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Multiple Ca 2+ signaling pathways converge on CaM kinase in PC12 cells
Author(s) -
MacNicol Melanie,
Schulman Howard
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80627-s
Subject(s) - microbiology and biotechnology , signal transduction , phospholipase c , chemistry , kinase , calmodulin , acetylcholine , protein kinase a , acetylcholine receptor , protein kinase c , biochemistry , biology , receptor , enzyme , endocrinology
The role of multifunctional Ca 2+ /calmodulin‐dependent protein kinase (CaM kinase) in mediating various Ca 2+ signaling pathways was examined in PC12 cells. Conversion of the kinase to a Ca 2+ ‐independent form was used to monitor which neurotransmitters activate the enzyme in situ. CaM kinase responds to Ca 2+ influx elicited by ligand‐gated Ca 2+ channels for ATP and acetylcholine. It also responds to Ca 2+ mobilization ofIP 3 ‐sensitive stores elicited by phospholipase C‐linked receptors for ATP and acetylcholine as well as by caffeine. CaM kinase mediates the actions of many neurotransmitters and Ca 2+ signaling pathways.