Role of Protein Phosphorylation in Regulation of Bioreactivity.
Abstract
Four neuron-specific phosphorproteins and calcium/calmodulin-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 calcium/calmodulin-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 calcium/calmodulin-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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 29, 1987
- Accession Number
- ADA180510
Entities
People
- Paul Greengard
Organizations
- The Rockefeller University