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CA2 — SYN1

Text-mined interactions from Literome

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
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
Cid et al., Neuroscience 2011 (Encephalomyelitis, Autoimmune, Experimental) : We also observed a loss of inhibition in the Ca2+ dependent phosphorylation of synapsin I mediated by GABA in nerve terminals from EAE animals, which could explain the loss of GABAergic regulation on evoked glutamate release
Cohen et al., Proc Natl Acad Sci U S A 1990 : In the presence of Ca2+/CaM , synapsin I was phosphorylated
Sihra et al., Proc Natl Acad Sci U S A 1989 : This translocation of synapsin I correlated with its phosphorylation state and was dependent on the presence of Ca2+ in the incubation medium
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
Kelly et al., J Neurochem 1985 : The kinase activity in synaptic fractions was examined for its capacity to phosphorylate endogenous proteins or exogenous synapsin I , in the presence or absence of Ca2+ plus CaM
Albert et al., Proc Natl Acad Sci U S A 1984 : Calmodulin also inhibited the Ca2+/phospholipid dependent phosphorylation of H1 histone, synapsin I , and the delta subunit of the acetylcholine receptor, with use of purified components
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
Majetschak et al., Eur J Biochem 1998 : UCaM Syn-F2 , which binds to calmodulin-Sepharose in a Ca2+ dependent manner, has been purified over 3500-fold in seven steps from rabbit reticulocytes and has a native molecular mass of approximately 620 kDa