Skip to main content
. Author manuscript; available in PMC: 2008 Jun 1.
Published in final edited form as: Biochim Biophys Acta. 2007 Apr 14;1773(6):891–902. doi: 10.1016/j.bbamcr.2007.04.004

Figure 7.

Figure 7

Myospryn is a substrate for PKA. A, Schematic of the N-terminal fragment of myospryn (amino acids 73-743) shows three consensus PKA phosphorylation sites between amino acids 138-158. B, The putative PKA phosphorylation sites are phosphorylated by PKA in vitro. The N-terminal myospryn fragment was subjected to an in vitro kinase assay using recombinant catalytic subunit of PKA. Deletion of all three sites from this myospryn fragment is unable to be phosphorylated by PKA in vitro. C, The N-terminal fragment of myospryn containing the PKA consensus sites was incubated in the kinase assay buffer without PKA enzyme demonstrating that other endogenous kinases were not responsible for the phosphorylation. Incubation with recombinant PKA and the PKA-specific peptide inhibitor, PKI, resulted in a loss of phosphorylation of the N-terminal fragment demonstrating specificity for PKA. For all of the above experiments protein expression of the wildtype and mutant proteins was confirmed by blotting protein extracts with the anti-FLAG antibody.