CaMKII inactivation by extracellular Ca(2+) depletion in dorsal root ganglion neurons

Cell Calcium
Jonathan E Cohen, R Douglas Fields

Abstract

A mechanism by which Ca(2+)/CaM-dependent protein kinase (CaMKII) is autophosphorylated by changes in extracellular calcium in the absence of detectable changes in cytoplasmic [Ca(2+)] has been identified. We find that when the external Ca(2+) concentration ([Ca(2+)](O)) is lowered, Ca(2+) is released from intracellular stores to maintain a constant cytoplasmic Ca(2+) level, gradually depleting the endoplasmic Ca(2+) stores. Accompanying the store-depletion is a rapid decrease in CaMKII activity. Approximately 25% of the measured CaMKII autophosphorylation in DRG neurons in culture can be regulated by Ca(2+) flux from intracellular stores caused by manipulating [Ca(2+)](O), as shown by blocking refilling of store-operated Ca(2+)-channels with SK&F 96365, Ruthenium Red, and a partial block with Ni(2+). Blocking voltage-gated Ca(2+)-channels with either isradipine or SR 33805, had no effect on CaMKII autophosphorylation induced by restoring Ca(2+)(O) to normal after depleting the intracellular Ca(2+) stores. These results show that removal of Ca(2+)(O) has profound effects on intracellular Ca(2+) signaling and CaMKII autophosphorylation, in the absence of measurable changes in intracellular Ca(2+). These findings have wide-rangin...Continue Reading

Citations

Jan 26, 2012·Science Signaling·Arnulfo TorresMaiken Nedergaard
Oct 23, 2008·Journal of Cell Science·Dario BonanomiFlavia Valtorta
Mar 11, 2011·The Journal of Neuroscience : the Official Journal of the Society for Neuroscience·Geza GemesQuinn H Hogan
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Jun 28, 2012·Chronobiology International·Takako NoguchiDavid K Welsh
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