6MIF
Lim5 domain of PINCH1 protein
Summary for 6MIF
| Entry DOI | 10.2210/pdb6mif/pdb |
| NMR Information | BMRB: 30518 |
| Descriptor | LIM and senescent cell antigen-like-containing domain protein 1, ZINC ION (2 entities in total) |
| Functional Keywords | lim domain, zn binding, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 9125.57 |
| Authors | Qin, J.,Vaynberg, J. (deposition date: 2018-09-19, release date: 2018-10-31, Last modification date: 2024-05-15) |
| Primary citation | Vaynberg, J.,Fukuda, K.,Lu, F.,Bialkowska, K.,Chen, Y.,Plow, E.F.,Qin, J. Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion. Nat Commun, 9:4465-4465, 2018 Cited by PubMed Abstract: Dynamic communication between integrin-containing complexes (focal adhesions, FAs) and actin filaments is critical for regulating cell adhesion. Pseudokinase ILK plays a key role in this process but the underlying mechanism remains highly elusive. Here we show that by recruiting FA adaptors PINCH and Parvin into a heterotrimeric complex (IPP), ILK triggers F-actin filament bundling - a process known to generate force/mechanical signal to promote cytoskeleton reassembly and dynamic cell adhesion. Structural, biochemical, and functional analyses revealed that the F-actin bundling is orchestrated by two previously unrecognized WASP-Homology-2 actin binding motifs within IPP, one from PINCH and the other from Parvin. Strikingly, this process is also sensitized to Mg-ATP bound to the pseudoactive site of ILK and its dysregulation severely impairs stress fibers formation, cell spreading, and migration. These data identify a crucial mechanism for ILK, highlighting its uniqueness as a pseudokinase to transduce non-catalytic signal and regulate cell adhesion. PubMed: 30367047DOI: 10.1038/s41467-018-06906-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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