TAILIEUCHUNG - Báo cáo khoa học: Oligomerization states of the association domain and the holoenyzme of Ca2+ ⁄CaM kinase II

Ca 2+ ⁄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. | iFEBS Journal Oligomerization states of the association domain and the holoenyzme of Ca2 CaM kinase II Oren S. Rosenberg1 3 Sebastian Deindl1 Luis R. Comolli2 Andre Hoelz5 Kenneth H. Downing2 Angus C. Nairn4 and John Kuriyan1 2 1 Department of Molecular and CellBiology and Department of Chemistry and Howard Hughes Medical institute University of California Berkeley CA USA 2 Life Sciences Division Lawrence Berkeley NationalLaboratory Berkeley CA USA 3 Department of Cell Biology and 4 Department of Psychiatry Yale University Schoolof Medicine New Haven CT USA 5 The Rockefeller University New York NY USA Keywords association domain Ca2 calmodulin dependent protein kinase II holoenzyme kinase activation oligomerization Correspondence J. Kuriyan University of California Berkeley Barker HallMC 3202 Berkeley CA 947203202 USA Fax Tel 1 510 643 0137 Fax 1 510 643 2352 E-mail kuriyan@ Website http Received 6 September 2005 revised 27 November 2005 accepted 5 December 2005 doi 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 w 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 CaMKIIa 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 .

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