PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
PDZ domain suppression of an ER retention signal in NMDA receptor NR1 splice variants
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DOI：
10.1016/s0896-6273(00)00161-6
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发表时间：
2000-12-01
期刊：
影响因子：
16.2
通讯作者：
Wenthold, RJ
中科院分区：
文献类型：
--
作者：
Standley, S;Roche, KW;Wenthold, RJ
NMDA受体NR1亚基有四种不同的剪接变异体，它们的C末端、胞浆结构域不同。我们研究了C端盒CO、C1、C2和C2‘对NR1在异种细胞和神经元中运输的贡献。我们在NR1的C1盒中发现了一个ER保留信号(RRR)，它类似于ATP敏感K+通道中的RXR基序(Zerangue等人，1999)。我们发现NR1-3的表面表达是由于C2‘盒上的一个位点，其中包括末端4个氨基酸的PDZ相互作用结构域。该位点抑制了C1盒的内质网滞留，并导致表面表达。这些发现表明，PDZ蛋白在促进受体从细胞内池转移到神经元表面的过程中发挥了作用。
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, CO, 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.