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CALM3 — CAMKK1

Text-mined interactions from Literome

Kitani et al., J Biochem 2001 : In the preceding paper, we demonstrated that changes in the activity of CaM-kinase IV by PKA results from the phosphorylation of CaM-kinase kinase alpha by PKA and identified six phosphorylation sites, Ser ( 24 ) for autophosphorylation, and Ser ( 52 ), Ser ( 74 ), Thr ( 108 ), Ser ( 458 ), and Ser ( 475 ) for phosphorylation by PKA
Tokumitsu et al., Biochemistry 2001 : The activities of CaM-KKalpha and CaM-KKbeta chimera, in which autoinhibitory sequences were replaced by each other, were completely dependent on Ca ( 2+ ) /CaM , suggesting that the autoinhibitory regions of CaM-KKalpha and CaM-KKbeta are functional
Turner et al., Diabetes 2008 : AMPK phosphorylation was examined in L6 myotubes and LKB1 ( -/- ) cells, with or without the Ca ( 2+ ) /calmodulin dependent protein kinase kinase ( CAMKK ) inhibitor STO-609
Quan et al., Biochem Pharmacol 2013 (Fatty Liver) : Ca(+2)-calmodulin dependent protein kinase kinase ( CAMKK ) and AMP activated protein kinase (AMPK) were both activated by BA treatment
Enslen et al., Biochem Biophys Res Commun 1995 : It is likely that the lower efficiency of transcriptional activation by transfected CaM-kinase IV in previous studies was due to the fact that the CaM-kinase IV was not activated by CaM-kinase IV kinase
Okuno et al., J Biochem 1994 : The purified CaM-kinase IV kinase phosphorylated and concomitantly activated CaM-kinase IV purified from rat brain as well as the recombinant kinase expressed in Escherichia coli in a Ca2+/calmodulin dependent manner
Tokumitsu et al., J Biol Chem 1994 : However, CaM-kinase IV can be activated by brain CaM-kinase IV kinase resulting in large increases in both total ( 5-7-fold ) and Ca2+/CaM independent ( > 20-fold ) CaM-kinase IV activities ... CaM-kinase IV is not significantly activated by autophosphorylation, but it can be activated 10-fold by a CaM-kinase IV kinase
Kitani et al., J Biochem 1997 : The phosphorylation site ( s ) involved in the activation of CaM-kinase IV by CaM-kinase kinase alpha was studied using a mutant CaM-kinase IV ( K71R ) in which Lys71 ( ATP binding site ) was replaced with Arg, because the autophosphorylation of CaM-kinase IV occurring at multiple sites made it difficult to study phosphorylation of the enzyme by CaM-kinase kinase