Abstract
IN many secretory cells materials destined for secretion are packaged in membrane-limited granules and are extruded by exocytosis1. This process is known to require metabolic energy and calcium2–6. Calcium probably acts as a common mediator in stimulus–secretion coupling2, but the molecular mechanisms involved are unknown. Increasing evidence that many physiological processes are regulated by phosphorylation of proteins7 has led to the suggestion that calcium-dependent phosphorylation of proteins may be involved in secretory responses8–13. We have sought evidence for this possibility in the mast cell, the rapid and extensive secretory activity of which conforms to the general pattern of exocytosis dependent on energy and calcium4,14–20. Here we report a rapid phosphorylation of several proteins in rat peritoneal mast cells stimulated to secrete either by the classic mast cell secretagogue 48/80 (refs 15 and 21–23) or by the calcium ionophore A23187 (refs 22–25).
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SIEGHART, W., THEOHARIDES, T., ALPER, S. et al. Calcium-dependent protein phosphorylation during secretion by exocytosis in the mast cell. Nature 275, 329–331 (1978). https://doi.org/10.1038/275329a0
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DOI: https://doi.org/10.1038/275329a0
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