AI Article Synopsis
- - Lysyl-tRNA synthetase (KRS) enhances cancer cell migration by interacting with the laminin receptor (LR/RPSA).
- - NMR studies reveal that KRS’s anticodon-binding domain directly binds to the C-terminal of 37LRP, and specific inhibitors hinder this binding.
- - The KRS anticodon-binding domain also binds to laminin, providing important insights into how KRS and LR interact at the cell surface.
Article Abstract
Lysyl-tRNA synthetase (KRS) interacts with the laminin receptor (LR/RPSA) and enhances laminin-induced cell migration in cancer metastasis. In this nuclear magnetic resonance (NMR)-based study, we show that the anticodon-binding domain of KRS binds directly to the C-terminal region of 37LRP, and the previously found inhibitors BC-K-01 and BC-K-YH16899 interfere with KRS-37LRP binding. In addition, the anticodon-binding domain of KRS binds to laminin, observed by NMR and SPR. These results provide crucial insights into the structural characteristics of the KRS-LR interaction on the cell surface.
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| http://dx.doi.org/10.1016/j.febslet.2014.06.048 | DOI Listing |
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