AKAP79/150 interacts with the neuronal calcium-binding protein caldendrin
Article first published online: 10 JUL 2012
© 2012 The Authors. Journal of Neurochemistry © 2012 International Society for Neurochemistry
Journal of Neurochemistry
Volume 122, Issue 4, pages 714–726, August 2012
How to Cite
Gorny, X., Mikhaylova, M., Seeger, C., Reddy, P. P., Reissner, C., Schott, B. H., Helena Danielson, U., Kreutz, M. R. and Seidenbecher, C. (2012), AKAP79/150 interacts with the neuronal calcium-binding protein caldendrin. Journal of Neurochemistry, 122: 714–726. doi: 10.1111/j.1471-4159.2012.07828.x
- Issue published online: 17 JUL 2012
- Article first published online: 10 JUL 2012
- Accepted manuscript online: 13 JUN 2012 11:12AM EST
- Received December 22, 2011; revised manuscript received May 24, 2012; accepted May 28, 2012.
- calcium sensor protein;
- postsynaptic density;
- surface plasmon resonance
J. Neurochem. (2012) 122, 714–726.
The A kinase-anchoring protein AKAP79/150 is a postsynaptic scaffold molecule and a key regulator of signaling events. At the postsynapse it coordinates phosphorylation and dephosphorylation of receptors via anchoring kinases and phosphatases near their substrates. Interactions between AKAP79 and two Ca2+ -binding proteins caldendrin and calmodulin have been investigated here. Calmodulin is a known interaction partner of AKAP79/150 that has been shown to regulate activity of the kinase PKC in a Ca2+-dependent manner. Pull-down experiments and surface plasmon resonance biosensor analyses have been used here to demonstrate that AKAP79 can also interact with caldendrin, a neuronal calcium-binding protein implicated in regulation of Ca2+ -influx and release. We demonstrate that calmodulin and caldendrin compete for a partially overlapping binding site on AKAP79 and that their binding is differentially dependent on calcium. Therefore, this competition is regulated by calcium levels. Moreover, both proteins have different binding characteristics suggesting that the two proteins might play complementary roles. The postsynaptic enrichment, the complex binding mechanism, and the competition with calmodulin, makes caldendrin an interesting novel player in the signaling toolkit of the AKAP interactome.