8IVZ
Crystal structure of talin R7 in complex with KANK1 KN motif
Summary for 8IVZ
| Entry DOI | 10.2210/pdb8ivz/pdb |
| Descriptor | Talin-1, KN motif and ankyrin repeat domains 1 (3 entities in total) |
| Functional Keywords | focal adhesion, protein binding |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 42465.86 |
| Authors | |
| 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 Cited by 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: 37874676DOI: 10.1016/j.celrep.2023.113321 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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