Abstract
Tetanization of afferent fibers in the transverse hippocampal slice, results in long-term potentiation (LTP) and a concomitant increase in the degree of phosphorylation of a 52 kDa synaptosomal protein. The in vitro phosphorylation of this 52 kDa protein is calcium/calmodulin and cyclic nucleotide independent. This 52 kDa protein, which was originally described in synaptosomal membrane fractions, resembles the major coated vesicle phosphoprotein with regard to its molecular weight (MW) and phosphorylation characteristics. In this study we compare the 52 kDa proteins from synaptosomal plasma membranes (SPM) and coated vesicles. The two proteins appear to be identical on basis of the following criteria: (i) relative MW, (ii) peptide map, and (iii) isoelectric point. Coated vesicles are thought to be involved in receptor-mediated endocytosis and membrane recycling. We suggest that the changes in 52 kDa phosphorylation, concomitant with LTP, may reflect an increase in membrane recycling through coated vesicles.
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