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Am J Physiol Cell Physiol 284: C1334-C1345, 2003. First published February 5, 2003; doi:10.1152/ajpcell.00510.2002
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Vol. 284, Issue 6, C1334-C1345, June 2003

TRANSLATIONAL PHYSIOLOGY
Nuclear CaMKII inhibits neuronal differentiation of PC12 cells without affecting MAPK or CREB activation

Louis W. Kutcher1, Shirelyn R. Beauman1, Eric I. Gruenstein2, Marcia A. Kaetzel1,3, and John R. Dedman1,3

Departments of 1 Molecular and Cellular Physiology, 2 Molecular Genetics, and 3 Genome Sciences, University of Cincinnati Medical School, Cincinnati, Ohio 45267

Ca2+/calmodulin-regulated protein kinase II (CaMKII) mediates many cellular events. The four CaMKII isoforms have numerous splice variants, three of which contain nuclear localization signals. Little is known about the role of nuclear localized CaMKII in neuronal development. To study this process, PC12 cells were transfected to produce CaMKII targeted to either the cytoplasm or the nucleus and then treated with nerve growth factor (NGF). NGF triggers a signaling cascade (MAPK) that results in the differentiation of PC12 cells into a neuronal phenotype, marked by neurite outgrowth. The present study found that cells expressing nuclear targeted CaMKII failed to grow neurites, whereas cells expressing cytoplasmic CaMKII readily produced neurites. Inhibition of neuronal differentiation by nuclear CaMKII was independent of MAPK signaling, as sustained Erk phosphorylation was not affected. Phosphorylation of CREB was also unaffected. Thus nuclear CaMKII modifies neuronal differentiation by a mechanism independent of MAPK and CREB activation.

calcium/calmodulin-dependent protein kinase II; mitogen-activated protein kinase; calmodulin; neurite outgrowth; CaMKII isoforms; extracellular signal-regulated protein kinase; cAMP-response element-binding protein


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