Abstract
The subcellular distribution of Ca2+- and calmodulin-dependent myosin light chain phosphorylating activity in rat cerebral cortex was studied. The activity showed a high degree of association to nerve endings (either crude or purified by discontinuous sucrose density gradient centrifugation). After osmotic shock of the nerve endings, the activity was largely membrane associated and could not be released from membranes by freeze-thawing, dilution, 75 mM NaCl or 4 mM EDTA. The association of Ca2+/calmodulin-dependent myosin light chain phosphorylating activity with synaptosomal membranes suggests a role for calcium-dependent myosin phosphorylation in events relating to neurotransmission.