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首页> 外文期刊>American Journal of Physiology >Shank2 contributes to the apical retention and intracellular redistribution of NaPiIIa in OK cells
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Shank2 contributes to the apical retention and intracellular redistribution of NaPiIIa in OK cells

机译：Shank2有助于OK细胞中NaPiIIa的根尖保留和细胞内重新分布

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摘要

In renal proximal tubule (PT) cells, sodium-phosphate cotransporter IIa (NaPiIIa) is normally concentrated within the apical membrane where it reabsorbs -70% of luminal phosphate (Pi). NaPiIIa activity is acutely regulated by moderating its abundance within the apical membrane. Under low-Pi conditions, NaPiIIa is retained within the apical membrane. Under high-Pi conditions, NaPiIIa is retrieved from the apical membrane and trafficked to the lysosomes for degradation. The present study investigates the role of Shank2 in regulating the distribution of NaPiIIa. In opossum kidney cells, a PT cell model, knockdown of Shank2 in cells maintained in low-Pi media resulted in a marked decrease in NaPiIIa abundance. After being transferred into high-Pi media, live-cell imaging showed that mRFP-Shank2E and GFP-NaPiIIa underwent endocytosis and trafficked together through the subapical domain. Fluorescence cross-correlation spectroscopy demonstrated that GFP-NaPiIIa and mRFP-Shank2 have indistinguishable diffusion coefficients and migrated through the subapical domain in temporal synchrony. Raster image cross-correlation spectroscopy demonstrated these two proteins course through the subapical domain in temporal-spatial synchrony. In the microvilli of cells under low-Pi conditions and in the subapical domain of cells under high-Pi conditions, fluorescence lifetime imaging microscopy-Forster resonance energy transfer analysis of Cer-NaPiIIa and EYFP-Shank2E found these fluors reside within 10 nm of each other. Demonstrating a complexity of functions, in cells maintained under low-Pi conditions, Shank2 plays an essential role in the apical retention of NaPiIIa while under high-Pi conditions Shank2 remains associated with NaPiIIa and escorts NaPiIIa through the cell interior.
机译：在肾近端小管（PT）细胞中，磷酸钠共转运蛋白IIa（NaPiIIa）通常集中在心尖膜内，在该膜中它重新吸收-70％的磷酸鲁米那（Pi）。 NaPiIIa活性通过调节其在根尖膜内的丰度而受到严格调节。在低Pi条件下，NaPiIIa被保留在根尖膜内。在高Pi条件下，NaPiIIa从根尖膜中回收并运输到溶酶体进行降解。本研究调查了Shank2在调节NaPiIIa分布中的作用。在负鼠肾细胞（一种PT细胞模型）中，在低Pi培养基中维持的细胞中Shank2的敲低导致NaPiIIa丰度明显降低。转移到高Pi培养基中后，活细胞成像显示mRFP-Shank2E和GFP-NaPiIIa经历了内吞作用，并一起通过根尖下区域转运。荧光互相关光谱表明，GFP-NaPiIIa和mRFP-Shank2具有不可区分的扩散系数，并在时间同步下迁移通过根下区域。光栅图像互相关光谱表明，这两种蛋白在时空同步过程中通过了根尖下区域。在低Pi条件下的细胞微绒毛和高Pi条件下的细胞的尖顶下，Cer-NaPiIIa和EYFP-Shank2E的荧光寿命成像显微镜-Forster共振能量转移分析发现这些荧光分别存在于10 nm内其他。在低Pi条件下维持的细胞中，Shank2在NaPiIIa的根尖保留中起着至关重要的作用，而Shank2在高Pi条件下仍与NaPiIIa相关并通过细胞内部护送NaPiIIa，这证明了功能的复杂性。

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