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Published February 2006 | Supplemental Material
Journal Article Open

Oligomerization states of the association domain and the holoenyzme of Ca²⁺/CaM kinase II


Ca²⁺/calmodulin activated protein kinase II (CaMKII) is an oligomeric protein kinase with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by the association domain, a C‐terminal region of ≈ 140 residues in the CaMKII polypeptide. Single particle analyses of electron micrographs have suggested previously that the holoenyzme forms a dodecamer that contains two stacked 6‐fold symmetric rings. In contrast, a recent crystal structure of the isolated association domain of mouse CaMKIIα has revealed a tetradecameric assembly with two stacked 7‐fold symmetric rings. In this study, we have determined the crystal structure of the Caenorhabditis elegans CaMKII association domain and it too forms a tetradecamer. We also show by electron microscopy that in its fully assembled form the CaMKII holoenzyme is a dodecamer but without the kinase domains, either from expression of the isolated association domain in bacteria or following their removal by proteolysis, the association domains form a tetradecamer. We speculate that the holoenzyme is held in its 6‐fold symmetric state by the interactions of the N‐terminal ≈ 1–335 residues and that the removal of this region allows the association domain to convert into a more stable 7‐fold symmetric form.

Additional Information

© 2006 The Authors. Journal compilation © 2006 FEBS. Received 6 September 2005, revised 27 November 2005, accepted 5 December 2005. We thank Robert Glaeser, Pietro de Camilli, Karin Reinisch and Cori Bargmann for helpful discussions. We thank Xiaoxian Cao, Holger Sondermann, Cori Ralston, David King and Arnie Falick for invaluable technical expertise. The cDNA for UNC‐43 splice variant K11E8.d was a kind gift of Dr Min Han. Oren Rosenberg is supported by the Yale Medical Scientist Training Grant. Parts of this work have been supported by the Director, Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy under Contract No. DE‐AC02‐05CH11231.

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