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CALM3 — 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)
  

Text-mined interactions from Literome

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
Kumar et al., Biochemistry 2004 : SkM Phk , expressed Phk, and the alphagammadelta subcomplex were activated by exogenous calmodulin and underwent Ca ( 2+ ) -dependent autophosphorylation
Strappazzon et al., Mol Cell Neurosci 2007 : Furthermore, we show that CGN grown in K25 medium exhibit detectable CaM dependent Pyk2 activity
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 ?
Xie et al., Mol Endocrinol 2008 : Furthermore, association of Pyk2 and Cam may be required to mediate the effects of calcium on Pyk2 phosphorylation and subsequent activation of ERKs by GnRH
Kelly et al., J Immunol 2010 (Calcium Signaling...) : Calmodulin dependent kinase and Pyk2 transduced calcium signals into activation of the ERK-MAPK pathway, CREB, and generation of an oxidative burst, leading to downstream production of IL-10
Pegova et al., Biokhimiia 1986 : [ The role of calmodulin ( delta-subunit ) in the activation of phosphorylase kinase from rabbit skeletal muscles ]
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
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
Erdödi et al., Int J Biochem 1984 : 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
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
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 )
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