{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMuscleblind‐like protein 1 (MBNL1) functions as a master regulator of alternative splicing during development and in adult tissues. Numerous studies have demonstrated that MBNL1 directs developmentally programmed splicing transitions by promoting the inclusion or exclusion of specific exons in key pre‐mRNAs—including those encoding cardiac troponin T, the insulin receptor, FOXP1, dystrophin and Tau—and that its functional depletion underlies the spliceopathy observed in myotonic dystrophies. In these disorders, expanded CUG/CCUG repeat‐containing RNAs sequester MBNL1, resulting in aberrant splicing, altered isoform expression and consequent multisystem pathologies. In addition, alternative MBNL1 isoforms generated by variable exon inclusion contribute to differential RNA binding and nuclear localization that are critical for the proper execution of splicing programs during muscle and stem cell differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical splicing‐regulatory role, MBNL1 exhibits remarkable RNA binding specificity and modulates diverse aspects of RNA metabolism. Its affinity for structured stem–loop motifs and short cis‐elements, such as GC‐rich sequences and pyrimidine‐mismatched hairpins, underpins not only pre–mRNA splicing regulation but also autoregulatory feedback through alternative splicing of its own transcript. In vitro and cellular studies have further shown that MBNL1 interacts with specific RNA targets—including transcripts involved in mRNA localization and miRNA biogenesis—and forms ribonucleoprotein complexes with auxiliary proteins in response to cellular stress. These mechanistic insights, gleaned from structural and biochemical analyses, emphasize that the precise recognition of target RNA elements by MBNL1 is essential for maintaining RNA processing fidelity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEmerging evidence also implicates MBNL1 in broader cellular functions that influence cell fate and disease progression. Alterations in MBNL1 activity have been linked to the modulation of stem cell differentiation, muscle regeneration and even tumor cell dedifferentiation, thereby impacting conditions as diverse as congenital malformations, vascular and corneal dystrophies, and various cancers. For instance, changes in MBNL1 levels not only affect the efficiency of satellite cell proliferation but also destabilize mRNAs that control epithelial–mesenchymal transitions and metastatic processes. Such findings illuminate a complex network in which MBNL1’s splicing and RNA‐processing activities intersect with key signaling pathways and transcriptional circuits across multiple disease settings."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "35"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Thai H Ho, Nicolas Charlet-B, Michael G Poulos, et al. 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