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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >NFAT5, a constitutively nuclear NFAT protein that does not cooperate with Fos and Jun
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NFAT5, a constitutively nuclear NFAT protein that does not cooperate with Fos and Jun

机译：NFAT5，一种本构核NFAT蛋白，不与Fos和Jun合作

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摘要

NFAT transcription factors are related to NF-#kappa#B/Rel proteins and form cooperative complexes with Fos and Jun on DNA. We have identified an NFAT-related protein, NFAT5, which differs from the conventional NFAT proteins NFAT1-4 in its structure, DNA binding, and regulation. NFAT5 contains a NFAT-like Rel homology domain, con- serves the DNA contact residues of NFAT1-4, and binds DNA sequences similar to those found in the regulatory regions of well-characterized NFAT-dependent genes. However, it lacks the majority of Fos/Jun contact residues and does not bind cooperatively with Fos and Jun to DNA. Unlike NFAT1-4, whose nuclear import is tightly regulated by calcineurin- mediated dephosphorylation, NFAT5 is a constitutively nu- clear phosphoprotein regardless of calcineurin activation. These features suggest that unlike the conventional NFAT proteins, NFAT1-4, which activate gene transcription by integrating inputs from calcium/calcineurin and protein ki- nase C/mitogen-activated protein kinase signaling pathways, NFAT5 participates in as-yet-unidentified signaling pathways in diverse immune and nonimmune cells.
机译：NFAT转录因子与NF-κB/ Rel蛋白有关，并与DNA上的Fos和Jun形成合作复合体。我们已经鉴定出一种NFAT相关蛋白NFAT5，它在结构，DNA结合和调控方面与常规NFAT蛋白NFAT1-4不同。 NFAT5包含一个类似NFAT的Rel同源结构域，保留NFAT1-4的DNA接触残基，并结合与在特征明确的NFAT依赖基因的调控区中发现的序列相似的DNA序列。但是，它缺少大多数Fos / Jun接触残基，并且不能与Fos和Jun协同结合到DNA。与NFAT1-4的核输入受钙调神经磷酸酶介导的去磷酸化作用严格调节不同，NFAT5是一种组成型核磷蛋白，而与钙调神经磷酸酶的激活无关。这些特征表明，与传统的NFAT蛋白NFAT1-4不同，后者通过整合钙/钙调神经磷酸酶和蛋白激酶C /促分裂原激活的蛋白激酶信号通路的输入来激活基因转录，而NFAT5参与了迄今尚未确定的信号通路。在各种免疫和非免疫细胞中

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