8IVZ

Crystal structure of talin R7 in complex with KANK1 KN motif

8IVZ の概要

• エントリーDOI: 10.2210/pdb8ivz/pdb
• 分子名称: Talin-1, KN motif and ankyrin repeat domains 1 (3 entities in total)
• 機能のキーワード: focal adhesion, protein binding
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 42465.86

構造登録者

Xu, Y.,Li, K.,Wei, Z.,Cong, Y. (登録日: 2023-03-29, 公開日: 2023-11-08, 最終更新日: 2026-03-11)

主引用文献

Guo, K.,Zhang, J.,Huang, P.,Xu, Y.,Pan, W.,Li, K.,Chen, L.,Luo, L.,Yu, W.,Chen, S.,He, S.,Wei, Z.,Yu, C.
KANK1 shapes focal adhesions by orchestrating protein binding, mechanical force sensing, and phase separation.
Cell Rep, 42:113321-113321, 2023

PubMed Abstract: Focal adhesions (FAs) are dynamic protein assemblies that connect cytoskeletons to the extracellular matrix and are crucial for cell adhesion and migration. KANKs are scaffold proteins that encircle FAs and act as key regulators of FA dynamics, but the molecular mechanism underlying their specified localization and functions remains poorly understood. Here, we determine the KANK1 structures in complex with talin and liprin-β, respectively. These structures, combined with our biochemical and cellular analyses, demonstrate how KANK1 scaffolds the FA core and associated proteins to modulate the FA shape in response to mechanical force. Additionally, we find that KANK1 undergoes liquid-liquid phase separation (LLPS), which is important for its localization at the FA edge and cytoskeleton connections to FAs. Our findings not only indicate the molecular basis of KANKs in bridging the core and periphery of FAs but also provide insights into the LLPS-mediated dynamic regulation of FA morphology.

PubMed: 37874676
DOI: 10.1016/j.celrep.2023.113321

実験手法

X-RAY DIFFRACTION (2.8 Å)