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首页> 外文期刊>Biochemistry >Simultaneous phosphorylation of Ser11 and Ser18 in the alpha-subunit promotes the recruitment of Na(+),K(+)-ATPase molecules to the plasma membrane.
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Simultaneous phosphorylation of Ser11 and Ser18 in the alpha-subunit promotes the recruitment of Na(+),K(+)-ATPase molecules to the plasma membrane.

机译：Ser11和Ser18在alpha亚基中的同时磷酸化促进了Na（+），K（+）-ATPase分子向质膜的募集。

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摘要

Renal sodium homeostasis is a major determinant of blood pressure and is regulated by several natriuretic and antinatriuretic hormones. These hormones, acting through intracellular second messengers, either activate or inhibit proximal tubule Na(+),K(+)-ATPase. We have shown previously that phorbol ester (PMA) stimulation of endogenous PKC leads to activation of Na(+),K(+)-ATPase in cultured proximal tubule cells (OK cells) expressing the rodent Na(+), K(+)-ATPase alpha-subunit. We have now demonstrated that the treatment with PMA leads to an increased amount of Na(+),K(+)-ATPase molecules in the plasmalemma, which is proportional to the increased enzyme activity. Colchicine, dinitrophenol, and potassium cyanide prevented the PMA-dependent stimulation of activity without affecting the increased level of phosphorylation of the Na(+), K(+)-ATPase alpha-subunit. This suggests that phosphorylation does not directly stimulate Na(+),K(+)-ATPase activity; instead, phosphorylation may be the triggering mechanism for recruitment of Na(+),K(+)-ATPase molecules to the plasma membrane. Transfected cells expressing either an S11A or S18A mutant had the same basal Na(+),K(+)-ATPase activity as cells expressing the wild-type rodent alpha-subunit, but PMA stimulation of Na(+),K(+)-ATPase activity was completely abolished in either mutant. PMA treatment led to phosphorylation of the alpha-subunit by stimulation of PKC-beta, and the extent of this phosphorylation was greatly reduced in the S11A and S18A mutants. These results indicate that both Ser11 and Ser18 of the alpha-subunit are essential for PMA stimulation of Na(+), K(+)-ATPase activity, and that these amino acids are phosphorylated during this process. The results presented here support the hypothesis that PMA regulation of Na(+),K(+)-ATPase is the result of an increased number of Na(+),K(+)-ATPase molecules in the plasma membrane.
机译：肾钠稳态是血压的主要决定因素，并由几种利钠和利尿激素调节。这些激素，通过细胞内的第二信使，激活或抑制近端肾小管Na（+），K（+）-ATPase。我们以前已经表明，内源性PKC的佛波酯（PMA）刺激导致表达啮齿动物Na（+），K（+）的培养近端肾小管细胞（OK细胞）中的Na（+），K（+）-ATPase活化。 -ATP酶α-亚基。现在我们已经证明，用PMA处理会导致血浆中的Na（+），K（+）-ATPase分子数量增加，这与增加的酶活性成正比。秋水仙碱，二硝基苯酚和氰化钾防止PMA依赖活动的刺激，而不会影响Na（+），K（+）-ATPaseα-亚基磷酸化水平的提高。这表明磷酸化不会直接刺激Na（+），K（+）-ATPase活性;相反，磷酸化可能是Na（+），K（+）-ATPase分子募集到质膜的触发机制。表达S11A或S18A突变体的转染细胞与表达野生型啮齿动物α-亚基的细胞具有相同的基础Na（+），K（+）-ATPase活性，但PMA刺激Na（+），K（+）在任一突变体中，-ATP酶活性均被完全消除。 PMA处理通过刺激PKC-β导致α亚基磷酸化，并且在S11A和S18A突变体中，这种磷酸化的程度大大降低。这些结果表明，α11亚基的Ser11和Ser18对于PMA刺激Na（+），K（+）-ATPase活性都是必不可少的，并且这些氨基酸在此过程中被磷酸化。此处提出的结果支持以下假设，即PMA对Na（+），K（+）-ATPase的调节是质膜中Na（+），K（+）-ATPase分子数量增加的结果。

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