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Neurogranin, a link between calcium/calmodulin and protein kinase C signaling in synaptic plasticity
Article first published online: 21 JUL 2010
Copyright © 2010 Wiley Periodicals, Inc.
Volume 62, Issue 8, pages 597–606, August 2010
How to Cite
Díez-Guerra, F. J. (2010), Neurogranin, a link between calcium/calmodulin and protein kinase C signaling in synaptic plasticity. IUBMB Life, 62: 597–606. doi: 10.1002/iub.357
- Issue published online: 28 JUL 2010
- Article first published online: 21 JUL 2010
- Manuscript Accepted: 24 MAY 2010
- Manuscript Received: 24 APR 2010
- The Spanish Ministry of Science and Technology. Grant Number: BFI2002–01581
- protein kinase C;
- synaptic plasticity;
Neurogranin (Ng) (also named RC3, p17 or BICKS) is a small protein originally identified in rat brain and abundantly expressed in several telencephalic areas, such as the cerebral cortex, hippocampus, amygdala, and striatum. In neurons, it is found concentrated at dendritic spines where it participates in synaptic signaling events through the regulation of calmodulin (CaM) availability. Ng features an IQ motif that mediates its interaction with CaM and phosphatidic acid (PA) and that is phosphorylated by protein kinase C (PKC) at serine 36 (Ser36). Ser36-phosphorylated Ng is unable to bind either CaM or PA. Ng knockout mice display an apparently normal phenotype; however, they show severe deficits in spatial and emotional learning and a decrease in LTP induction, mostly due to the attenuation of the signaling that depends on calcium/CaM kinase II (CaMKII), PKC, and protein kinase A (PKA) activation. The present review is an update on the most relevant information about Ng expression, localization, interactions, and modifications as well as on its role in synaptic plasticity. © 2010 IUBMB IUBMB Life, 62(8): 594–606, 2010.