{Models}
Symbol: PKAr {Links}
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Flybase ID: {Flybase_ID} |
Synonyms: {Name}
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{GadFly} |
Function: {Short_Function} |
{LocusLink} |
Keywords: {Keywords} |
{Interactive_Fly} |
{Summary}
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- Binding of 4 cAMP molecules in domains A and B is required to dissociate
the PKAc from PKAr
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- Two regulatory subunits type I monomers dimerize in reverse orientation
and are covalently linked by disulfide bonds between the pairs of cysteine
residues in the dimerization domains to give PKAr
- The dimerization domain also contains residues that are essential
for PKAr type I binding to dual specificity A-kinase anchoring proteins
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- PKAr*, defective in binding cAMP, is shown to activate Hh target genes
solely through its ability to bind and inhibit endogenous PKAc (Kiger,
2001)
- However PKI(1-31), a small fragment of the rabbit skeletal muscle
PKAc-inhibitor protein, is unable to have an effect despite its ability
to inhibit endogenous PKAc (Kiger,
2001)
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