TFIP11 (tuftelin interacting protein 11) is a multifunctional spliceosomal protein with primary roles in pre-mRNA splicing and spliceosome regulation. Its canonical function involves spliceosome disassembly, where TFIP11 cooperates with the RNA helicase DHX15 to detect mRNA release and initiate disassembly of terminal intron lariat spliceosomes 1. TFIP11 contains a conserved G-patch domain essential for DHX15 interaction and recruits DHX15 to catalytic U6 snRNA to promote lariat-intron release 2. Beyond disassembly, TFIP11 has DHX15-independent functions in U6 snRNA 2'-O-methylation and U4/U6.U5 tri-snRNP assembly, localizing to nucleoli and Cajal bodies to facilitate these processes 3. Structurally, TFIP11 is an intrinsically disordered protein with salt-responsive conformational properties that promote protein-protein and protein-RNA interactions 4. Clinically, TFIP11 genetic variants associate with dental phenotypes: SNPs in TFIP11 correlate with low caries trajectory 5 and represent risk factors for dental fluorosis susceptibility 67. TFIP11 functions within interactive genetic networks regulating enamel development and caries pathogenesis 8, highlighting its relevance to orofacial biology and potential biomarker utility in predicting individual disease susceptibility.