He Yanan, Chen Yihong, Mooney Steven M, Rajagopalan Krithika, Bhargava Ajay, Sacho Elizabeth, Weninger Keith, Bryan Philip N, Kulkarni Prakash, Orban John
From the W. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850, the Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742.
the Department of Urology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21287.
J Biol Chem. 2015 Oct 9;290(41):25090-102. doi: 10.1074/jbc.M115.658583. Epub 2015 Aug 4.
Prostate-associated gene 4 (PAGE4) is an intrinsically disordered cancer/testis antigen that is up-regulated in the fetal and diseased human prostate. Knocking down PAGE4 expression results in cell death, whereas its overexpression leads to a growth advantage of prostate cancer cells (Zeng, Y., He, Y., Yang, F., Mooney, S. M., Getzenberg, R. H., Orban, J., and Kulkarni, P. (2011) The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. J. Biol. Chem. 286, 13985-13994). Phosphorylation of PAGE4 at Thr-51 is critical for potentiating c-Jun transactivation, an important factor in controlling cell growth, apoptosis, and stress response. Using NMR spectroscopy, we show that the PAGE4 polypeptide chain has local and long-range conformational preferences that are perturbed by site-specific phosphorylation at Thr-51. The population of transient turn-like structures increases upon phosphorylation in an ∼20-residue acidic region centered on Thr-51. This central region therefore becomes more compact and more negatively charged, with increasing intramolecular contacts to basic sequence motifs near the N and C termini. Although flexibility is decreased in the central region of phospho-PAGE4, the polypeptide chain remains highly dynamic overall. PAGE4 utilizes a transient helical structure adjacent to the central acidic region to bind c-Jun with low affinity in vitro. The binding interaction is attenuated by phosphorylation at Thr-51, most likely because of masking the effects of the more compact phosphorylated state. Therefore, phosphorylation of PAGE4 leads to conformational shifts in the dynamic ensemble, with large functional consequences. The changes in the structural ensemble induced by posttranslational modifications are similar conceptually to the conformational switching events seen in some marginally stable ("metamorphic") folded proteins in response to mutation or environmental triggers.
前列腺相关基因4(PAGE4)是一种内在无序的癌胚抗原,在胎儿和患病的人类前列腺中上调。敲低PAGE4表达会导致细胞死亡,而其过表达则会导致前列腺癌细胞具有生长优势(曾毅、何宇、杨峰、穆尼、格岑伯格、奥尔班、库尔卡尼,2011年,癌胚抗原前列腺相关基因4(PAGE4)是一种高度内在无序的蛋白质,《生物化学杂志》,第286卷,第13985 - 13994页)。PAGE4在苏氨酸 - 51处的磷酸化对于增强c - Jun反式激活至关重要,c - Jun是控制细胞生长、凋亡和应激反应的重要因子。利用核磁共振光谱,我们表明PAGE4多肽链具有局部和远程构象偏好,这些偏好会因苏氨酸 - 51处的位点特异性磷酸化而受到干扰。在以苏氨酸 - 51为中心的约20个残基的酸性区域中,磷酸化后瞬态转角样结构的数量增加。因此,这个中心区域变得更加紧凑且带更多负电荷,与N和C末端附近的碱性序列基序的分子内接触增加。尽管磷酸化的PAGE4中心区域的灵活性降低,但多肽链整体上仍然高度动态。PAGE4利用与中心酸性区域相邻的瞬态螺旋结构在体外以低亲和力结合c - Jun。苏氨酸 - 51处的磷酸化会减弱这种结合相互作用,最有可能是因为掩盖了更紧凑的磷酸化状态的影响。因此,PAGE4的磷酸化导致动态集合中的构象转变,具有重大的功能后果。翻译后修饰引起的结构集合变化在概念上类似于一些边缘稳定(“变态”)折叠蛋白因突变或环境触发而发生的构象转换事件。