+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Regulatory interactions of calmodulin-binding proteins: phosphorylation of calcineurin by autophosphorylated Ca2+/calmodulin-dependent protein kinase II



Regulatory interactions of calmodulin-binding proteins: phosphorylation of calcineurin by autophosphorylated Ca2+/calmodulin-dependent protein kinase II



Proceedings of the National Academy of Sciences of the United States of America 85(18): 7001-7005



The Ca2+/calmodulin (CaM)-dependent protein phosphatase calcineurin is rapidly phosphorylated (0.8 mol of 32PO4 per mol of 60-kDa subunit of calcineurin) by brain Ca2+/CaM-dependent protein kinase II (CaM-kinase II). This reaction requires the autophosphorylated, Ca2+-independent form of CaM-kinase II since Ca2+/CaM binding to calcineurin inhibits phosphorylation. However, the phosphorylation reaction does require Ca2+, presumably acting through the 19-kDa subunit of calcineurin. Calcineurin is a good substrate for CaM-kinase II, with a Km of 19 microM and Vmax of 2.4 mumol/min per mg. Phosphorylation of calcineurin changed its phosphatase activity with either a 2-fold increase in Km (32P-labeled myosin light chain as substrate) or a 50% decrease in Vmax (p-nitrophenyl phosphate as substrate). The phosphorylated calcineurin exhibited very slow autodephosphorylation (0.09 nmol/min per mg) but was effectively dephosphorylated by brain protein phosphatase IIA. Dephosphorylation, like phosphorylation, was blocked by high concentrations of Ca2+/CaM and stimulated by Ca2+ alone. Thus calcineurin has a regulatory phosphorylation site that is phosphorylated by the Ca2+-independent form of CaM-kinase II and blocked by high concentrations of Ca2+/CaM.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 041214299

Download citation: RISBibTeXText

PMID: 2842800

DOI: 10.2307/32510


Related references

Regulatory interactions of calmodulin dependent proteins phosphorylation of calcineurin by calcium calmodulin dependent protein kinase ii. FASEB Journal 2(5): ABSTRACT 4050, 1988

Phosphorylation regulation of calmodulin binding proteins by autophosphorylated calcium calmodulin dependent protein kinase ii. Journal of Cell Biology 107(6 Part 3): 285A, 1988

Regulatory interactions of the calmodulin-binding, inhibitory, and autophosphorylation domains of Ca2+/calmodulin-dependent protein kinase II. Journal of Biological Chemistry 263(34): 18145-18151, 1988

Nitric oxide synthase regulatory sites phosphorylation by cyclic amp dependent protein kinase protein kinase c and calcium calmodulin protein kinase identification of flavin and calmodulin binding sites. Journal of Biological Chemistry 267(16): 10976-10981, 1992

Interaction of autophosphorylated Ca2+/calmodulin-dependent protein kinase II with neuronal cytoskeletal proteins. Characterization of binding to a 190-kDa postsynaptic density protein. Journal of Biological Chemistry 270(17): 10043-9, 1995

Regulation of calcineurin by phosphorylation. Identification of the regulatory site phosphorylated by Ca2+/calmodulin-dependent protein kinase II and protein kinase C. Journal of Biological Chemistry 264(28): 16524-9, 1989

Regulation of calcineurin by phosphorylation identification of the regulatory site phosphorylated by calcium calmodulin dependent protein kinase ii and protein kinase c. Journal of Biological Chemistry 264(28): 16524-16529, 1989

Regulation of Ca2+/calmodulin-dependent cyclic nucleotide phosphodiesterase by the autophosphorylated form of Ca2+/calmodulin-dependent protein kinase II. Journal of Biological Chemistry 264(18): 10884-7, 1989

Calcium calmodulin independent autophosphorylation sites of calcium calmodulin dependent protein kinase ii studies on the effect of phosphorylation of threonine 305 306 and serine 314 on calmodulin binding using synthetic peptides. Journal of Biological Chemistry 265(19): 11213-11219, 1990

Detection of calmodulin-binding proteins and calmodulin-dependent phosphorylation linked to calmodulin-dependent chemotaxis to folic and cAMP in Dictyostelium. Cellular Signalling 13(8): 575-584, 2001

Calcium dependent and calmodulin dependent phosphorylation of calspectin spectrin like calmodulin binding protein fodrin by protein kinase systems in synaptosomal cytosol and membranes. Biomedical Research 3(5): 561-570, 1982

In vitro phosphorylation of bovine cardiac muscle high molecular weight calmodulin binding protein by cyclic AMP-dependent protein kinase and dephosphorylation by calmodulin-dependent phosphatase. Molecular & Cellular Biochemistry. 177(1-2): 215-219,., 1997

In vitro phosphorylation of bovine cardiac muscle high molecular weight calmodulin binding protein by cyclic AMP-dependent protein kinase and dephosphorylation by calmodulin-dependent phosphatase. Molecular and Cellular Biochemistry 177(1-2): 215-219, 1997

The regulatory region of calcium/calmodulin-dependent protein kinase I contains closely associated autoinhibitory and calmodulin-binding domains. Journal of Biological Chemistry 270(40): 23851-9, 1995

Ca2+/calmodulin-dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains. Journal of Biological Chemistry 263(27): 13486-9, 1988