5J19

phospho-Pon binding-induced Plk1 dimerization

5J19 の概要

• エントリーDOI: 10.2210/pdb5j19/pdb
• 分子名称: Serine/threonine-protein kinase PLK1, Phosphorylated peptide from Partner of Numb, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: polo-box domain, cell cycle
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: P53350
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57535.17

構造登録者

Zhu, K.,Shan, Z.,Zhang, L.,Wen, W. (登録日: 2016-03-29, 公開日: 2016-06-15, 最終更新日: 2024-10-09)

主引用文献

Zhu, K.,Shan, Z.,Zhang, L.,Wen, W.
Phospho-Pon Binding-Mediated Fine-Tuning of Plk1 Activity
Structure, 24:1110-1119, 2016

PubMed Abstract: In Drosophila neuroblasts (NBs), the asymmetrical localization and segregation of the cell-fate determinant Numb are regulated by its adaptor Partner of Numb (Pon) and the cell-cycle kinase Polo. Polo phosphorylates the Pon localization domain, thus leading to its basal distribution together with Numb, albeit through an unclear mechanism. Here, we find that Cdk1 phosphorylates Pon at Thr63, thus creating a docking site for the Polo-box domain (PBD) of Polo-like kinase 1 (Plk1). The crystal structure of the Plk1 PBD/phospho-Pon complex reveals that two phospho-Pon bound PBDs associate to form a dimer of dimers. We provide evidence that phospho-Pon binding-induced PBD dimerization relieves the autoinhibition of Plk1. Moreover, we demonstrate that the priming Cdk1 phosphorylation of Pon is important for sequential Plk1 phosphorylation. Our results not only provide structural insight into how phosphoprotein binding activates Plk1 but also suggest that binding to different phosphoproteins might mediate the fine-tuning of Plk1 activity.

PubMed: 27238966
DOI: 10.1016/j.str.2016.04.012

実験手法

X-RAY DIFFRACTION (2 Å)