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Background
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PDZ domain, but not the AH domain, of PICK1 interacts with the C termini of the GTP-bound forms of ADP-ribosylation factor-1 (ARF1) and ARF3. The interactions with ARF5 and ARF6 are weak, suggesting that the PICK1 interaction is specific for class I ARFs and that it may regulate Golgi-to-endoplasmic reticulum vesicle transport. The PDZ domain of rat Pick1 interacts with the last 10 amino acids of the short C-terminal alternative splice variants of AMPA receptor subunits. It has thus been proposed that E-S-V/I-K-I, a sequence found in these 10 amino acids, is a novel PDZ-binding motif. PRKCA phosphorylates Pick1 efficiently but binds Pick1 in both the phosphorylated and unphosphorylated states. Consistent with a neuronal role for PICK1, the mouse homolog interacts with mouse AMPA glutamate receptors and colocalizes at excitatory synapses in the brain. Metabotropic glutamate receptor-7 (mGluR7) localizes specifically to presynaptic active zones. The extreme C-terminal 3 amino acids of mGluR7 have been shown to interact with the PDZ domain of PICK1. Immunofluorescence microscopy demonstrated that both proteins are localized at excitatory synapses in hippocampal neurons, with clustering of mGluR7 at synapses requires PICK1 C-terminal PDZ-binding residues. Mutant mGluR7 lacking the PDZ-binding residues localized diffusely along axons rather than at the synapse, suggesting a role for Pick1 as a scaffolding molecule at presynaptic sites.
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Background
References
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