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CA2 — PHKA1

Text-mined interactions from Literome

Andreeva et al., Biochemistry (Mosc) 1999 : Binding of phosphorylase kinase by glycogen occurs only in the presence of Ca2+ and Mg2+
Furuya et al., Proc Natl Acad Sci U S A 1982 : The enzyme is also inactivated by phosphorylase kinase in the presence of Ca2+ and calmodulin
Silver et al., Mol Pharmacol 1983 : The activities of phosphorylase kinase and myosin light-chain kinase are regulated by Ca2+ binding to calmodulin
Cohen et al., Ann N Y Acad Sci 1980 : The current evidence suggests that the regulation of phosphorylase kinase by Ca2+ in vivo is achieved through the interaction of this divalent cation with calmodulin ( the delta subunit ) and troponin C, and that the relative importance of these two calcium binding proteins depends on the state of phosphorylation of the enzyme [ FIGURE 1 ]
Nadeau et al., J Biol Chem 1997 : The structural effects of endogenous and exogenous Ca2+/calmodulin on phosphorylase kinase
Shmelev et al., Biochem Mol Biol Int 1997 : The complex formation occurs in two stages : ( i ) the formation of phosphorylase-glycogen complex controlled by ATP, ( ii ) the binding of phosphorylase kinase to the previously formed phosphorylase-glycogen complex exclusively in the presence of Ca2+ and Mg2+