CDC-like kinase 2 (CLK2), a family of autophosphorylating kinases termed CLK (CDC2/CDC28-like kinases) was shown to phosphorylate SR proteins and to influence alternative splicing in overexpression systems. Recent findings demonstrated that the CLK kinases activate PTP-1B family members, and this phosphatase may be an important cellular target for CLK action. Mutations in the clk-2 proteins affect organismal features such as development, behavior, reproduction, and aging as well as cellular features such as the cell cycle, apoptosis, the DNA replication checkpoint, and telomere length.
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The Journal of biological chemistry, 278(24), 21678-21684 (2003-04-03)
Mutations in the clk-2 gene of the nematode Caenorhabditis elegans affect organismal features such as development, behavior, reproduction, and aging as well as cellular features such as the cell cycle, apoptosis, the DNA replication checkpoint, and telomere length. clk-2 encodes
The Journal of biological chemistry, 273(51), 34341-34348 (1998-12-16)
Pre-mRNA splicing is catalyzed by a multitude of proteins including serine/arginine-rich (SR) proteins, which are thought to play a crucial role in the formation of spliceosomes and in the regulation of alternative splicing. SR proteins are highly phosphorylated, and their
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