Diacylglycerol Signaling

20 A.C. Newton
diacylglycerol, a membrane interaction that is increased by the specific binding of
phosphatidylserine to the C1 domain. Novel isozymes translocate to membranes
enriched in diacylglycerol, with selective activation at Golgi membranes. Activity
at this location tends to be significantly sustained relative to the shorter-lived activation
of conventional protein kinase C isozymes at the plasma membrane because of
the sustained elevation of diacylglycerol at Golgi following agonist stimulation.
Protein scaffolds also play a major role in fine-tuning the cellular location of
specific protein kinase C isozymes. Thus, a unique signature of protein kinase C
activity exists throughout the cellular terrain.
Acknowledgments This work was supported in part by National Institutes of Health R01
GM43154 (ACN). I thank Lisa Gallegos and Christine Gould for helpful comments.
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