EurekaMag.com logo
+ Site Statistics
References:
53,869,633
Abstracts:
29,686,251
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on LinkedInFollow on LinkedIn

+ Translate

Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain



Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain



Journal of Biological Chemistry 265(19): 11204-11212



It is now well established that autophosphorylation of a threonine residue located next to each calmodulin-binding domain in the subunits of type II Ca2+/calmodulin-dependent protein kinase causes the kinase to remain active, although at a reduced rate, after Ca2+ is removed from the reaction. This autophosphorylated form of the kinase is still sensitive to Ca2+/calmodulin, which is required for a maximum catalytic rate. After removal of Ca2+, new sites are autophosphorylated by the partially active kinase. Autophosphorylation of these sites abolishes sensitivity of the kinase to Ca2+/calmodulin (Hashimoto, Y., Schworer, C. M., Colbran, R. J., and Soderling, T. R. (1987) J. Biol. Chem. 262, 8051-8055). We have identified two pairs of homologous residues, Thr305 and Ser314 in the alpha subunit and Thr306 and Ser315 in the beta subunit, that are autophosphorylated only after removal of Ca2+ from an autophosphorylation reaction. The sites were identified by direct sequencing of labeled tryptic phosphopeptides isolated by reverse-phase high pressure liquid chromatography. Thr305-306 is rapidly dephosphorylated by purified protein phosphatases 1 and 2A, whereas Ser314-315 is resistant to dephosphorylation. We have shown by selective dephosphorylation that the presence of phosphate on Thr305-306 blocks sensitivity of the kinase to Ca2+/calmodulin. In contrast, the presence of phosphate on Ser314-315 is associated with an increase in the Kact for Ca2+/calmodulin of only about 2-fold, producing a relatively small decrease in sensitivity to Ca2+/calmodulin.

(PDF emailed within 1 workday: $29.90)

Accession: 017756339

Download citation: RISBibTeXText

PMID: 2162838



Related references

Activation of type ii calcium calmodulin dependent protein kinase by calcium calmodulin is inhibited by autophosphorylation of threonine within the calmodulin binding domain. Journal of Biological Chemistry 265(19): 11204-11212, 1990

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

Interactions of the autophosphorylation sites of calcium calmodulin dependent protein kinase ii with the calmodulin binding domain. FASEB Journal 2(5): ABSTRACT 4048, 1988

Cloning and characterization of an apple malus domestica l. borkh cdna encoding a calmodulin binding protein domain similar to the calmodulin binding region of type ii mammalian calcium calmodulin dependent protein kinase. Plant Science (Shannon) 81(2): 227-235, 1992

Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. Embo Journal 14(15): 3679-3686, 1995

Inactivation of calmodulin-dependent protein kinase IV by autophosphorylation of serine 332 within the putative calmodulin-binding domain. Journal of Biological Chemistry 271(12): 6903-6910, 1996

A calcium/calmodulin-binding serine/threonine protein kinase homologous to the mammalian type II calcium/calmodulin-dependent protein kinase is expressed in plant cells. Plant Physiology 101(4): 1381-1384, 1993

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

Cloning and characterization of an apple (Malus domestica (L.) Borkh) cDNA encoding a calmodulin-binding protein domain similar to the calmodulin-binding region of type II mammalian Ca2+/calmodulin-dependent protein kinase. Plant Science Limerick 81(2): 227-235, 1992

Calcium 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): 13486-13489, 1988

Mapping of the calmodulin binding domain of calcium calmodulin dependent protein kinase ii. Clinical Research 36(3): 622A, 1988

Mapping of calmodulin binding domain of calcium calmodulin dependent protein kinase ii from rat brain. Biochemical & Biophysical Research Communications 152(1): 122-128, 1988

Regulation of multifunctional calcium calmodulin dependent protein kinase by calmodulin and by autophosphorylation. Journal of Cell Biology 107(6 PART 3): 445A, 1988

The neural visinin-like domain of the chimeric Ca2+/calmodulin-dependent protein kinase from plants regulates autophosphorylation and calmodulin affinity. Plant Biology (Rockville) : 33-34, 2000

Calmodulin rapping and autophosphorylation in calcium/calmodulin dependent protein kinase II. Biophysical Journal 74(2 PART 2): A379, 1998