IndraLab
Statements
rlimsp
"Along with information from the crystal structure of Ca2+/CaM bound to CKII(290-314) (Meador, W. E., Means, A. R., and Quiocho, F. A. (1993) Science 262, 1718-1721), our results suggest a model in which CaM-dependent autophosphorylation of CaM-kinase induces a conformational change in the region of the CaM-binding domain which allows the formation of additional stabilizing interactions with CaM."
rlimsp
"Autophosphorylation of CaM-kinase II produces a form of the enzyme not requiring Ca(2+)/calmodulin for sustained activity. We report that autophosphorylated CaM-kinase II dephosphorylates itself in the presence of ADP (termed autodephosphorylation). The dephosphorylation was unaffected by phosphatase inhibitors and was nucleotide specific, occurring with ADP but not with AMP, GTP, or GDP. (32)P-ATP was produced when ADP was added to (32)P-labeled CaM-kinase II, indicating that the enzyme was undergoing dephosphorylation through a reversal of the autophosphorylation reaction. ATP addition also produced loss of (32)P from the autophosphorylated enzyme while maintaining the kinase in a phosphorylated state."