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首页> 外文期刊>American Journal of Physiology >Cytoplasmic targeting signals mediate delivery of phospholemman to the plasma membrane.
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Cytoplasmic targeting signals mediate delivery of phospholemman to the plasma membrane.

机译：细胞质靶向信号介导磷脂质向膜的传递。

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摘要

The FXYD protein family consists of several small, single-span membrane proteins that exhibit a high degree of homology. The best-known members of the family include the gamma-subunit of the Na(+)-K(+)-ATPase and phospholemman (PLM), a phosphoprotein of cardiac sarcolemma. Other members of the family include corticosteroid hormone-induced factor (CHIF), mammary tumor protein of 8 kDa (Mat-8), and related to ion channels (RIC). The exact physiological roles of the FXYD proteins remain unknown. To better characterize the function of the members of the FXYD protein family, we expressed several members of the family in Madin-Darby canine kidney (MDCK) cells. All of the FXYD proteins, with the exception of PLM, were primarily found in the basolateral plasma membrane. Surprisingly, PLM, a previously characterized plasma membrane protein, was found to colocalize with the endoplasmic reticulum marker protein disulfide isomerase. Treatment of MDCK cells expressing PLM with an agonist of PKC caused some of the PLM to be redistributed to the plasma membrane. Site-directed mutagenesis of residues within the cytoplasmic domain of PLM indicated that a negative charge at Ser69 is necessary to shift the localization of PLM to the plasma membrane. In addition, other regions of PLM necessary for either its endoplasmic reticulum or plasma membrane localization have been elucidated. In contrast to PLM, the plasma membrane localization of CHIF and RIC was not altered by mutation of potential cytoplasmic phosphorylation sites. Overall, these results suggest that phosphorylation of specific residues of PLM may direct PLM from an intracellular compartment to the plasma membrane.
机译：FXYD蛋白家族由几种小单跨膜蛋白组成，这些蛋白具有高度的同源性。该家族中最知名的成员包括Na（+）-K（+）-ATPase的γ-亚基和心脏肌膜的磷蛋白phosphorlemman（PLM）。该家族的其他成员包括皮质类固醇激素诱导因子（CHIF），8 kDa的乳腺肿瘤蛋白（Mat-8），并与离子通道（RIC）相关。 FXYD蛋白的确切生理作用仍然未知。为了更好地表征FXYD蛋白家族成员的功能，我们在Madin-Darby犬肾（MDCK）细胞中表达了该家族的几个成员。除PLM外，所有FXYD蛋白都主要存在于基底外侧质膜中。出乎意料的是，发现PLM是一种先前表征的质膜蛋白，与内质网标记蛋白二硫键异构酶共定位。用PKC激动剂处理表达PLM的MDCK细胞会导致某些PLM重新分布到质膜上。 PLM胞质结构域内残基的定点诱变表明，Ser69处的负电荷对于将PLM的定位转移到质膜是必需的。另外，已经阐明了PLM的内质网或质膜定位所必需的其他区域。与PLM相反，CHIF和RIC的质膜定位不会因潜在的细胞质磷酸化位点的突变而改变。总体而言，这些结果表明，PLM特定残基的磷酸化可能将PLM从细胞内区室引导至质膜。

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