Ontology highlight
ABSTRACT:
SUBMITTER: Bhattacharyya M
PROVIDER: S-EPMC4859805 | biostudies-literature | 2016 Mar
REPOSITORIES: biostudies-literature
eLife 20160307
Activation triggers the exchange of subunits in Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), an oligomeric enzyme that is critical for learning, memory, and cardiac function. The mechanism by which subunit exchange occurs remains elusive. We show that the human CaMKII holoenzyme exists in dodecameric and tetradecameric forms, and that the calmodulin (CaM)-binding element of CaMKII can bind to the hub of the holoenzyme and destabilize it to release dimers. The structures of CaMKII from ...[more]