Ask about this productRelated genes to: SMYD5 Blocking Peptide
- Gene:
- SMYD5 NIH gene
- Name:
- SMYD family member 5
- Previous symbol:
- RAI15
- Synonyms:
- RRG1, NN8-4AG, ZMYND23
- Chromosome:
- 2p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-17
- Date modifiied:
- 2015-04-21
Related products to: SMYD5 Blocking Peptide
Related articles to: SMYD5 Blocking Peptide
- Histone H4K20 methylation is critical in regulating the cell cycle, DNA damage response, and gene repression in proliferating cells. However, its role in the heart remains poorly understood. Our previous work revealed that histone H4K20 tri-methylation is elevated in acute cell models of cardiomyocyte hypertrophy but is reduced in mouse models of cardiac hypertrophy and ischemia. Although these findings highlight the dynamic nature of this modification and its significance in regulating gene expression, the data on enzymes regulating H4K20 methylation is sparse. To build upon this work and investigate H4K20 di-methylation and the enzymes modulating this site in cardiac pathology, we quantified histone H4K20 di-methylation and 12 methyltransferases and demethylases across one cell model, two mouse models of cardiac dysfunction, and cardiac tissue from heart failure patients. While we observed no global changes in H4K20 di-methylation, we detected alterations in methyltransferases and and demethylases and in humans and mice. These findings suggest changes in H4K20 di-methylation may occur on an individual gene basis but do not lead to global alterations in H4K20 di-methylation. Additionally, this work identified four enzymes differentially modulated in cardiac dysfunction to advance our understanding of epigenetic mechanisms involved in heart disease. - Source: PubMed
Publication date: 2025/11/02
Hickenlooper SamuelBrady CameronBia RyanVisker Joseph RWang LiValdez StevenGwynn ClintRoland Maya NKyriakopoulos Christos PSideris KonstantinosDrakos Stavros GSzulik Marta WFranklin Sarah - To investigate the mechanism by which the effective-component combination of Bufei Yishen formula III (ECC-BYF III) ameliorates airway epithelial barrier injury in chronic obstructive pulmonary disease (COPD) through miRNA-mRNA regulatory networks. - Source: PubMed
Publication date: 2025/09/04
Liu ChunleiYue ChangyuanXing XiaoxiangHuang LidongWei YanxinZhao PengLi JianshengGuan Qingzhou - Hepatocellular carcinoma (LIHC) poses significant challenges due to limited targeted therapeutic options. This study investigates SMYD5, an oncogene implicated in the pathogenesis of LIHC, and its interaction with the BRD4 protein. : We employed bioinformatics analyses alongside experimental validations to assess SMYD5 expression across various cancers, particularly LIHC. This included survival analysis, protein expression studies, and functional assays to understand the role of SMYD5 in LIHC progression. : Our findings demonstrate that SMYD5 expression is markedly elevated in LIHC tumor tissues compared to normal liver tissues. Moreover, high levels of SMYD5 correlate with poor overall survival and disease-free survival rates in LIHC patients. Functional assays indicate that the knockdown of SMYD5 significantly inhibits cell proliferation and increases apoptosis in LIHC cell lines. Additionally, a notable interaction between SMYD5 and BRD4 was identified, suggesting a potential therapeutic target in the SMYD5-BRD4 axis. : These findings collectively establish SMYD5 as a molecular driver in LIHC pathology and identify the SMYD5-BRD4 interaction axis as a promising therapeutic target for future drug development. - Source: PubMed
Publication date: 2025/07/25
Hu MingyeChen ShijiZhen YumiaoWang XinZhong YiwenLiang XiaoxuChong Cheong-MengZhong Hai-Jing - The eukaryotic ribosome is highly modified by protein methylation, yet many of the responsible methyltransferases remain unknown. Here, we identify SET and MYND domain-containing protein 5 (SMYD5) as a ribosomal protein methyltransferase that catalyzes trimethylation of RPL40/eL40 at lysine 22. Through a systematic mass spectrometry-based approach, we identify 12 primary sites of protein methylation in ribosomes from K562 cells, including at RPL40 K22. Through in vitro methylation of synthetic RPL40 using fractionated lysate, we then identify SMYD5 as a candidate RPL40 K22 methyltransferase. We show that recombinant SMYD5 has robust activity toward RPL40 K22 in vitro and that active site mutations ablate this activity. Knockouts of SMYD5 in K562 cells show a complete loss of RPL40 K22 methylation and decreased polysome levels. We show that SMYD5 does not methylate histones in vitro, and by systematic analysis of its recognition motif, we find that SMYD5 requires a KXY motif for methylation, explaining its lack of activity toward histones. - Source: PubMed
Publication date: 2025/04/05
Hamey Joshua JShah MananWade John DBartolec Tara KWettenhall Richard E HQuinlan Kate G RWilliamson Nicholas AWilkins Marc R - Fibroblast-like synoviocytes (FLS) are crucial for maintaining synovial homeostasis. SMYD5, a member of the histone lysine methyltransferase subfamily SMYDs, is involved in many pathological processes. This study aimed to investigate the role of SMYD5 in regulating synovial fibroblast homeostasis and the pathogenesis of rheumatoid arthritis (RA). - Source: PubMed
Publication date: 2025/03/31
Xiao ChenxiSu ZhenghuaZhao JialinTan SubeiHe MengtingLi YuhuiLiu JiayaoXu JieHu YajieLi ZhongzhengFan ChunxiangLiu Xinhua