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首页> 外文期刊>Biochemistry >Critical Role of the Isoform-Specific Region in α1-Na,K-ATPase Trafficking and Protein Kinase C-Dependent Regulation
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Critical Role of the Isoform-Specific Region in α1-Na,K-ATPase Trafficking and Protein Kinase C-Dependent Regulation

机译：亚型特异性区域在α1-Na，K-ATPase贩运和蛋白激酶C依赖性调节中的关键作用。

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The isoform-specific region (ISR) is a region of structural heterogeneity among the four isoformsnof the catalytic R-subunit of the Na,K-ATPase and an important structural determinant for isoform-specificnfunctions. In the present study, we examined the role of a potential dileucine clathrin adaptor recognitionnmotif [DE]XXXL[LI] embedded within the R1-ISR. To this end, a rat R1 construct where leucine 499 wasnreplaced by a valine (as found in the R2 isoform sequence) was compared to wild-type rat R1 after stablenexpression in opossum kidney cells. Total Na,K-ATPase expression, activity, or in situ 86nRbþ transport wasnnot affected by the L499V mutation. However, surface Na,K-ATPase expression was nearly doubled. Thisnincrease was associated with a reduced rate of internalization from the cell surface of about 50% after a 4 hnchase and became undetectable if clathrin-coated pit-mediated trafficking was blocked with chlorpromazine.nFurther, PKC-induced stimulation of Na,K-ATPase-mediated 86nRbþ uptake was doubled in mutant-nexpressing cells, comparable to the chimera containing the intact R2-ISR. Similar results were observednwhen the potential motif was disrupted by means of an E495S mutation. These findings suggest that andileucine motif embedded within the Na,K-ATPase R1-ISR plays a critical role in the surface expression ofnNa,K-ATPase R1 polypeptides at steady state and in the response to PKC activation.
机译：亚型特异性区（ISR）是Na，K-ATPase催化R亚基的四个亚型之间结构异质性的区域，也是亚型特异性功能的重要结构决定因素。在本研究中，我们研究了嵌入R1-ISR中的潜在双亮氨酸网格蛋白衔接子识别基序[DE] XXXL [LI]的作用。为此，将在鼠胚肾细胞中稳定表达后，将亮氨酸499替换为缬氨酸的大鼠R1构建体（如在R2同工型序列中发现的）与野生型大鼠R1进行了比较。 L499V突变不影响Na，K-ATPase的总表达，活性或原位86nRbþ转运。然而，表面Na，K-ATP酶表达几乎翻倍。这种增加与4hchase后细胞表面内在化率降低约50％有关，如果用氯丙嗪阻断网格蛋白包衣的基坑介导的运输，则无法检测到.n，PKC诱导的Na，K-ATPase-刺激介导突变体的细胞中，介导的86nRb 4的摄取增加了一倍，与含有完整R2-ISR的嵌合体相当。当潜在的基序被E495S突变破坏时，观察到相似的结果。这些发现表明，嵌入Na，K-ATPase R1-ISR内的雄性亮氨酸基序在稳定状态下的nNa，K-ATPase R1多肽的表面表达以及对PKC激活的响应中起关键作用。

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    《Biochemistry》 |2010年第17期|p.3602-3610|共9页
  • 作者

    Yoann Sottejeau Aude Belliard Marie-Jose Duran Thomas A. Pressley and Sandrine V. Pierre;

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    ‡Department of Physiology and Pharmacology, University of Toledo College of Medicine, Toledo, Ohio 43614, and §Center forMembrane Protein Research, Department of Cell Physiology and Molecular Biophysics, Texas Tech University Health SciencesCenter, Lubbock, Texas 79430 ) Current address: ELA Research Foundation, 26, rue de Londres, F-75009 Paris, France;

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