◀ Back to CA2
CA2 — CSN2
Text-mined interactions from Literome
Hilfiker et al., J Neurochem 1999
:
SyntagI, the purified, recombinant, cytoplasmic domain of rat synaptotagmin I, was an effective substrate in vitro for
Ca2+/calmodulin dependent protein kinase II ( CaMKII ), protein kinase C ( PKC ), and
casein kinase II ( caskII )
Kameda et al., J Mol Cell Cardiol 2006
:
CSN5/Jab1 inhibits cardiac L-type
Ca2+ channel activity through protein-protein interactions
Kuret et al., Biochemistry 1984
:
Purified Ca2+/calmodulin dependent
casein kinase activity was
dependent upon
Ca2+ , calmodulin, and ATP X Mg2+ or ATP X Mn2+ when measured under saturating casein concentrations
Sacks et al., Biochem Mol Biol Int 1994
:
Here we demonstrate that in the
presence or absence of
Ca2+ , calmodulin did not significantly alter either in vitro
casein kinase II activity or autophosphorylation of its beta-subunit ... In contrast,
Ca2+ inhibited in a dose dependent manner both
casein kinase II activity and casein kinase II-catalysed calmodulin phosphorylation
Urao et al., Mol Gen Genet 1994
:
The ATCDPK2 protein expressed in Escherichia coli was found to phosphorylate
casein and myelin basic protein preferentially, relative to a histone substrate, and
required Ca2+ for activation
Burgoyne et al., Biochem Soc Symp 1998
:
In an attempt to define control points within the secretory pathway for casein synthesis and secretion, we have examined the
role of both cytosolic and intra-organelle
Ca2+ in the control of
casein synthesis, phosphorylation and secretion ... Experiments examining the effects of depletion of intra-organelle Ca2+ indicated that intra-organelle
Ca2+ was
required for maintained
casein phosphorylation, but not its secretion ... Depletion of
Ca2+ from the endoplasmic reticulum
led to a marked inhibition of
casein synthesis