Role of Protein Phosphorylation in Regulation of Bioreactivity.
Abstract
Four neuron-specific phosphoproteins ad calcium/calmodulin-dependent protein kinase II were used as model proteins to investigate the role of protein phosphorylationin the regulation of bioreactivity in the nerfous system. These studies were carried out at the levels of electrophysiology, biochemistry, and molecular biology, in an attempt to obtain the dependent proetin kinase II were pressure-injecdted into the preterminal digit of the squid giant synapse to test directly the possible reguilatiom of neurotrnsmitter release by these substances. The binding of Synapsin I to small synaptic vesicles was examined. The mechanism of calcium/calmodulin-dependent protein kinase II autophosphorylation and its effect on the activity 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. A partial cDNA clone for Synapsin I was obtained.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 13, 1986
- Accession Number
- ADA170024
Entities
People
- Paul Greengard
Organizations
- The Rockefeller University