Regulation of brain Type II Ca2+/calmodulin-dependent protein kinase by autophosphorylation: A Ca2+-triggered molecular switch
- 28 March 1986
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 44 (6), 861-870
- https://doi.org/10.1016/0092-8674(86)90008-5
Abstract
Calcium/calmodulin-stimulated autophosphorylation of a prominent brain calmodulin-dependent protein kinase (Type II CaM kinase) produces dramatic changes in its enzymatic activity. These changes suggest a mechanism by which the kinase could act as a calcium-triggered molecular switch. Incorporation of 3–12 of a possible total of 30 phosphate groups per holoenzyme causes kinase activity toward exogenous substrates as well as autophosphorylation itself to become independent of calcium. Thus, kinase activity could be prolonged beyond the duration of an initial activating calcium signal. The calcium-independent autophosphorylation could further prolong the active state by opposing dephosphorylation by cellular phosphatases.This publication has 3 references indexed in Scilit:
- Intraterminal injection of synapsin I or calcium/calmodulin-dependent protein kinase II alters neurotransmitter release at the squid giant synapse.Proceedings of the National Academy of Sciences of the United States of America, 1985
- Purification and characterization of a calmodulin-dependent protein kinase that is highly concentrated in brain.Journal of Biological Chemistry, 1983
- Ca2+-Calmodulin-Dependent Phosphorylation of Soluble and Nuclear Proteins in the Rat Ovary*Endocrinology, 1983