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Vol. 17, Issue 11, 4656-4665, November 2006

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CaMKII Association with the Actin Cytoskeleton Is Regulated by Alternative Splicing

Heather O'Leary^*, Erika Lasda, and K. Ulrich Bayer^*,,

*Department of Pharmacology, Biomedical Sciences Program, and Neuroscience Program, University of Colorado Health Sciences Center, Aurora, CO 80045

Submitted March 30, 2006; Revised August 2, 2006; Accepted August 11, 2006
Monitoring Editor: Paul Forscher

The Ca²⁺/calmodulin (CaM)-dependent protein kinase II (CaMKII) has morphogenic functions in neurons not shared by the isoform. CaMKII contains three exons (v1, v3, and v4) not present in the CaMKII gene, and two of these exons (v1 and v4) are subject to differential alternative splicing. We show here that CaMKII, but not , mediated bundling of F-actin filaments in vitro. Most importantly, inclusion of exon v1 was required for CaMKII association with the F-actin cytoskeleton within cells. CaMKIIe, which is the dominant variant around birth and lacks exon v1 sequences, failed to associate with F-actin. By contrast, CaMKII', which instead lacks exon v4, associated with F-actin as full-length CaMKII. Previous studies with CaMKII mutants have indicated a role of nonstimulated kinase activity in enhancing dendritic arborization. Here, we show that F-actin–targeted CaMKII, but not , was able to phosphorylate actin in vitro even by nonstimulated basal activity in absence of Ca²⁺/CaM. In rat pancreatic islets and in skeletal muscle, the actin-associated CaMKII' and M were the predominant variants, respectively. Thus, cytoskeletal targeting may mediate functions of CaMKII variants also outside the nervous system.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-03-0252) on August 23, 2006.

Address correspondence to: K. Ulrich Bayer (ulli.bayer{at}uchsc.edu)

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