Castigli E, Chatila T A, Geha R S
Children's Hospital, Department of Pediatrics, Harvard Medical School, Boston, MA 02115.
J Immunol. 1993 Apr 15;150(8 Pt 1):3284-90.
Nuclear factor of activated T cells (NF-AT) is a transcriptional activator involved in the induction of IL-2 gene expression. The response element for NF-AT is a sequence localized between -285/-254 in the IL-2 regulatory region. The composition of NF-AT protein is still not fully elucidated. We demonstrate that, in normal human T cells, an AP-1 protein is a component of the NF-AT protein complex. This was evidenced by the ability of the AP-1 site to compete with the NF-AT site for binding to NF-AT and by the capacity of immobilized anti-Jun and anti-Fos antibodies to deplete NF-AT-binding activity from nuclear extracts of activated T cells. There was no detectable binding of in vitro translated Jun/Fos heterodimer (AP-1) to the NF-AT sequence, and the NF-AT sequence was unable to inhibit the binding of Jun/Fos to the AP-1 sequence. The presence of an AP-1 protein in the NF-AT protein complex may regulate NF-AT-binding activity through protein-protein interaction.
活化T细胞核因子(NF-AT)是一种参与白细胞介素-2(IL-2)基因表达诱导的转录激活因子。NF-AT的反应元件是位于IL-2调控区-285/-254之间的一段序列。NF-AT蛋白的组成仍未完全阐明。我们证明,在正常人T细胞中,一种活化蛋白-1(AP-1)蛋白是NF-AT蛋白复合物的一个组成部分。这一点通过AP-1位点与NF-AT位点竞争结合NF-AT的能力以及固定化的抗Jun和抗Fos抗体从活化T细胞核提取物中耗尽NF-AT结合活性的能力得到了证明。体外翻译的Jun/Fos异二聚体(AP-1)与NF-AT序列没有可检测到的结合,并且NF-AT序列无法抑制Jun/Fos与AP-1序列的结合。NF-AT蛋白复合物中AP-1蛋白的存在可能通过蛋白质-蛋白质相互作用调节NF-AT结合活性。