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Title: Regulation of the phosphorylation of the inositol 1,4,5-trisphosphate receptor by protein kinase C
Authors: Vermassen, Elke ×
Fissore, Rafael A
Nadif Kasri, Nael
Vanderheyden, Veerle
Callewaert, Geert
Missiaen, Ludwig
Parys, Jan
De Smedt, Humbert #
Issue Date: Jun-2004
Series Title: Biochemical and Biophysical Research Communications vol:319 issue:3 pages:888-93
Abstract: The various inositol 1,4,5-trisphosphate receptor (IP(3)R) isoforms are potential substrates for several protein kinases. We compared the in vitro phosphorylation of purified IP(3)R1 and IP(3)R3 by the catalytic subunit of protein kinase C (PKC). Phosphorylation of IP(3)R1 by PKC was about eight times stronger than that of IP(3)R3 under identical conditions. Protein kinase A strongly stimulated the PKC-induced phosphorylation of IP(3)R1. In contrast, Ca(2+) inhibited its phosphorylation (IC(50)<or=2microM) and this inhibition was further potentiated by calmodulin (CaM), while the Ca(2+)-independent CaM mutant CaM(1234) was ineffective. Ca(2+) and CaM, however, did not inhibit IP(3)R3 phosphorylation by PKC. Taken together, these findings show that Ca(2+) and CaM differentially regulate the PKC-mediated phosphorylation of IP(3)R1 and IP(3)R3 and are indicative for a role for the inhibition of IP(3)R1 phosphorylation by Ca(2+) and CaM in the negative slope of the bell-shaped effect of Ca(2+) on IP(3)R function.
URI: 
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Physiology Section (-)
Toxicology and Pharmacology
Laboratory of Molecular and Cellular Signaling
× corresponding author
# (joint) last author

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