7D2S

Crystal structure of Rsu1/PINCH1_LIM5C complex

Summary for 7D2S

• Entry DOI: 10.2210/pdb7d2s/pdb
• Descriptor: Ras suppressor protein 1, LIM and senescent cell antigen-like-containing domain protein 1, GLYCEROL, ... (5 entities in total)
• Functional Keywords: leucine rich repeat, protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 34163.29

Authors

Yang, H.,Wei, Z.,Cong, Y. (deposition date: 2020-09-17, release date: 2021-02-24, Last modification date: 2023-11-29)

Primary citation

Yang, H.,Lin, L.,Sun, K.,Zhang, T.,Chen, W.,Li, L.,Xie, Y.,Wu, C.,Wei, Z.,Yu, C.
Complex structures of Rsu1 and PINCH1 reveal a regulatory mechanism of the ILK/PINCH/Parvin complex for F-actin dynamics.
Elife, 10:-, 2021

PubMed Abstract: Communications between actin filaments and integrin-mediated focal adhesion (FA) are crucial for cell adhesion and migration. As a core platform to organize FA proteins, the tripartite ILK/PINCH/Parvin (IPP) complex interacts with actin filaments to regulate the cytoskeleton-FA crosstalk. Rsu1, a Ras suppressor, is enriched in FA through PINCH1 and plays important roles in regulating F-actin structures. Here, we solved crystal structures of the Rsu1/PINCH1 complex, in which the leucine-rich-repeats of Rsu1 form a solenoid structure to tightly associate with the C-terminal region of PINCH1. Further structural analysis uncovered that the interaction between Rsu1 and PINCH1 blocks the IPP-mediated F-actin bundling by disrupting the binding of PINCH1 to actin. Consistently, overexpressing Rsu1 in HeLa cells impairs stress fiber formation and cell spreading. Together, our findings demonstrated that Rsu1 is critical for tuning the communication between F-actin and FA by interacting with the IPP complex and negatively modulating the F-actin bundling.

PubMed: 33587032
DOI: 10.7554/eLife.64395

Experimental method

X-RAY DIFFRACTION (1.653 Å)