AI Article Synopsis
- The serine/arginine subfamily of protein kinases is important for regulating various cellular processes and has been conserved through evolution.
- Recombinant GST-SRPK1 was used to discover possible kinases in testis extracts that could modulate SRPK1's activity.
- CK2 was identified as the main kinase responsible for phosphorylating SRPK1, particularly at Ser(51) and Ser(555), leading to a significant increase in its activity.
Article Abstract
The serine/arginine subfamily of protein kinases has been conserved throughout evolution and its members are thought to play important roles in the regulation of multiple cellular processes. Mammalian SRPK1 has been considered as a constitutively active kinase that is predominantly expressed in testis. In the present study, recombinant GST-SRPK1 was used as substrate to identify potential protein kinase(s) in testis extracts, involved in phosphorylating and thereby regulating the activity of this enzyme. Using a panel of chromatography media, inhibition by heparin, immunoblot analysis, and phosphopeptide mapping, CK2 was determined to be the major kinase that phosphorylates SRPK1. Phosphorylation of SRPK1 by CK2 occurred mainly at Ser(51) and Ser(555) in vitro, and resulted in approximately 6-fold activation of the enzyme. These findings suggest that SRPK1 may be an important cellular target for CK2 action.
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| http://dx.doi.org/10.1016/s0006-291x(02)03055-3 | DOI Listing |
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