8IW5

Crystal structure of liprin-beta H2H3 dimer

Summary for 8IW5

• Entry DOI: 10.2210/pdb8iw5/pdb
• Descriptor: Liprin-beta-1, CALCIUM ION (3 entities in total)
• Functional Keywords: focal adhesion, cortical microtubule stabilizing complex, protein binding
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 11471.07

Authors

Zhang, J.,Chen, S.,Wei, Z. (deposition date: 2023-03-29, release date: 2023-11-08, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)