CLK2

CLK2 encodes a broadly expressed CDC-like kinase that pairs an N-terminal RS-rich region with a dual-specificity catalytic domain. As with its paralogs, autophosphorylation of the activation-segment tyrosine licenses serine/threonine activity directed at the RS domains of SR splicing factors, positioning CLK2 within the nuclear speckle machinery that governs alternative splicing and mRNA maturation. Knockdown experiments link CLK2 to cell-cycle progression and to the survival of proliferating cells, and its activity is sensitive to the same ATP-competitive chemotypes that inhibit CLK1 and CLK3. The recombinant kinase is valuable for comparative splicing studies and for defining compound selectivity across the CLK family.