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Journal of Neuroscience, Vol 16, 10-18, Copyright © 1996 by Society for Neuroscience
Expression and characterization of Aplysia protein kinase C: a negative regulatory role for the E region
WS Sossin, X Fan and F Saberi
Department of Neurology and Neurosurgery, McGill University, Montreal Neurological Institute, Quebec, Canada.
The Aplysia nervous system contains two phorbol ester-activated protein
kinase C isoforms, the Ca(2+)-activated Apl I and the Ca(2+)- independent
Apl II. Short-term applications of the facilitatory transmitter serotonin
(5-HT) activates Apl I, but not Apl II. In contrast, Apl II, but not Apl I,
can form an autonomous kinase. To investigate the biochemical
characteristics of the Aplysia kinases that might underlie their
differential activation, we expressed Apl I, Apl II, and two derivatives of
Apl II with deletions in the amino-terminal 150 amino acid E region in
insect cells using the baculovirus system. Similar to nervous system
extracts, expressed Apl II has more autonomous activity than Apl I. Removal
of the E region lowered the amount of phosphatidylserine required for
activation of Apl II, but did not remove the autonomous kinase activity. In
addition, phosphatidylserine vesicles could sediment fusion proteins
containing the E region, consistent with a role for the E region in lipid
interactions. A partial deletion of the E region modifies activation of Apl
II by phorbol esters and oleic acid, suggesting that in the intact enzyme
the E region interacts with the phorbol ester-binding domain of the kinase.
These results introduce a model whereby the E region acts as a negative
regulator of Apl II activation and suggest that this inhibition may explain
the inability of short-term applications of 5-HT to activate Apl II.
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