Ask about this productRelated genes to: METTL5 antibody
- Gene:
- METTL5 NIH gene
- Name:
- methyltransferase like 5
- Previous symbol:
- -
- Synonyms:
- HSPC133
- Chromosome:
- 2q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-04-14
- Date modifiied:
- 2014-11-18
Related products to: METTL5 antibody
Related articles to: METTL5 antibody
- The methyltransferase-like 5 (METTL5) protein has been shown to catalyze m6A deposition on 18S ribosomal RNA. However, whether it also methylates mRNAs remains unclear. To address this, we employed direct RNA sequencing (ONT) for m6A detection on native mRNA molecules. We first validated the quantitative detection of m6A by ONT by treating mESCs with a METTL3 inhibitor. We then compared methylation levels of m6A sites between -KO and WT mESCs. Our analysis provides no compelling evidence for METTL5 mediated mRNA methylation in vivo, indicating that its catalytic activity is restricted to rRNA. - Source: PubMed
Publication date: 2026/05/08
Le Cam SamuelValenta MagdalenaSchneider Robert - METTL5-related neurodevelopmental disorder is a rare autosomal recessive condition characterized by primary microcephaly, intellectual disability, and variable neurobehavioral manifestations. While the genetic etiology is well-established, targeted pharmacological management for the severe neuropsychiatric components of the syndrome remains undefined. - Source: PubMed
Publication date: 2026/05/18
Gündoğdu Öğütlü Özge BeyzaBaştan FurkanErdem Zeynep SeverÖğütlü HakanErdem Haktan Bağış - Sleep plays a critical role in animal physiology, primarily governed by the brain, and its disruption is prevalent in various brain disorders. Mettl5 is associated with intellectual disability (ID), which often includes sleep disturbances. However, the mechanism underlying these sleep disruptions in ID remains poorly understood. In this study, we investigated the sleep phenotypes resulting from mutations. Rescue experiments revealed that functions predominantly within neurons and glia marked by -Gal4 to regulate sleep. Previous work established that Mettl5 forms a complex with Trmt112 to influence rRNA methylation. Notably, a mutation in recapitulated these sleep disturbances, implicating translational regulation by the Mettl5/Trmt112 complex. Subsequent RNA-seq and Ribo-seq analyses of mutants uncovered downstream effects, including altered expression of proteasome components and clock genes. Rescue experiments confirmed that the net increase in PERIOD protein underlies the sleep phenotype. This study illuminates the interplay between ribosome function, clock genes, and the proteasome in sleep regulation, highlighting the integrated roles of protein synthesis and degradation. These findings could potentially provide an example for in vivo study of rRNA methylation function, expand our understanding of protein homeostasis in sleep, and offer insights into the sleep phenotypes associated with ID. - Source: PubMed
Publication date: 2026/05/08
Wu XiaoyuYang XingzhuoFu TiantianRong YikangDu Juan - Methyltransferase-like 5 (METTL5) is a methyltransferase responsible for rRNA N6-methyladenosine (m6A) modification, mutations in which are associated with skeletal abnormalities and cognitive deficits. Despite METTL5's clinical relevance, the molecular mechanisms underlying METTL5-related genetic disorders remain poorly understood. In this study, we demonstrated that Mettl5 KO led to reduced bone mass and smaller body size in mice and impaired the osteogenic differentiation of mesenchymal stem cells. Mechanistically, Mettl5 deficiency decreased the translation efficiency of oxidative stress-responsive serine-rich protein 1 mRNA, downregulated the expression of key antioxidant genes, and diminished antioxidant capacity. Importantly, administration of the antioxidant N-acetylcysteine (NAC) partially rescued skeletal defects in Mettl5-KO mice. These findings reveal a critical role for METTL5 in antioxidant defense and suggest that NAC supplementation may represent a promising therapeutic strategy for METTL5-related disorders. - Source: PubMed
Publication date: 2026/05/08
Lei KexinYin QiLi QiwenWang QianZhang ZhongXue FeiXu RuoshiZhou XinyiPeng LinKokabu ShoichiroLin ShuibinYuan Quan - N-methyladenosine (mA) RNA methylation is implicated in cancer metabolism; however, to the best of our knowledge, the role of methyltransferase 5 (METTL5) in non-small cell lung cancer (NSCLC) progression remains unclear. Reprogrammed glycolytic metabolism (Warburg effect) supports tumor growth and immune evasion; however, the regulatory mechanisms of this process require further investigation. We hypothesized that METTL5 drives NSCLC progression by regulating glycolytic metabolism through mA modification of phosphoglycerate mutase 1 (PGAM1) mRNA. The present study aimed to elucidate the molecular mechanisms, functional impacts and clinical relevance of the METTL5/PGAM1 axis. Integrated analyses of NSCLC cohorts from The Cancer Genome Atlas database were performed, and models (A549 and PC9 cell lines) and molecular techniques, including methylation inhibition, RNA stability assays and metabolic flux measurements (Seahorse XFe96 analyzer), were used. Key interactions were validated through western blotting, reverse transcription-quantitative PCR and correlation analyses. METTL5 was significantly upregulated in NSCLC tissues and in A549, PC9 and H520 cell lines, and high METTL5 expression was associated with poor patient survival (P<0.05). Silencing of METTL5 suppressed NSCLC cell proliferation and migration, while overexpression promoted proliferation and migration. METTL5 directly targeted PGAM1 mRNA through mA modification, and the expression levels of METTL5 and PGAM1 exhibited a statistically significant but moderate positive correlation (R=0.45; P=5.4×10). YTH N-methyladenosine RNA binding protein 1 (YTHDF1) is an m6A reader that recognizes and binds to methylated PGAM1 mRNA, enhancing its stability and expression. PGAM1 knockdown reduced glycolysis (decreased extracellular acidification rate) and increased oxidative phosphorylation (increased oxygen consumption rate). Notably, the positive correlation between PGAM1 and GLUT1 expression (R=0.6; P=4.12×10) supports the role of the METTL5/PGAM1 axis in regulating GLUT1, thereby influencing glycolytic flux. Rescue experiments demonstrated that PGAM1 overexpression reversed GLUT1 downregulation in METTL5-knockdown cells. Overall, METTL5 may drive NSCLC progression by reprogramming glycolytic metabolism through mA modification of PGAM1 mRNA. The METTL5/PGAM1/GLUT1 axis represents a novel therapeutic target for NSCLC. - Source: PubMed
Publication date: 2026/04/20
Shan YuchenDuan XiaoyuYuan KaiLou MingWu QiyongGao Zhaojia