NMR 1H, 13C, 15N backbone resonance assignments of 14-3-3ζ binding region of human FOXO3a (residues 1-284)

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2024-09-11 DOI:10.1007/s12104-024-10200-7
Shota Enomoto, Shoichi Nakatsuka, Tomoya Kuwayama, Kosaku Kawatsu, Mariko Yokogawa, Masanori Osawa
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Abstract

In tumors, mutation in Ras proteins stimulates a signaling cascade through phosphorylation. Downstream of the cascade, many transcription and translation factors are up- or down-regulated by phosphorylation, leading to cancer progression. This phosphorylation cascade is sustained by 14-3-3ζ protein. 14-3-3ζ binds to its client proteins that are Ser/Thr-phosphorylated and prevents their dephosphorylation. One of those transcription factors is FOXO3a, whose transcriptional activity is suppressed in the phosphorylation cascade. FOXO3a binds to specific DNA sequences and activates the transcription of apoptosis-related proteins. In cancer cells, however, FOXO3a is phosphorylated, bound to 14-3-3ζ, and dissociated from the DNA, resulting in FOXO3a inactivation. To elucidate the mechanism of FOXO3a inactivation by the 14-3-3ζ binding, we aim to perform NMR analysis of the interaction between 14-3-3ζ and di-phosphorylated FOXO3a residues 1-284 (dpFOXO3a). Here, we report the backbone resonance assignments of dpFOXO3a, which are transferred from those of the N-terminal domain (NTD) and the DNA-binding domain (DBD) of dpFOXO3a.

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人类 FOXO3a 的 14-3-3ζ 结合区(残基 1-284)的核磁共振 1H、13C 和 15N 骨架共振赋值
在肿瘤中,Ras 蛋白的突变会通过磷酸化刺激信号级联。在级联的下游,许多转录和翻译因子通过磷酸化被上调或下调,从而导致癌症进展。这种磷酸化级联由 14-3-3ζ 蛋白质维持。14-3-3ζ 蛋白会与 Ser/Thr 磷酸化的客户蛋白结合,阻止它们解除磷酸化。其中一个转录因子是 FOXO3a,它的转录活性在磷酸化级联过程中受到抑制。FOXO3a 与特定的 DNA 序列结合,激活凋亡相关蛋白的转录。然而,在癌细胞中,FOXO3a 被磷酸化,与 14-3-3ζ 结合,并与 DNA 分离,导致 FOXO3a 失活。为了阐明 14-3-3ζ 结合导致 FOXO3a 失活的机制,我们旨在对 14-3-3ζ 和二磷酸化 FOXO3a 残基 1-284 (dpFOXO3a)之间的相互作用进行核磁共振分析。在此,我们报告了 dpFOXO3a 的骨架共振分配,这些分配是从 dpFOXO3a 的 N 端结构域(NTD)和 DNA 结合结构域(DBD)的骨架共振分配转移而来的。
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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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