CLK

CLKs (Cdc2-like kinases) belong to the dual-specificity protein kinase family and regulate transcript splicing through phosphorylation of SR proteins[1]. Mechanistically, CLK activity supports spliceosome molecular machinery and alternative pre-mRNA splicing, processes linked to cancer, neurodegeneration, inflammation, viral replication, and Duchenne muscular dystrophy[1]. In cellular models, CLK inhibitors reduce phosphorylated SR proteins, alter pre-mRNA splicing, suppress cancer cell growth, and induce apoptosis[2]. Compared with related isoforms, CLK1-CLK4 share splicing-control functions, but inhibitor selectivity remains difficult, especially because many CLK1 inhibitors also target CLK4, DYRK kinases, or haspin[3]. Structural studies show that CX-4945 inhibits CLK1, CLK2, and CLK3, with the strongest inhibitory effect on CLK2, supporting isoform-aware inhibitor design[4]. For experimental applications, TG003 suppresses CLK-mediated phosphorylation, SR-protein phosphorylation, nuclear-speckle dissociation, and CLK1-dependent alternative splicing in mammalian cells[5].
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