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CALM1 — PHKA2

Pathways - manually collected, often from reviews:

• KEGG Calcium signaling pathway: PHKA1/PHKA2/PHKB/PHKG1/PHKG2 → CALM1/CALM2/CALM3/CALML3/CALML5/CALML6 (protein-protein, binding/association)
  
• Reactome Reaction: CALM1 → PHKA2 (direct_complex)

Text-mined interactions from Literome

Andreeva et al., FEBS Lett 1999 : On the other hand, the interaction of phosphorylase kinase with glycogen requires Ca2+ at both pH values
Satoh et al., J Biol Chem 2001 : Since Pyk2 has no calcium binding domain, and neither Ca ( 2+ ) nor Ca ( 2+ ) /calmodulin directly activates Pyk2, it is not clear how Ca ( 2+ ) transduces the signal to activate Pyk2, a key tyrosine kinase, in the early events of Ang II signaling
Ginnan et al., Am J Physiol Cell Physiol 2002 : The results implicate CaM kinase II as an intermediate in the Ca ( 2+ ) /calmodulin dependent activation of PYK2
Heidinger et al., J Neurosci 2002 : Here we show that in cortical neurons, brief selective activation of group I mGluRs with ( S ) -3,5-dihydroxy-phenylglycine ( DHPG ) induced a Ca ( 2+ ) -calmodulin dependent activation of Pyk2/CAKbeta and the Src-family kinases Src and Fyn that was independent of protein kinase C ( PKC ) ... Furthermore, antagonizing calmodulin or mGluR1, but not PKC, reduced the basal tyrosine phosphorylation levels of Pyk2 and Src, suggesting that mGluR1 may control the basal activity of these kinases and thus the tyrosine phosphorylation levels of NMDA receptors
Lin et al., J Biol Chem 2002 : The calmodulin dependent tyrosine kinase Pyk2 was also activated by M1 but not M3, and Pyk2 appears also to play a role in M1-SRF activation, as judged by experiments with two dominant negative Pyk2 mutants
Espiritu et al., American journal of physiology. Renal physiology 2002 (Acidosis) : Pyk2 phosphorylation was calcium/calmodulin dependent , and Pyk2 associated with Src by means of SH2 domain interaction
De Moliner et al., Eur J Biochem 2003 : Three other kinases [cyclin dependent protein kinase 2 ( CDK2 ), phosphorylase kinase and glycogen synthase kinase 3beta ] exhibit approximately 10-fold weaker affinity for TBB than CK2
Newsholme et al., Biochem J 1992 : In contrast, all published kinetic data to date have strongly suggested that activation of phosphorylase kinase by Ca2+ or phosphorylation is attributable solely to a change in affinity for phosphorylase, with no effect on the Vmax
St Louis et al., Eur J Pharmacol 1977 : Stimulation of cardiac sarcolemmal ( Na+ -- K+ ) ATPase activity by phosphorylase kinase
Kumar et al., Biochemistry 2004 : SkM Phk , expressed Phk, and the alphagammadelta subcomplex were activated by exogenous calmodulin and underwent Ca ( 2+ ) -dependent autophosphorylation
Priddy et al., Protein Sci 2005 : Ca2+ induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering
McConville et al., Am J Physiol Endocrinol Metab 2007 : These findings are consistent with beta ( 1 ) -AR-specific PKA dependent glycogen phosphorylase kinase signaling
Kohno et al., Biochem J 2008 : Protein-tyrosine kinase CAKbeta/PYK2 is activated by binding Ca2+/calmodulin to FERM F2 alpha2 helix and thus forming its dimer
Schaller et al., Biochem J 2008 : Calcium dependent Pyk2 activation : a role for calmodulin ?
Chan et al., J Biol Chem 1979 : Activation of phosphorylase kinase by glucagon was reduced in hepatocytes from adrenalectomized rats, although the half-maximal effective concentration of glucagon was unchanged ... It is concluded that impaired activation of phosphorylase kinase contributes to the reduced glucagon stimulation of hepatic glycogenolysis in adrenalectomized rats
Carlsen et al., Can J Physiol Pharmacol 1985 (Fatigue) : We also propose that the slow Ca2+ current may contribute to the allosteric activation of phosphorylase kinase during muscle activity
Krause et al., Biomed Biochim Acta 1987 : Contrary the activity ratio of phosphorylase retains, in the presence of propranolol, its transient changes during the cardiac cycle, probably caused by a Ca2+ mediated activation of phosphorylase kinase during the contraction process
Bode et al., Mol Cell Biochem 1988 : Isoproterenol and prostaglandin E1 both stimulate cAMP accumulation, but only isoproterenol causes activation of particulate cAMP dependent protein kinase, leading to activation of phosphorylase kinase and glycogen phosphorylase, and inhibition of glycogen synthase
Pegova et al., Biokhimiia 1986 : [ The role of calmodulin ( delta-subunit ) in the activation of phosphorylase kinase from rabbit skeletal muscles ]
Farkas et al., FEBS Lett 1986 : Liver protein kinases ( regulatory subunit of cAMP dependent protein kinase and/or Ca2+ dependent phosphorylase kinase ) are suggested to regulate the activity of hepatic phosphorylase phosphatase ( type 1 and 2A )
Andreeva et al., Eur J Biochem 1986 : The activity of chicken phosphorylase kinase was largely dependent on Ca2+
Cox et al., Arch Biochem Biophys 1987 : The activation of phosphorylase kinase ( EC 2.7.1.38 ; ATP : phosphorylase b phosphotransferase ) by the catalytic subunit of cAMP dependent protein kinase ( EC 2.7.1.37 ; ATP : protein phosphotransferase ) is inhibited by calmodulin
Tsutou et al., Biochem Biophys Res Commun 1985 : Calcium- and calmodulin dependent phosphorylase kinase activity in porcine uterine smooth muscle ... The physiological role of the calcium and calmodulin dependent activation of myometrium phosphorylase kinase is briefly discussed
Van de Werve et al., Biochem J 1979 : In the presence of hexokinase , glucose also stimulated phosphorylase kinase , both in an Na+ or a K+ medium
Sørensen et al., Biochim Biophys Acta 1979 : The non activated form of phosphorylase kinase was activated by Ca2+ in the range 10 ( -7 ) -- 5
Borregaard et al., Eur J Clin Invest 1981 : However, since phosphorylase kinase was not activated, the activation of phosphorylase is believed to be secondary to non-covalent activation of phosphorylase kinase by Ca2+
Cox et al., J Biol Chem 1982 : Calmodulin is shown to inhibit both the activation and phosphorylation of phosphorylase kinase by cAMP dependent protein kinase
Wang et al., J Biol Chem 1983 : It was shown to immunoprecipitate the calmodulin (CaM) dependent phosphodiesterase and phosphorylase kinase activities but not those of CaM itself, CaM independent phosphodiesterase and the catalytic unit of cAMP dependent protein kinase
Livanova et al., Biochem Int 1983 : Regulation of muscle phosphorylase kinase by actin and calmodulin ... There is evidence suggesting that the activation of phosphorylase kinase by actin is not due to trace contamination of actin preparations with calmodulin: (1) Troponin I and trifluoperazine inhibit the activation of phosphorylase kinase by calmodulin but do not inhibit the activation of phosphorylase kinase by F-actin ... ( 3 ) The activation of phosphorylase kinase by calmodulin and actin has different pH profiles
Hashimoto et al., J Biochem 1984 : Effect of free Mg2+ on liver phosphorylase kinase activity
Erdödi et al., Int J Biochem 1984 : Heparin stimulates the activity of nonactivated and activated skeletal muscle phosphorylase kinase in a Ca2+ dependent manner ... The stimulatory effect of heparin on the activity of nonactivated phosphorylase kinase is also expressed in the presence of calmodulin and glycogen
Silonova et al., Biokhimiia 1984 : [ Activation of phosphorylase kinase from rabbit muscle by actin and calmodulin ] ... ( 3 ) The activation of phosphorylase kinase by calmodulin and actin has different pH profiles
Hashimoto et al., Biochem Biophys Res Commun 1984 : These results suggest that a possible role of Mg2+ in the regulation of liver phosphorylase kinase is to protect the enzyme from the inhibitory action of a polyamine such as spermine
King et al., J Biol Chem 1981 : A synergistic activation of phosphorylase kinase by Ca2+ plus Mg2+ was found to be the primary cause of the hysteresis, or lag, in the phosphorylase kinase reaction ... A synergistic activation of phosphorylase kinase by Ca2+ plus Mg2+ was found to be the primary cause of the hysteresis, or lag, in the phosphorylase kinase reaction
Nakamura et al., FEBS Lett 1983 : Calcium -- calmodulin dependent activation of porcine liver phosphorylase kinase ... Porcine liver phosphorylase kinase was activated about 1.5-fold by calmodulin in a calcium dependent manner ... The physiological role of the calmodulin dependent activation for liver phosphorylase kinase is discussed
Cohen et al., Ann N Y Acad Sci 1980 : The regulation of phosphorylase kinase by Ca2+ may therefore also provide a mechanism for achieving synchronous control of the pathways of glycogenolysis and glycogen synthesis
Picton et al., Cell Calcium 1981 : Recent work has demonstrated that phosphorylase kinase not only activates phosphorylase, but also phosphorylates glycogen synthase thereby decreasing its activity ( 45-49 )
Gergely et al., Biochim Biophys Acta 1980 : In the presence of calmodulin phosphorylase kinase has only one, high affinity binding site for Ca2+ ( Ka = 0.27 microM ) ... The changing level of intracellular Ca2+ and cyclic AMP may control the activity of phosphorylase kinase , regulating the mobilization of glycogen
Khoo et al., Biochim Biophys Acta 1976 : Ca2+ dependent activation of phosphorylase by phosphorylase kinase in adipose tissue
Stokoe et al., Biochem J 1993 : The catalytic domain was most similar ( 35-40 % identity ) to calmodulin dependent protein kinases II and IV, phosphorylase kinase , putative serine kinase H1 and the C-terminal domain of MAPKAP kinase-1, which form one branch of the protein kinase phylogenetic tree