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The interaction causes a conformational change in the structure of the protein that leads to the opening of the channel pore and subsequent ion flux across the plasma membrane. Most ROCs are permeable to Ca and represent an important mechanism for the generation of second messengers.
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).
This interaction facilitates the localization of the receptor in specific areas, such as the postsynaptic density (PSD), and the connection to a variety of downstream signaling molecules (Traynelis et al., 2010).
In particular, NMDA-dependent Ca influxes are known to regulate CREB-dependent gene transcription (Hardingham et al., 1999, 2001a,b; Impey and Goodman, 2001; Wu et al., 2001) which has considerable physiological relevance for the establishment of long-term synaptic plasticity and learning and memory (Barco et al., 2002).
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).
This is probably due to the fact the although they are localized at the cell body, dendrites and presynaptic terminal, their position is further away from the release sites (Yokoyama et al., 1995; Day et al., 1996; Wu et al., 1999).