Emerging role of SMYD family of proteins in human tumorigenesis

Protein lysine methylation is a post-translational modification (PTM) that promotes protein complex formation to regulate DNA replication, gene expression, and repair mechanisms. The Su(Var)3–9, Enhancer-of-zeste and Trithorax (SET) and Myeloid, Nervy, and DEAF-1 (MYND) domain-containing proteins SM...

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Main Authors: Bibi, Afshan, Sarfraz, Ayesha, Sajjad, Amna, Sarfraz, Iqra, Munawwar, Aasma, Zarbab, Aneeqa, Sattar, Mehran, Rasul, Azhar
Format: Article
Language:English
Published: Universiti Kebangsaan Malaysia 2023
Online Access:http://journalarticle.ukm.my/22075/1/SE%2018.pdf
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spelling my-ukm.journal.220752023-08-10T01:04:41Z http://journalarticle.ukm.my/22075/ Emerging role of SMYD family of proteins in human tumorigenesis Bibi, Afshan Sarfraz, Ayesha Sajjad, Amna Sarfraz, Iqra Munawwar, Aasma Zarbab, Aneeqa Sattar, Mehran Rasul, Azhar Protein lysine methylation is a post-translational modification (PTM) that promotes protein complex formation to regulate DNA replication, gene expression, and repair mechanisms. The Su(Var)3–9, Enhancer-of-zeste and Trithorax (SET) and Myeloid, Nervy, and DEAF-1 (MYND) domain-containing proteins SMYD are lysine methyltransferases that catalyze the methylation of various histone and non-histone proteins. There are five members of this SMYD family, and all of these have conserved SET and MYND domains. The SET domain is divided into two segments by the MYND domain (the S-sequence and a core SET domain). SMYD Family performs a key role in numerous biological functions, including growth, development, apoptosis, and proliferation. SMYD family members are associated with skeletal and cardiac muscle physiology and pathology. Several studies have shown that aberrant lysine methylation plays a significant role in oncogenesis. Recently, the SMYD family has gained importance for its role in various mechanisms involved in cancer development and progressions, such as methylation and modification of tumor suppressor proteins (p53 and pRb), transcriptional factors (STAT3, NF-κB), nuclear proteins (PARP1), chaperons (Hsp90), protein kinases (MAPK, ERK), and cell cycle regulatory proteins (CDKN2). SMYD family proteins drive oncogenesis, lead the way to metastasis, and develop chemoresistance, allowing cancer cells to grow, invade the neighboring tissues, and resist therapeutics. In this review, we summarize SMYD family members’ role in different cancers by focusing on their histone and non-histone methylation targets and illustrating the mechanism of SMYD family-mediated oncogenesis. Universiti Kebangsaan Malaysia 2023 Article PeerReviewed application/pdf en http://journalarticle.ukm.my/22075/1/SE%2018.pdf Bibi, Afshan and Sarfraz, Ayesha and Sajjad, Amna and Sarfraz, Iqra and Munawwar, Aasma and Zarbab, Aneeqa and Sattar, Mehran and Rasul, Azhar (2023) Emerging role of SMYD family of proteins in human tumorigenesis. Sains Malaysiana, 52 (4). pp. 1273-1289. ISSN 0126-6039 http://www.ukm.my/jsm/index.html
institution Universiti Kebangsaan Malaysia
building Tun Sri Lanang Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Kebangsaan Malaysia
content_source UKM Journal Article Repository
url_provider http://journalarticle.ukm.my/
language English
description Protein lysine methylation is a post-translational modification (PTM) that promotes protein complex formation to regulate DNA replication, gene expression, and repair mechanisms. The Su(Var)3–9, Enhancer-of-zeste and Trithorax (SET) and Myeloid, Nervy, and DEAF-1 (MYND) domain-containing proteins SMYD are lysine methyltransferases that catalyze the methylation of various histone and non-histone proteins. There are five members of this SMYD family, and all of these have conserved SET and MYND domains. The SET domain is divided into two segments by the MYND domain (the S-sequence and a core SET domain). SMYD Family performs a key role in numerous biological functions, including growth, development, apoptosis, and proliferation. SMYD family members are associated with skeletal and cardiac muscle physiology and pathology. Several studies have shown that aberrant lysine methylation plays a significant role in oncogenesis. Recently, the SMYD family has gained importance for its role in various mechanisms involved in cancer development and progressions, such as methylation and modification of tumor suppressor proteins (p53 and pRb), transcriptional factors (STAT3, NF-κB), nuclear proteins (PARP1), chaperons (Hsp90), protein kinases (MAPK, ERK), and cell cycle regulatory proteins (CDKN2). SMYD family proteins drive oncogenesis, lead the way to metastasis, and develop chemoresistance, allowing cancer cells to grow, invade the neighboring tissues, and resist therapeutics. In this review, we summarize SMYD family members’ role in different cancers by focusing on their histone and non-histone methylation targets and illustrating the mechanism of SMYD family-mediated oncogenesis.
format Article
author Bibi, Afshan
Sarfraz, Ayesha
Sajjad, Amna
Sarfraz, Iqra
Munawwar, Aasma
Zarbab, Aneeqa
Sattar, Mehran
Rasul, Azhar
spellingShingle Bibi, Afshan
Sarfraz, Ayesha
Sajjad, Amna
Sarfraz, Iqra
Munawwar, Aasma
Zarbab, Aneeqa
Sattar, Mehran
Rasul, Azhar
Emerging role of SMYD family of proteins in human tumorigenesis
author_facet Bibi, Afshan
Sarfraz, Ayesha
Sajjad, Amna
Sarfraz, Iqra
Munawwar, Aasma
Zarbab, Aneeqa
Sattar, Mehran
Rasul, Azhar
author_sort Bibi, Afshan
title Emerging role of SMYD family of proteins in human tumorigenesis
title_short Emerging role of SMYD family of proteins in human tumorigenesis
title_full Emerging role of SMYD family of proteins in human tumorigenesis
title_fullStr Emerging role of SMYD family of proteins in human tumorigenesis
title_full_unstemmed Emerging role of SMYD family of proteins in human tumorigenesis
title_sort emerging role of smyd family of proteins in human tumorigenesis
publisher Universiti Kebangsaan Malaysia
publishDate 2023
url http://journalarticle.ukm.my/22075/1/SE%2018.pdf
http://journalarticle.ukm.my/22075/
http://www.ukm.my/jsm/index.html
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