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Journal of Neuroscience, Vol 5, 3414-3422, Copyright © 1985 by Society for Neuroscience
Identification of protein phosphatase 1 in synaptic junctions: dephosphorylation of endogenous calmodulin-dependent kinase II and synapse-enriched phosphoproteins
SM Shields, TS Ingebritsen and PT Kelly
A calcium/calmodulin-dependent protein kinase termed CaM-kinase II is a
major component of synaptic junctions from forebrain and constitutes
approximately 12% of total synaptic junction protein. CaM-kinase II
phosphorylates at least seven polypeptides that are enriched in synaptic
junctions, of which two represent the 50- and 60-kilodalton subunits of the
protein kinase. In this report the nature of endogenous protein
phosphatases which dephosphorylate each of the seven synaptic junction
phosphoproteins was examined. Assays of synaptic junctions and other
subcellular fractions from rat forebrain for type-1 and type-2 protein
phosphatases revealed that protein phosphatase 1 (PrP-1) was specifically
enriched in synaptic junctions with respect to cytosolic fractions. The
activity of type-2 protein phosphatases was very low in synaptic junctions.
Homogeneous PrP-1 from rabbit skeletal muscle was found to dephosphorylate
each of the seven phosphoproteins in synaptic junctions. Inhibitors-1 and
-2 were found to inhibit endogenous protein phosphatase activity by 70 to
80%. Since inhibitors-1 and -2 are specific inhibitors of PrP-1, these
results indicate that this enzyme accounts for the majority of endogenous
protein phosphatase activity in synaptic junctions. Approximately 15% of
the protein phosphatase activity in synaptic junctions was type 2A, whereas
PrP-2B and PrP-2C accounted for little, if any, of the activity toward
endogenous or exogenous phosphoproteins. These results indicate that PrP-1
may be important in controlling the state of phosphorylation of synaptic
junction proteins.
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