Role of Protein Phosphorylation in Regulation of Bioreactivity.
Final progress rept. 1 Mar 84-28 Feb 87,
ROCKEFELLER UNIV NEW YORK
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Four neuron-specific phosphorproteins and calciumcalmodulin-dependent protein kinase II were used as model proteins to investigate the role of protein phosphorylation in the regulation of bioreactivity in the nervous system. These studies were carried out at the levels of electrophysiology, biochemistry, and molecular biology, in an attempt to obtain the most comprehensive understanding of their functions. Synapsin I and calciumcalmodulin-dependent protein kinase II were pressure-injected into the preterminal digit of the squid giant synapse to test directly the possible regulation of neurotransmitter release by these substances. The binding of synapsin I to small synaptic vesicles was examined. The mechanism of calciumcalmodulin-dependent protein autophosphorylation and its effects on the actvity of the enzyme were studied. The regional and subcellular distributions of proteins IIIa and IIIb in the nervous system were determined. The regional and subcellular distributions of protein p38 in the nervous system were determined. Two cDNA clones for protein IIIa and IIIb were obtained and sequenced. Keywords deoxyribonucleic acids.