Cell Biology
The N-terminal Fragment from Caspase-cleaved Serine/Arginine Protein-specific Kinase2 (SRPK2) Translocates into the Nucleus and Promotes Apoptosis*

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SRPK2 belongs to a family of serine/arginine (SR) protein-specific kinases (SRPKs), which phosphorylate SR domain-containing proteins in the nuclear speckles and mediate the pre-mRNA splicing. Previous studies have shown that SRPK2 plays a pivotal role in cell proliferation and apoptosis. However, how SRPK2 is regulated during the apoptosis is unclear. Here, we show that SRPK2 is cleaved by caspases at Asp-139 and -403 residues. Its N terminus cleaved product translocates into the nucleus and promotes VP16-induced apoptosis. Akt phosphorylation of SRPK2 prevents its apoptotic cleavage by caspases. 14-3-3β, the binding partner of Akt-phosphorylated SRPK2, further protects it from degradation. Hence, our results suggest that the N-terminal domain of SRPK2 cleaved by caspases translocates into the nucleus, where it promotes chromatin condensation and apoptotic cell death.

Akt PKB
Apoptosis
Caspase
Nuclear Translocation
Protein-Protein Interactions
14-3-3
SRPK2

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*

This work was supported, in whole or in part, by Grant NS060680 from NCI, National Institutes of Health (to K. Y.).