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N-methyladenosine (mA) is the most abundant internal modification of eukaryotic mRNA. This modification has previously been shown to alter the export kinetics for mRNAs though the molecular details surrounding this phenomenon remain poorly understood. Recruitment of the TREX mRNA export complex to mRNA is driven by transcription, 5' capping and pre-mRNA splicing. Here we identify a fourth mechanism in human cells driving the association of TREX with mRNA involving the mA methylase complex. We show that the mA complex recruits TREX to mA modified mRNAs and this process is essential for their efficient export. TREX also stimulates recruitment of the mA reader protein YTHDC1 to the mRNA and the mA complex influences the interaction of TREX with YTHDC1. Together our studies reveal a key role for TREX in the export of mA modified mRNAs.
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http://dx.doi.org/10.1038/s41598-018-32310-8 | DOI Listing |
Anal Bioanal Chem
September 2025
GuangDong Engineering Technology Research Center of Antibody Drug and Immunoassay, Department of Biological Sciences and Biotechnology, College of Life Science and Technology, Jinan University, Guangzhou, 510632, China.
Illicit drug abuse poses a significant global threat to public health and social security, highlighting the urgent need for rapid, sensitive, and versatile detection technologies. To address the limitations of traditional chromatographic techniques-such as high costs and slow response times-and the drawbacks of conventional immunochromatographic sensors (ICS), including low sensitivity and non-intuitive signal outputs, a fluorescence-quenching ICS (FQICS) was developed. This sensor leverages fluorescence resonance energy transfer (FRET) between aggregation-induced emission fluorescent microspheres (AIEFMs) and gold nanoparticles (AuNPs).
View Article and Find Full Text PDFACS Chem Biol
September 2025
Laboratory of Chemical Biology, Department of Biomedical Engineering and Institute of Complex Molecular Systems, Technische Universiteit Eindhoven, 5612 AZ Eindhoven, The Netherlands.
The orphan nuclear receptor NR2F6 (Nuclear Receptor subfamily 2 group F member 6) is an emerging therapeutic target for cancer immunotherapy. Upregulation of NR2F6 expression in tumor cells has been linked to proliferation and metastasis, while in immune cells NR2F6 inhibits antitumor T-cell responses. Small molecule modulation of NR2F6 activity might therefore be a novel strategy in cancer treatment, benefiting from this dual role of NR2F6.
View Article and Find Full Text PDFJ Neurosci
September 2025
Retina and Optic Nerve Research Laboratory, Dalhousie University, Halifax, Nova Scotia, Canada, B3H4R2
At the glutamatergic synapses between rod photoreceptors and ON-type bipolar cells, neurotransmitter is detected by the postsynaptic metabotropic glutamate receptor mGluR6. This receptor forms trans-synaptic interactions with ELFN1, a presynaptic cell adhesion molecule expressed in rods, and ELFN1 is important for mGluR6 localization at bipolar cell dendritic tips. Here, we show that in mice of either sex lacking mGluR6, the presynaptic localization of ELFN1 is disrupted.
View Article and Find Full Text PDFCell Signal
September 2025
School of Forensic Medicine, Xinxiang Medical University, Xinxiang, Henan 453003, People's Republic of China.
Triple-negative breast cancer (TNBC) presents a formidable therapeutic challenge due to its aggressive behavior, molecular heterogeneity, and lack of actionable targets. This study identifies activation-induced cytidine deaminase (AID) as a pivotal epigenetic driver reprogramming the tumor microenvironment (TME) via non-canonical regulation of NOTCH signaling. Mechanistically, AID recruits histone acetyltransferase 1 (HAT1) to form a chromatin-remodeling complex that binds the JAG1 promoter region (-1.
View Article and Find Full Text PDFThromb Res
September 2025
Departamento de Química and Institute for advanced research in chemical Science (IAdChem), Facultad de Ciencias, Módulo 13, Universidad Autónoma de Madrid, 28049, Madrid, Spain.
Platelet integrin αIIbβ3 is the final common effector of arterial thrombosis: it switches from a low-affinity to a high-affinity state, binds fibrinogen, and initiates the outside-in signals that stabilize a growing clot. Calcium- and integrin-binding protein 1 (CIB1) emerged as the first endogenous partner of the αIIb cytoplasmic tail and is now recognized as a dual-role adaptor. At rest, Ca-free CIB1 tethers the inner membrane clasp and restrains premature integrin activation; after ligand engagement, Ca-bound CIB1 docks onto αIIb, recruits focal-adhesion kinase and amplifies Src-dependent cytoskeletal remodeling.
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