Ask about this productRelated genes to: C14orf172 antibody
- Gene:
- TRMT61A NIH gene
- Name:
- tRNA methyltransferase 61A
- Previous symbol:
- C14orf172
- Synonyms:
- FLJ40452, GCD14, Gcd14p, hTRM61
- Chromosome:
- 14q32
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-11
- Date modifiied:
- 2015-08-26
Related products to: C14orf172 antibody
Related articles to: C14orf172 antibody
- Hematopoietic stem and progenitor cell (HSPC) development requires finely tuned gene expression programs, yet the role of tRNA modifications in this process remains largely unknown. Here, we uncover the essential function of the tRNA methyltransferase Trmt61a in sustaining fetal liver (FL) HSPCs through N1-methyladenosine (m¹A) deposition. Ribosome profiling revealed globally declined translation efficiency due to translational blockage upon Trmt61a loss in HSPCs, notably the transferrin receptor (Tfrc). Mechanistically, m1A reduction caused ribosomal stalling at Arginine-CGG codons in Tfrc mRNA, thus suppressing Tfrc synthesis and leading to intra-cellular iron depletion. This iron deficiency triggered DNA damage and compromised HSPC survival. Our work elucidates an epitranscriptomic pathway, the Trmt61a-m¹A-Tfrc axis, that safeguards HSPC integrity by linking tRNA modification to iron homeostasis and preventing DNA damage, providing mechanistic and therapeutic insights into hematopoietic disorders. - Source: PubMed
Publication date: 2026/04/13
Liu YiningMa YichenLi PanfengLi YongjieLiang GuixianZhang XiaotingHuang BaofengPeng JinyingMa DongyuanWang LuLi AngYi ChengqiLiu Feng - Nucleotide repeat expansions contribute to a number of neurological disorders. Mutations and augmented expression in fused in sarcoma (FUS) can result in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). Here we reveal that FUS is an N1- and N6-methyladenosine (m1A- and m6A)-binding protein, where the protein interacts with the methylated adenosines in CAG repeat expansion RNA, thereby leading to the protein's cytoplasmic redistribution in SH-SY5Y cells. We also found that ectopically expressed FUS co-localizes with CAG repeat RNA in the cytosol. This co-localization is diminished upon genetic depletion of m6A and m1A writer proteins (i.e. METTL3 and TRMT61A), pharmacological inhibition of METTL3, and ectopic overexpression of m1A and m6A eraser proteins (i.e. ALKBH3 and FTO). Moreover, binding to methylated CAG repeat RNA renders the ectopically expressed FUS protein less dynamic in cells. Together, our study underscores a critical role for m1A and m6A in enhancing FUS-RNA interaction, which results in aberrant subcellular distribution and attenuated mobility of the protein in cells. These findings unveil a novel mechanism underlying neurodegenerative disorders emanating from elevated expression of FUS and suggest targeting FUS-methylated adenosine interactions as a potential therapeutic strategy for FUS proteinopathy. - Source: PubMed
Liang XiaochenZhao TingDai XiaoxiaSun YuxiangYuan JunAfzalpurkar SanatDuong ConnorYu AlbertTang FengHe XiaomeiLiu XiaochuanChen XingyuanCao ZhongwenWang Yinsheng - Anaplastic thyroid cancer (ATC) is a highly aggressive malignancy with rapid progression and poor prognosis. Although N1-methyladenosine (mA) modification has been implicated in cancer development, the specific role of tRNA mA modification in ATC remains unclear. - Source: PubMed
Publication date: 2026/02/10
Ding YingFeng ZiyangChen GuanjunLiu YunqingZhu YuxingCao Ke - Tumor-associated macrophages (TAMs) play crucial roles in tumor progression. However, the mechanisms underlying the posttranscriptional regulation of TAMs remain largely unknown. Here, we demonstrated that Trmt61a, the "writer" enzyme of tRNA N1-methyladenosine (mA) modification, is highly expressed in proinflammatory macrophages in tumor microenvironment. We generated conditional knockout (KO) mice for Trmt61a and observed that Trmt61a deletion in macrophages significantly promoted tumor growth. Mechanistically, we identified that mA maintains the translation of STING, enhances STING-TBK1-IFN-β signaling in macrophages and therefore suppresses tumor cell growth. We further generated TRMT61A-overexpressing human iPSC-derived CAR-macrophage and demonstrated that human TRMT61A effectively promoted antitumor CAR-macrophage therapy in vivo. Collectively, our findings reveal a novel regulatory mechanism of tRNA mA modification in macrophages, highlighting the antitumor therapeutic potential of targeting tRNA mA modification in macrophages. - Source: PubMed
Publication date: 2026/01/14
Wang XuefeiWang XudongLi HaoLiu ShuyuLu YangChen HuifangCai XuemingSu SiyuLi BinLiu RujuanHu WeiguoZhu XiangjiaZhang JinYe YouqiongLi Hua-Bing - Cellular senescence, a fundamental hallmark of aging, plays a paradoxical, often pro-tumorigenic role in cancer. This malignancy is largely driven by the senescence-associated secretory phenotype (SASP), yet the mechanisms that govern the production of a pro-tumorigenic SASP remain poorly understood. This study uncovers an epitranscriptomic axis in colorectal cancer (CRC) where the TRMT6/TRMT61A tRNA N-methyladenosine (mA) methyltransferase complex is aberrantly elevated, driving a senescent state in malignant cells. Mechanistically, TRMT6/61A-dependent mA deposition on specific tRNAs enhances the translational efficiency of their cognate codons. This codon-biased translational control selectively boosts the synthesis of ARG2. Accumulation of ARG2 subsequently activates mTOR and NF-κB signaling and thereby establishes a robust SASP, which actively reprograms the tumor microenvironment by promoting the growth and invasiveness of neighboring cancer cells, activating cancer-associated fibroblasts, and polarizing immunosuppressive M2 macrophages. Collectively, these findings define the TRMT6/61A-ARG2 pathway as a driver for pro-tumorigenic senescence in an mA-dependent manner, revealing a new layer of translational control in aging-associated pathology and offering a compelling rationale for developing senomorphic therapies. - Source: PubMed
Publication date: 2026/01/08
Li TuoyangHuang MingzheCai JinlinLi XuanXing YaokangHe RongzhaoWan ZixiaoGan YingguoLi ZimingWeng JingrongXie YumoWu YuanhuiLiu XiaoxiaWang XiaolinLuo YanxinHuang MeijinLin JinxinYu Huichuan