Development of a Single Cell Ca2+ Imaging System to Study the Role of PKC Substrate B-50 in Neurotransmitter Release and Neurite Outgrowth
One of the well-characterized substrates of protein kinase C (PKC) in neurons is the protein B-50. B-50 is a nervous tissue-specific substrate of PKC associated with the cytosolic face of the presynaptic membrane (see De Graan et al., 1991). Protein B-50 is identical to the growth-associated protein GAP-43, the calmodulin (CaM)-binding protein neuromodulin, and protein F1, which is implicated in long-term potentiation (for a review see Skene, 1989). B-50 is one of the abundant proteins in the neuronal growth cone (Skene, 1989) and has been implicated in signal transduction and the mechanism of neurite outgrowth during development and differentiation (Skene, 1989). In a series of studies we have shown that the degree of PKC-mediated phosphorylation of B-50 in hippocampal slices and synaptosomes is correlated with transmitter release (Dekker et al., 1991a; Heemskerk et al., 1989,1990). Based on these correlative studies and the fact that phorbol esters which stimulate PKC enhance neurotransmitter release (see Dekker et al., 1991a), we have suggested that PKC-mediated B-50 phosphorylation may be involved in the regulation of neurotransmitter release.
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