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Calcineurin-NFATc signaling pathway regulates AQP2 expression in response to calcium signals and osmotic stress 总被引:3,自引:0,他引:3
Li SZ McDill BW Kovach PA Ding L Go WY Ho SN Chen F 《American journal of physiology. Cell physiology》2007,292(5):C1606-C1616
The aquaporin (AQP)2 channel mediates the reabsorption of water in renal collecting ducts in response to arginine vasopressin (AVP) and hypertonicity. Here we show that AQP2 expression is induced not only by the tonicity-responsive enhancer binding protein (TonEBP)/nuclear factor of activated T cells (NFAT)5-mediated hypertonic stress response but also by the calcium-dependent calcineurin-NFATc pathway. The induction of AQP2 expression by the calcineurin-NFATc pathway can occur in the absence of TonEBP/NFAT5. Mutational and chromatin immunoprecipitation analyses revealed the existence of functional NFAT binding sites within the proximal AQP2 promoter responsible for regulation of AQP2 by NFATc proteins and TonEBP/NFAT5. Contrary to the notion that TonEBP/NFAT5 is the only Rel/NFAT family member regulated by tonicity, we found that hypertonicity promotes the nuclear translocation of NFATc proteins for the subsequent induction of AQP2 expression. Calcineurin activity was also found to be involved in the induction of TonEBP/NFAT5 expression by hypertonicity, thus further defining the signaling mechanisms that underlie the TonEBP/NFAT5 osmotic stress response pathway. The coordinate regulation of AQP2 expression by both osmotic stress and calcium signaling appears to provide a means to integrate diverse extracellular signals into optimal cellular responses. aquaporin; nuclear factor of activated T cells; tonicity-responsive enhancer binding protein; osmotic response 相似文献
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Irarrazabal CE Williams CK Ely MA Birrer MJ Garcia-Perez A Burg MB Ferraris JD 《The Journal of biological chemistry》2008,283(5):2554-2563
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在胰岛细胞株 H I T 细胞中,用瞬时转染法观察高 K+ 导致的膜去极化与c A M P对 C B P C端片段转录活性的影响.发现二者均可诱导 C B P C端片段的转录活性增强,并有协同效应; C B P C端片段的突变体( Ser 1 772 突变为 Ala)表现相同的诱导特性,但其基本转录活性降低.说明膜去极化和 c A M P对 C B P C 端片段转录活性的诱导作用与 P K A 磷酸化位点 Ser 1 772 无关,而该位点的磷酸化对调节 C B P C 端片段的基本转录活性起重要作用.蛋白激酶 C 通路对 C B P Ti的转录活性无影响. 相似文献