+ 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

Site-specific phosphorylation of the purified receptor for calcium-channel blockers by cAMP- and cGMP-dependent protein kinases, protein kinase C, calmodulin-dependent protein kinase II and casein kinase II



Site-specific phosphorylation of the purified receptor for calcium-channel blockers by cAMP- and cGMP-dependent protein kinases, protein kinase C, calmodulin-dependent protein kinase II and casein kinase II



European Journal of Biochemistry 178(2): 535-542



Five protein kinases were used to study the phosphorylation pattern of the purified skeletal muscle receptor for calcium-channel blockers (CaCB). cAMP kinase, cGMP kinase, protein kinase C, calmodulin kinase II and casein kinase II phosphorylated the 165-kDa and the 55-kDa proteins of the purified CaCB receptor. The 130/28-kDa and the 32-kDa protein of the receptor are not phosphorylated by these protein kinases. Among these protein kinases only cAMP kinase phosphorylated the 165-kDa subunit with 2-3-fold higher initial rate than the 55-kDa subunit. Casein kinase II phosphorylated the 165-kDa and the 55-kDa protein of the receptor with comparable rates. cGMP kinase, protein kinase C and calmodulin kinase II phosphorylated preferentially the 55-kDa protein. The 55-kDa protein is phosphorylated 50 times faster by cGMP kinase and protein kinase C than by calmodulin kinase II or casein kinase II and about 10 times faster by these enzymes than by cAMP kinase. Two-dimensional peptide maps of the 165-kDa subunit yielded a total of 11 phosphopeptides. Four or five peptides are phosphorylated specifically by cAMP kinase, cGMP kinase, casein kinase II and protein kinase C, whereas the other peptides are modified by several kinases. The same kinases phosphorylate 11 peptides in the 55-kDa subunit. Again, some of these peptides are modified specifically by each kinase. These results suggest that the 165-kDa and the 55-kDa subunit contain specific phosphorylation sites for cAMP kinase, cGMP kinase, casein kinase II and protein kinase C. Phosphorylation of these sites may be relevant for the in vivo function of the CaCB receptor.

Please choose payment method:






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

Accession: 041376030

Download citation: RISBibTeXText

PMID: 2850184

DOI: 10.1111/j.1432-1033.1988.tb14480.x


Related references

Conserved phosphorylation of the intracellular domains of GABA(A) receptor beta2 and beta3 subunits by cAMP-dependent protein kinase, cGMP-dependent protein kinase protein kinase C and Ca2+/calmodulin type II-dependent protein kinase. Neuropharmacology 36(10): 1377-1385, 1997

Ethanol has no effect on camp dependent protein kinase protein kinase c or calcium calmodulin dependent protein kinase ii stimulated phosphorylation of highly purified substrates in vitro. Alcoholism Clinical & Experimental Research 15(6): 1040-1044, 1991

Phosphorylation of P1, a high mobility group-like protein, catalyzed by casein kinase II, protein kinase C, cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II. Febs Letters 258(1): 106-108, 1989

Ethanol has no effect on cAMP-dependent protein kinase-, protein kinase C-, or Ca(2+)-calmodulin-dependent protein kinase II-stimulated phosphorylation of highly purified substrates in vitro. Alcoholism Clinical and Experimental Research 15(6): 1040-1044, 1991

Phosphorylation of the purified receptor for calcium channel blockers by cAMP kinase and protein kinase C. European Journal of Biochemistry 169(1): 137-142, 1987

Differential phosphorylation of intracellular domains of gamma-aminobutyric acid type A receptor subunits by calcium/calmodulin type 2-dependent protein kinase and cGMP-dependent protein kinase. Journal of Biological Chemistry 269(27): 18111-7, 1994

Differential phosphorylation of intracellular domains of c-aminobutyric acid type A receptor subunits by calcium/calmodulin type 2-dependent protein kinase and cGMP-dependent protein kinase. The Journal of Biological Chemistry 269: 111-17, 1994

Activators of protein kinase c increase the phosphorylation of the synapsins at sites phosphorylated by camp dependent and calcium calmodulin dependent protein kinases in the rat hippocampal slice. Synapse (New York) 10(1): 62-70, 1992

Phosphorylation of the heavy chain of purified bovine aortic smooth muscle myosin by calcium calmodulin dependent protein kinase ii and casein kinase ii. Journal of Cell Biology 107(6 Part 3): 679A, 1988

Phosphorylation of connexin 32, a hepatocyte gap-junction protein, by cAMP-dependent protein kinase, protein kinase C and Ca2+/calmodulin-dependent protein kinase II. European Journal of Biochemistry 192(2): 263-273, 1990

Bidirectional control of phospholipase A2 activity by Ca2+/calmodulin-dependent protein kinase II, cAMP-dependent protein kinase, and casein kinase II. Proceedings of the National Academy of Sciences of the United States of America 88(15): 6770-6774, 1991

Phosphorylation of connexin 32 a hepatocyte gap junction protein by cyclic amp dependent protein kinase protein kinase c and calcium ion calmodulin dependent protein kinase ii. European Journal of Biochemistry 192(2): 263-274, 1990

Phosphorylation of cytochrome P4502E1 (CYP2E1) by calmodulin dependent protein kinase, protein kinase C and cAMP dependent protein kinase. Alcohol and Alcoholism 28(4): 445-451, 1993

Phosphorylation of keratin intermediate filaments by protein kinase C, by calmodulin-dependent protein kinase and by cAMP-dependent protein kinase. European Journal of Biochemistry 197(2): 281-290, 1991

Effects of protein kinase modulator on cAMP-and cGMP-dependent protein kinase-catalyzed phosphorylation and the rate of calcium uptake by cardiac microsomes. Journal of Molecular and Cellular Cardiology 9(11-Supp-S): 45-45, 1977