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CALM2 — SYN1

Text-mined interactions from Literome

Fiumara et al., Neuroscience 2001 : C1 neurons were cultured with the wrong target neuron C3 for three to five days and then injected with either dephosphorylated or Ca ( 2+ ) /calmodulin dependent protein kinase II-phosphorylated Cy3 labeled synapsin I ... A three-fold increase in the amplitude of the sniffer depolarization with respect to the pre-injection amplitude ( 190+/-29 % increase, n=10, P < 0.006 ) was found 5 min after injection of Ca ( 2+ ) /calmodulin dependent protein kinase II-phosphorylated synapsin I that lasted for about 30 min
Yamamoto et al., J Pharmacol Sci 2003 : New aspects of neurotransmitter release and exocytosis : involvement of Ca2+/calmodulin dependent phosphorylation of synapsin I in insulin exocytosis
Dittgen et al., Proc Natl Acad Sci U S A 2004 : First, lentiviral vectors are used for neuron-specific gene delivery from alpha-calcium/calmodulin dependent protein kinase II or Synapsin I promoters, optionally in combination with gene knockdown by means of U6 promoter-driven expression of short interfering RNAs
Musazzi et al., Eur J Neurosci 2005 : Accordingly, the Ca ( 2+ ) /calmodulin dependent posthoc endogenous phosphorylation of synapsin I in the same area was increased
Hrabec et al., Gen Pharmacol 1991 : 1. We have used synaptosomal membranes to study the influence of substance P and its fragments and analogues of its C-terminal fragment on Ca2+/calmodulin dependent synapsin I endogenous phosphorylation
Scott-Woo et al., Biochem J 1990 : Phosphorylation of synapsin I is Ca2 ( + ) - and calmodulin dependent : half-maximal activation occurs at 0.13 microM-Ca2+ and maximal activity at 0.4 microM-Ca2+
Jackson et al., Eur J Pharmacol 2013 (Substance Withdrawal Syndrome...) : The proteins calcium/calmodulin dependent protein kinase II ( CaMKII ) and synapsin I are essential for neurotransmitter release and were shown to be involved in drug dependence
Saitoh et al., J Cell Biol 1985 (Synaptic Transmission) : We now provide evidence that this Mr 55,000 protein is a subunit of a Ca2+/calmodulin dependent kinase : ( a ) both the Mr 55,000 calmodulin binding protein and kinase activity are loosely attached to the membrane-cytoskeletal complex ; ( b ) both kinase activity and the Mr 55,000 protein are translocated from the membrane-cytoskeleton complex to the cytoplasm under conditions that cause the change in the subcellular distribution of the Mr 55,000 calmodulin binding protein ; and ( c ) calmodulin binding activity of the Mr 55,000 protein and the ability to carry out the Ca2+/calmodulin dependent phosphorylation of synapsin I are purified in parallel
Steiner et al., J Biol Chem 1987 : The binding of synapsin with the neurofilament subunit is specific since this binding interaction is saturable, with a 1 : 1 stoichiometry, the binding involves only certain proteolytically derived domains of synapsin, and is therefore not a simple electrostatic interaction between the basic domains of synapsin and the acidic regions in the neurofilament subunit, and Ca2+/calmodulin dependent phosphorylation of synapsin inhibits this interaction
Bartelt et al., Biochem J 1986 : In the presence of Ca2+ and calmodulin , phosphorylation of smooth-muscle myosin light chain and brain synapsin and autophosphorylation of a Mr-50,000 protein were observed
Nayak et al., Proc Natl Acad Sci U S A 1996 : Ca2+/calmodulin dependent protein kinase II phosphorylation of the presynaptic protein synapsin I is persistently increased during long-term potentiation
Hayashi et al., Brain Res 1998 (Brain Ischemia...) : The level of calmodulin and the phosphorylation of synapsin I in the synaptosomes were not altered up to the 7th day, but the levels of calcium/calmodulin dependent protein kinase II and synapsin I in the synaptosomes were significantly decreased by microsphere embolism