Nonisotopic Signaling Cascades

Traditionally, ionotropic receptors signal by ion flux through their ion channels. However, recent studies reported new signaling mechanisms, such as association with G-proteins, protein tyrosine kinases, or calmodulin. For example, AMPA receptors have been reported to be associated with Gail (80), and pertussis toxin-sensitive MAP kinase activation was observed after AMPA receptor activation (81). Furthermore, in retinal ganglion cells, an AMPA-induced suppression of the cGMP-gated current could be blocked by pertussis toxin (82). Moreover, the C-tail of GluR2 was found to associate with the Src-family kinase Lyn, and in cerebellar granule cell cultures, stimulation of AMPA receptors resulted in Lyn activation and subsequent MAP kinase activation (83). Finally, kainate receptors may couple to Gi/G0 proteins in the hippocampus and inhibit GABA release presynaptically (84,85).

NMDA receptors coimmunoprecipitate with Src protein and phospholipase C, and the NR2B C-tail has a high affinity for autophosphorylated CAMKII. Moreover, the C-terminus of the NR2D subunit can associate with the SH3 domain of c-Abl, but not other tested tyrosine kinases, and inhibit c-Abl (86). Furthermore, the calcium-dependent binding of calmodulin to the C1 cassette of NR1 can be weakened by PKC phosphorylation. Both PKC phosphorylation and calmodulin binding weakens the association of NR1 with spectrin.

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