6AKL

Crystal structure of Striatin3 in complex with SIKE1 Coiled-coil domain

6AKL の概要

• エントリーDOI: 10.2210/pdb6akl/pdb
• 分子名称: Suppressor of IKBKE 1, Striatin-3 (3 entities in total)
• 機能のキーワード: coiled-coil domain, heterotrimer, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 16034.38

構造登録者

Zhou, L.,Chen, M.,Zhou, Z.C. (登録日: 2018-09-02, 公開日: 2019-01-16, 最終更新日: 2023-11-22)

主引用文献

Tang, Y.,Chen, M.,Zhou, L.,Ma, J.,Li, Y.,Zhang, H.,Shi, Z.,Xu, Q.,Zhang, X.,Gao, Z.,Zhao, Y.,Cheng, Y.,Jiao, S.,Zhou, Z.
Architecture, substructures, and dynamic assembly of STRIPAK complexes in Hippo signaling.
Cell Discov, 5:3-3, 2019

PubMed Abstract: Striatin-interacting phosphatases and kinases (STRIPAKs) are evolutionarily conserved supramolecular complexes, which have been implicated in the Hippo signaling pathway. Yet the topological structure and dynamic assembly of STRIPAK complexes remain elusive. Here, we report the overall architecture and substructures of a Hippo kinase-containing STRIPAK complex. PP2Aa/c-bound STRN3 directly contacts the Hippo kinase MST2 and also controls the loading of MST2 via two "arms" in a phosphorylation-dependent manner, one arm being STRIP1 and the other SIKE1-SLMAP. A decreased cell density triggered the dissociation of the STRIP1 arm from STRIPAK, reflecting the dynamic assembly of the complex upon sensing upstream signals. Crystallographic studies defined at atomic resolution the interface between STRN3 and SIKE1, and that between SIKE1 and SLMAP. Disrupting the complex assembly abrogated the regulatory effect of STRIPAK towards Hippo signaling. Collectively, our study revealed a "two-arm" assembly of STRIPAK with context-dependent dynamics, offering a framework for further studies on Hippo signaling and biological processes involving MST kinases.

PubMed: 30622739
DOI: 10.1038/s41421-018-0077-3

実験手法

X-RAY DIFFRACTION (1.75 Å)