CAMK2D (assoc. domain)
CAMK2D (assoc. domain): Human calcium/calmodulin-dependent protein kinase (CaM kinase) II delta, association domain
PDB Code: 2W2C
The protein kinase CAMK2δ is ubiquitously expressed and forms oligomeric, ring like structures composed of 6-12 subunits. There are four isoforms present in mammalian cells (alpha, beta, gamma, and delta).
CAMK2δ is one of the most important transducers of Ca2+ signals and has been linked to a multitude of pathways. Regulatory functions for CAMK2δ have been suggested in cardiomyocyte apoptosis and functional remodelling of the developing heart, signal transduction in lymphocytes, stabilization of the cytoskeleton in neuritis as well as long-term potentiation and neurotransmitter release. It may also be involved in regulation of insulin secretion and glucose transport and is a positive regulator of serum-stimulated proliferation of vascular smooth muscle cells.
The pathophysiological role of CAMK2δ in cardiac hypertrophy and heart failure has been confirmed in several transgenic mouse models over-expressing different isoforms in the heart, which all develop cardiomyopathies. Moreover, inhibition of CAMKII has been shown to inhibit arrhythmias.
The overall organization of each of the four CAMK2 isoforms is similar: an N-terminal catalytic domain is followed by a regulatory domain that contains an autoinhibitory region with a calmodulin (CaM) binding site and a C-terminal association domain, through which the subunits interact to assemble into holoenzymes. A variable domain is located between the CaM-binding domain and the association domain. CAMK2δ is activated by a two step activation process: The first activation event involves the dissociation of the autoinhibitory regulatory segment. This process involves binding of Ca2+/CaM which leads to the exposure of a regulatory threonine residue. The now accessible threonine is phosphorylated by a neighboring kinase domain within the oligomeric dodecameric assembly. Once activated phosphorylation prevents rebinding of the regulatory segment to the kinase domain and tighter binding of Ca2+/CaM. Thus, at high Ca2+/CaM concentration the phosphorylation at the regulatory threonine propagates rapidly through the holoenzyme resulting in active Ca2+/CaM-independent CAMK2δ.
Here we present the structure of CAMK2δ C-terminal oligomerization domain at 2.7Å resolution which oligomerized as a 14mer forming two stacked 7 membered rings. Previously we have also solved the catalytic domain of CAMK2δ (PDB ID 2VN9).
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