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Activation of exocytosis by the heterotrimeric G protein Gi3
M Aridor1, G Rajmilevich, M A Beaven
1Weizmann Institute of Science, Department of Chemical Immunology, Rehovot, Israel.
Secretagogues of rat peritoneal mast cells, such as mastoparan and compound 48/80, induce mast cell exocytosis by activating directly the guanosine triphosphate-binding proteins that are required for exocytosis. The introduction of a synthetic peptide that corresponds to the carboxyl-terminal end sequence of G alpha i3 into the cells specifically blocked this secretion. Similar results were obtained when antibodies to this peptide were introduced. The G alpha i3 was located in both the Golgi and the plasma membrane, but only the latter source of G alpha i3 appeared to be essential for secretion. These results indicate that G alpha i3 functions to control regulated exocytosis in mast cells.
Secretagogues of rat peritoneal mast cells, such as mastoparan and compound 48/80, induce mast cell exocytosis by activating directly the guanosine triphosphate-binding proteins that are required for exocytosis. The introduction of a synthetic peptide that corresponds to the carboxyl-terminal end sequence of G alpha i3 into the cells specifically blocked this secretion. Similar results were obtained when antibodies to this peptide were introduced. The G alpha i3 was located in both the Golgi and the plasma membrane, but only the latter source of G alpha i3 appeared to be essential for secretion. These results indicate that G alpha i3 functions to control regulated exocytosis in mast cells.