Abstract
Protein I, a neurone-specific protein concentrated at synapses, is present in most, and probably all, presynaptic nerve terminals where it is at least partially associated with neurotransmitter vesicles (refs 1–5 and P. De Camilli, W. B. Huttner, R. Cameron, M. Harris and P.G., in preparation). Protein I is a major endogenous substrate in nervous tissue for both cyclic AMP-dependent1 and calcium/calmodulin-dependent6–8 protein kinases. Neurotransmitters9,10, apparently acting through cyclic AMP, and depolarizing agents9–11, apparently acting through calcium, have been shown to increase the state of phosphorylation of protein I in intact preparations of the central and peripheral nervous systems. To determine whether impulse conduction regulates the state of phosphorylation of protein I, we have now studied this process in the rabbit superior cervical ganglion, a well characterized neuronal preparation that is suitable for both physiological and biochemical studies. Using a technique developed to quantify the state of phosphorylation of the small amounts of protein I contained in ganglion tissue, we show here that in physiological conditions brief periods of impulse conduction increase the state of phosphorylation of protein I in this ganglion.
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Nestler, E., Greengard, P. Nerve impulses increase the phosphorylation state of protein I in rabbit superior cervical ganglion. Nature 296, 452–454 (1982). https://doi.org/10.1038/296452a0
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DOI: https://doi.org/10.1038/296452a0
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