6U4M

Solution structure of paxillin LIM4

6U4M の概要

• エントリーDOI: 10.2210/pdb6u4m/pdb
• NMR情報: BMRB: 30658
• 分子名称: Paxillin, ZINC ION (2 entities in total)
• 機能のキーワード: lim domain, zinc finger, cell adhesion
• 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: 8440.58

構造登録者

Zhu, L.,Qin, J. (登録日: 2019-08-26, 公開日: 2019-10-23, 最終更新日: 2024-05-15)

主引用文献

Zhu, L.,Liu, H.,Lu, F.,Yang, J.,Byzova, T.V.,Qin, J.
Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion.
Structure, 27:1686-, 2019

PubMed Abstract: Activation of cell surface receptor integrin has been extensively studied as the first key step to trigger cell adhesion, but the subsequent events, widely regarded as integrin "outside-in" signaling to form supramolecular complexes (focal adhesions [FAs]) to promote dynamic cell adhesion, remain poorly elucidated. Integrin activator kindlin-2 was recently found to associate with paxillin in nascent FAs, implicating an early yet undefined integrin outside-in signaling event. Here we show structurally that kindlin-2 recognizes paxillin via a distinct interface involving the ubiquitin-like kindlin-2 F0 domain and the paxillin LIM4 domain. The interface is adjacent to the membrane binding site of kindlin-2 F0, suggesting a mechanism for kindlin-2 to recruit paxillin to the membrane-proximal site where FA assembly is initiated. Disruption of the interface impaired the localization of paxillin, causing strong defects in FA assembly and cell migration. These data unveil a structural basis of the kindlin-2/paxillin interaction in controlling dynamic cell adhesion.

PubMed: 31590942
DOI: 10.1016/j.str.2019.09.006

実験手法

SOLUTION NMR