6MIF

Lim5 domain of PINCH1 protein

6MIF の概要

• エントリーDOI: 10.2210/pdb6mif/pdb
• NMR情報: BMRB: 30518
• 分子名称: LIM and senescent cell antigen-like-containing domain protein 1, ZINC ION (2 entities in total)
• 機能のキーワード: lim domain, zn binding, signaling protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9125.57

構造登録者

Qin, J.,Vaynberg, J. (登録日: 2018-09-19, 公開日: 2018-10-31, 最終更新日: 2024-05-15)

主引用文献

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

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: 30367047
DOI: 10.1038/s41467-018-06906-7

実験手法

SOLUTION NMR