{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMETTL16 is a multifunctional RNA methyltransferase that plays a pivotal role in maintaining cellular S‐adenosylmethionine (SAM) homeostasis by directly controlling the processing of MAT2A mRNA and modifying U6 small nuclear RNA. Under conditions of SAM depletion, METTL16 binds a conserved hairpin in the MAT2A 3′‐UTR to promote efficient splicing and stabilize the mature mRNA, while it also catalyzes N6‐methylation of U6 snRNA at a critical adenosine residue that participates in 5′‐splice site recognition. These activities establish a critical post‐transcriptional mechanism for cells to sense and regulate intracellular SAM levels."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nHigh‐resolution structural and biochemical analyses have revealed that METTL16 possesses a conserved Rossmann‐fold methyltransferase domain as well as additional RNA–binding modules that confer substrate selectivity. In particular, METTL16 directly interacts with the triple‐helical RNA element of the long noncoding RNA MALAT1 and employs a vertebrate conserved region to enhance its binding affinity toward U6 snRNA. These structural insights underscore unique elements of METTL16 that distinguish it from the canonical METTL3/METTL14 complex."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its established role as an m6A “writer” in the nucleus, METTL16 exerts dual functions in gene regulation. It deposits m6A marks on a select set of mRNAs—thereby influencing splicing, stability, and degradation—and additionally performs methylation‐independent roles in the cytosol by interacting directly with translation initiation factors (such as eIF4E2) to facilitate the assembly of the translation‐initiation complex. Detailed enzymological studies, including kinetic and isotope partitioning assays, have illuminated its ordered‐sequential substrate binding and relatively modest catalytic efficiency, highlighting the precision of its regulatory functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of METTL16 has been implicated in a broad range of human malignancies and other diseases. In diverse tumor types—including hepatocellular carcinoma, acute myeloid leukemia, gastric, uterine, bladder, colorectal, osteosarcoma, and papillary thyroid carcinomas—altered METTL16 expression affects tumor cell proliferation, survival, chemoresistance, and metastatic potential by reprogramming RNA metabolism, modulating key cell‐cycle regulators and oncogenic transcripts (for example, cyclin D1, GPX4, VPS33B, Soga1) and disrupting chromosomal stability. Furthermore, aberrant METTL16 levels have been linked to metabolic rewiring (affecting glycolysis and branched‐chain amino acid metabolism), cell fate decisions in embryonic hematopoiesis, and even cardiovascular risk modulation. 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