The CLK (Cdc2-like kinase) family has four family members: CLK1/STY, CLK2, CLK3 and CLK4. CLKs are dual specificity protein kinases which are self-activated through autophosphorylation on tyrosine residues and phosphorylate their substrates on serine and threonine residues. All family members have N-terminal domains which are rich in serine and arginine residues. They also have a conserved EHLAMMERRIG sequence in the catalytic domain and are thus also known as LAMMER kinases.
Mammalian CLK families contain a SR domain which has been shown to phosphorylate serine/arginine-rich (SR) proteins in vitro and phosphorylate SR protein ASF/SF2 in vivo. This phosphorylation modulates gene splicing and consequently gene expression. CLKs may also modulate the intranuclear distribution of SR proteins, adding a further layer of complexity to the control of gene splicing.
Furthermore, phosphorylation of SR proteins affects their protein-protein interactions, protein-RNA interactions, intracellular localization and trafficking, as well as their alternative splicing of pre-mRNA. In addition, CLKs are useful targets for studying diseases attributed to mis-splicing events as well as conditions such as muscular dystrophy and HIV.
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Literature for Cdc2-like Kinases
A collection of over 400 products for kinase research, the listing includes inhibitors of:
- Receptor Tyrosine Kinases
- Protein Kinases A, C, D and G
- PI-3 Kinase, Akt and mTOR
- MAPK Signaling
- Receptor Serine/Threonine Kinases
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