumors

AU - Topchu, Iuliia

AU - Pangeni, Rajendra P.

AU - Bychkov, Igor

AU - Miller, Sven A.

AU - Izumchenko, Evgeny

AU - Yu, Jindan

AU - Golemis, Erica

AU - Karanicolas, John

AU - Boumber, Yanis

PY - 2022/6

Y1 - 2022/6

N2 - 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.

AB - 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.

KW - Cancer

KW - H3K36 methyltransferases

KW - Histone methylation

KW - NSD1/KMT3B

KW - NSD2/MMSET/WHSC1

KW - NSD3/WHSC1L1

KW - Solid tumors

UR - http://www.scopus.com/inward/record.url?scp=85129513470&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85129513470&partnerID=8YFLogxK

U2 - 10.1007/s00018-022-04321-2

DO - 10.1007/s00018-022-04321-2

M3 - Review article

C2 - 35532818

AN - SCOPUS:85129513470

SN - 1420-682X

VL - 79

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

IS - 6

M1 - 285

ER -

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

Abstract

Funding

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this