Abstract
Background The type I cGMP-dependent protein kinases (PKGIa and PKGIb) are splice variants that differ in their first ~100 amino acids, giving each isoform unique dimerization and autoinhibitory domains. The unique coiled-coil dimerization domains mediate isoform specific proteinprotein interactions, and we have previously identified the amino acids that are important in mediating the interaction between PKGIb and its two known interaction partners, TFII-I and IRAG [1].
Highlights
The type I cGMP-dependent protein kinases (PKGIa and PKGIb) are splice variants that differ in their first ~100 amino acids, giving each isoform unique dimerization and autoinhibitory domains
Since serine 12 is not conserved in mouse or rat, our results indicate that PKGIb regulates caldesmon in a species-specific manner
While the PKGI-mediated indirect phosphorylation site(s) have not been determined, our preliminary data suggests that PKGI could potentially regulate all CaD isoforms, albeit in a cell type and species specific manner
Summary
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