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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants.

The NMDA receptor NR1 subunit has four splice variants that differ in their C-terminal, cytoplasmic domain. We investigated the contribution of the C-terminal cassettes, C0, C1, C2, and C2', to trafficking of NR1 in heterologous cells and neurons. We identified an ER retention signal ( RRR) in the C1 cassette of NR1, which is similar to the RXR motif in ATP-sensitive K(+) channels (Zerangue et al., 1999). We found that surface expression of NR1-3, which contains C1, is due to a site on the C2' cassette, which includes the terminal 4 amino acid PDZ-interacting domain. This site suppresses ER retention of the C1 cassette and leads to surface expression. These findings suggest a role for PDZ proteins in facilitating the transition of receptors from an intracellular pool to the surface of the neuron.[1]

References

  1. PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants. Standley, S., Roche, K.W., McCallum, J., Sans, N., Wenthold, R.J. Neuron (2000) [Pubmed]
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