Rongo C, Whitfield C W, Rodal A, Kim S K, Kaplan J M
Department of Molecular and Cell Biology, University of California, Berkeley 94720-3200, USA.
Cell. 1998 Sep 18;94(6):751-9. doi: 10.1016/s0092-8674(00)81734-1.
We tested the model that neurons and epithelial cells use a shared mechanism for polarized protein sorting by comparing the pathways for localizing basolateral and postsynaptic proteins in C. elegans. GLR-1 glutamate receptors are localized to postsynaptic elements of central synapses and, when ectopically expressed, to basolateral membranes of epithelial cells. Proper localization of GLR-1 in both neurons and epithelia requires the PDZ protein LIN-10, defining LIN-10 as a shared component of the basolateral and postsynaptic localization pathways. Changing the GLR-1 carboxy-terminal sequence from a group I PDZ-binding consensus (-TAV) to a group II consensus (-FYV) restores GLR-1 synaptic localization in lin-10 mutants. Thus, these interneurons utilize at least two separate postsynaptic localization pathways.
我们通过比较秀丽隐杆线虫中基底外侧蛋白和突触后蛋白的定位途径，测试了神经元和上皮细胞使用共享机制进行极化蛋白分选的模型。GLR-1谷氨酸受体定位于中枢突触的突触后元件，当异位表达时，定位于上皮细胞的基底外侧膜。GLR-1在神经元和上皮细胞中的正确定位都需要PDZ蛋白LIN-10，这将LIN-10定义为基底外侧和突触后定位途径的共享成分。将GLR-1羧基末端序列从I类PDZ结合共有序列（-TAV）改为II类共有序列（-FYV），可恢复lin-10突变体中GLR-1的突触定位。因此，这些中间神经元至少利用两种独立的突触后定位途径。
