Glutamate receptor-interacting protein

[4] These findings confirmed the initial hypothesis that the GRIP protein plays an important role in binding AMPA receptors to excitatory synapses.

The structure of GRIP contains seven PDZ domains and binds to the C-terminus of the GluR2 subunit of AMPA receptors.

[5] The AMPA receptor amino acid sequence that the GRIP protein binds to is ESVKI.

The conserved serine amino acid in the C- terminus of both AMPA and NMDA receptors suggests that it plays an important role in facilitating the interaction for GRIP and PSD-95.

The ratio returns to normal when constitutive recycling is allowed to happen, suggesting that the stabilization of intracellular receptors is critical only under AMPA-induced internalization.

The apparent difference in both cases is that one isoform (GRIP1b and pABP-L respectively) is capable of being conjugated with Palmitic acid, an action called Palmitoylation.

[11] GRIP-1a has been shown to reduce the expected intracellular levels of AMPA receptors after NMDA stimulation.

Mutations to GRIP1 play a role in less than 10% of confirmed cases of the group of congenital defects known as Fraser syndrome.

[13] Using immunofluorescence, it has been shown that GRIP1 is found in several kinds of embryonic tissues, including the GI tract, ureter buds, skin and oral and nasal cavities.

[15] In mouse models, knocking out GRIP1 protein leads to several deformities that begin in embryo.

These deformities include subepidermal hemorrhagic blistering, renal agenesis, syndactylism, polydactylism and cryptopthalmos.

[18] It is vitally important in initial development as knock out experiments in murine models result in skin blisters and embryonic lethality.

[18] Motor proteins such as Kinesin (KIF5) are bound to adapter molecules like GRIP1 to move cargo from the Golgi to the extremities of a neuron cell.