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首页> 外文期刊>Journal of Cellular Physiology >Identification of basolateral membrane targeting signal of human sodium-dependent dicarboxylate transporter 3.
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Identification of basolateral membrane targeting signal of human sodium-dependent dicarboxylate transporter 3.

机译：基底膜目标的识别信号的人类sodium-dependent dicarboxylate运输3。

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摘要

Sodium-dependent dicarboxylate transporters (NaDC) include low-affinity NaDC1 and high-affinity NaDC3. Despite high similarities structurally and functionally, both are localized to opposite surfaces of renal tubular cells. The molecular mechanisms and localization signals leading to this polarized distribution remain unknown. In this study, distribution of NaDC3 in human kidney tissue was firstly observed by immunohistochemistry and immunofluorescence. Then, EGFP-fused wild-type, NH2- and COOH-terminal deletion and point mutants of NaDC3, and chimera between NaDC3 and NaDC1, were generated and transfected into polarized renal cells lines, LLC-PK1 and MDCK. Their subcellular localizations were analyzed by laser confocal microscopy. Immunolocalization results revealed that NaDC3 was expressed at basolateral membrane of human renal proximal tubular epithelia. Confocal examinations showed that wild-type NaDC3 was targeted to the basolateral membrane of MDCK and LLC-PK1. Deletion mutations indicated that the basolateral targeting signal of NaDC3 located within a short sequence AKKVWSARR of its amino-terminal cytoplasmic domain. Addition of this sequence could redirect apical NaDC1 to the basolateral membrane of LLC-PK1. Point mutagenesis revealed that mutation of either of two hydrophobic amino acids V and W in this short sequence largely redirected NaDC3 to both apical and basolateral surfaces of LLC-PK, indicating that the two hydrophobic amino acids are critical for the basolateral targeting of NaDC3. Our studies provide direct evidence of the localization of NaDC3 at the basolateral membrane of human renal proximal tubule cells and identify a di-hydrophobic amino acid motif VW as basolateral localization signal in the N-terminal cytoplasmic domain of NaDC3.
机译：Sodium-dependent dicarboxylate转运蛋白(NaDC)包括低亲和力NaDC1和高亲和性NaDC3。功能上,两者都是本地化的相反肾小管细胞的表面。导致机制和定位信号这个偏振分布仍然未知。这项研究中,人类肾脏NaDC3分布组织首先观察到免疫组织化学和免疫荧光。然后,EGFP-fused野生型氨基-COOH-terminal删除和点突变体NaDC3,妄想NaDC3和NaDC1之间生成并转染成两极分化的肾细胞,LLC-PK1和MDCK。本地化分析激光共焦显微镜。在基底膜,NaDC3表示人肾近端小管上皮细胞。共焦检查表明,野生型NaDC3是针对MDCK的基底膜吗和LLC-PK1。基底外侧的目标信号NaDC3所在地在一个短序列AKKVWSARR的伴胞质域。这个序列可以重定向顶端NaDC1LLC-PK1的基底膜。诱变透露,变异的两个疏水氨基酸在这短V和W序列主要重定向NaDC3顶端LLC-PK基底表面,指示这两个疏水氨基酸是至关重要的NaDC3基底外侧定位。研究提供直接的证据本地化的NaDC3基底外侧膜人肾近端小管细胞和识别大众di-hydrophobic氨基酸基序基底外侧定位信号的n端胞质域NaDC3。

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