Synapsin I phosphorylated by Ca2+, calmodulin-dependent protein kinase II is able to self-degrade.
Phosphorylation of the neurospecific protein synapsin I (SI) by various cellular protein kinases was studied. The analysis of functional properties of phosphosynapsins showed that in the case of PK II-mediated modification of the protein, it becomes capable of self-degradation. The latter process was found to be specific and did not appear to be characteristic of the phosphoforms emerging after the protein modification by PK C or PK A. A possible involvement of the process in the regulation of neurotransmitter secretion is discussed.
Gubin
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AN
Research Center of Molecular Diagnostics, USSR Ministry of Health, Moscow.
Severin
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SE
D000818:Animals; D001921:Brain / Q000201:enzymology; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013552:Swine; D016704:Synapsins
D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D016704:Synapsins; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases