- Title
- Modulation of the phosphorylation and activity of calcium/calmodulin-dependent protein kinase II by zinc
- Creator
- Lengyel, Imre; Fieuw-Makaroff, Sabine; Hall, Amanda L.; Sim, Alistair T.M.; Rostas, John A. P.; Dunkley, Peter R.
- Relation
- Journal of Neurochemistry Vol. 75 , Issue 2, p. 594-605
- Relation
- http://www3.interscience.wiley.com/journal/119005299/abstract?CRETRY=1&SRETRY=0
- Publisher
- Wiley-Blackwell Publishing Ltd
- Resource Type
- journal article
- Date
- 2000
- Description
- Calcium/calmodulin-dependent protein kinase II (CaMPK-II) is a key regulatory enzyme in living cells. Modulation of its activity, therefore, could have a major impact on many cellular processes. We found that Zn²⁺ has multiple functional effects on CaMPK-II. Zn²⁺ generated a Ca²⁺/CaM-independent activity that correlated with the autophosphorylation of Thr²⁸⁶, inhibited Ca²⁺/CaM binding that correlated with the autophosphorylation of Thr³⁰⁶, and inhibited CaMPK-II activity at high concentrations that correlated with the autophosphorylation of Ser²⁷⁹. The relative level of autophosphorylation of these three sites was dependent on the concentration of zinc used. The autophosphorylation of at least these three sites, together with Zn²⁺ binding, generated an increased mobility form of CaMPK-II on sodium dodecyl sulfate gels. Overall, autophosphorylation induced by Zn²⁺ converts CaMPK-II into a different form than the binding of Ca2+/CaM. In certain nerve terminals, where Zn²⁺ has been shown to play a neuromodulatory role and is present in high concentrations, Zn²⁺ may turn CaMPK-II into a form that would be unable to respond to calcium signals.
- Subject
- zinc; calcium/calmodulin; calcium/calmodulin-stimulated protein kinase II; autonomous activity; autophosphorylation; phosphorylation site analysis
- Identifier
- http://hdl.handle.net/1959.13/32221
- Identifier
- uon:2957
- Identifier
- ISSN:0022-3042
- Language
- eng
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