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Each channel consists of two NR1 subunits, which are essential for the assembly of functional NMDA receptors, and two NR2 subunits that confer a unique set of characteristic upon the resultant NMDA receptor (Kutsuwada et al., 1992; Monyer et al., 1992). Dendritic calcium channels and hippocampal long-term depression.
The cytoplasmic C-terminals of the NR1 and NR2 subunits link the receptor to a large multi-protein complex.
The Ca3.1–3.3 channels leads to depolarization of the membrane allowing the generation of low threshold spikes that trigger bursts of Na-dependent action potentials (Llinas, 1988).
Depending on the specific channel subtype the time course of activation, inactivation, deactivation, and recovery from inactivation varies, resulting in unique biophysical properties and specific responses to action potential which can be extended during burst firing (Huguenard, 1996).
For example, by regulating the release of neurotransmitters from the presynaptic terminals it influences both long-term potentiation (LTP; Grover and Teyler, 1990; Impey et al., 1996) and long-term depression (LTD; Bolshakov and Siegelbaum, 1994; Christie et al., 1996) forms of synaptic plasticity.
These channels play a critical role toward neuronal firing both in conducting Ca currents are activated at rather negative near resting membrane potentials (Huguenard, 1996).
Specifically, they are activated during the initial depolarization phase although the highest conductance occur during the repolarization phase and return to resting membrane potential (Mc Cobb and Beam, 1991).
Moreover the expression of individual or multiple Ca H gene encoding the Cav3.2 channels have been linked to epilepsy and autism spectrum disorders (Heron et al., 2004; Splawski et al., 2006).
Receptor-operated (ligand-gated) channels open in response to the binding of specific ligands, such as neurotransmitters to the extracellular domain of the receptor. Phosphorylated CREB binds specifically to the nuclear protein CBP. Pubmed Abstract | Pubmed Full Text | Cross Ref Full Text Clarke, V. The Gβγ subunits released from receptor-coupled heteromeric G-proteins of the Gi/Go class are usually responsible for this inhibition by binding to the loop between domains I and II and the amino- and carboxy-terminal domains of Ca current) channels control transmitter release with a lower efficacy (Wu et al., 1998).