Pfeffer L M, Mullersman J E, Pfeffer S R, Murti A, Shi W, Yang C H
Department of Pathology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.
Science. 1997 May 30;276(5317):1418-20. doi: 10.1126/science.276.5317.1418.
STAT (signal transducers and activators of transcription) proteins undergo cytokine-dependent phosphorylation on serine and tyrosine. STAT3, a transcription factor for acute phase response genes, was found to act as an adapter molecule in signal transduction from the type I interferon receptor. STAT3 bound to a conserved sequence in the cytoplasmic tail of the IFNAR1 chain of the receptor and underwent interferon-dependent tyrosine phosphorylation. The p85 regulatory subunit of phosphatidylinositol 3-kinase, which activates a series of serine kinases, bound to phosphorylated STAT3 and subsequently underwent tyrosine phosphorylation. Thus, STAT3 acts as an adapter to couple another signaling pathway to the interferon receptor.
信号转导子和转录激活子(STAT)蛋白在丝氨酸和酪氨酸上进行细胞因子依赖性磷酸化。STAT3是急性期反应基因的转录因子,被发现可作为I型干扰素受体信号转导中的衔接分子。STAT3与受体IFNAR1链细胞质尾部的保守序列结合,并进行干扰素依赖性酪氨酸磷酸化。激活一系列丝氨酸激酶的磷脂酰肌醇3激酶的p85调节亚基与磷酸化的STAT3结合,随后进行酪氨酸磷酸化。因此,STAT3作为衔接分子,将另一条信号通路与干扰素受体偶联。