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Coilin is a highly conserved nuclear protein that serves as the indispensable structural scaffold of the Cajal body—a non-membrane-bound nuclear domain involved in the maturation and trafficking of small nuclear ribonucleoproteins (snRNPs) and other RNA-processing factors. Coilin is essential for Cajal body formation, acting as a molecular hub that facilitates multivalent interactions with proteins such as the Survival Motor Neuron (SMN) complex, Sm proteins, and RNA molecules including snRNAs and scaRNAs. Its N-terminal domain directs self-oligomerization, necessary for Cajal body assembly, while its C-terminal Tudor-like domain mediates protein-protein interactions. Coilin post-translational modifications (phosphorylation and methylation) regulate its function and localization. Though coilin and Cajal bodies have been linked to quality control in snRNP assembly, telomere maintenance, and DNA repair, coilin is not a classical therapeutic or pharmacological target (e.g., receptor, enzyme, channel), and no drugs are known to directly affect it. Coilin disruption may indirectly impair nuclear RNA metabolism and is of research interest in cell biology and neurodegeneration but has no direct clinical application or biomarker status at present.
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