Abstract
Protein kinase CK2 (formerly known as casein kinase II) has been viewed traditionally as a stable heterotetrameric complex, but new analytical techniques are bringing a different picture into focus. The transient nature of this complex has been highlighted by the elucidation of its structure. Furthermore, analysis of the spatiotemporal organization of individual CK2 subunits in living cells has shown that they are dynamic and that they integrate into different multimolecular assemblies. These new studies give an additional dimension to the challenge of determining the cellular regulation of this protein kinase.
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