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Author Notes:

To whom correspondence should be addressed: 1365-C Clifton Rd., Rm. 4092-C, Atlanta, GA 30322. Tel.: 404-778-4597; Fax: 404-778-5530; E-mail: aimarcu@emory.edu.

We thank the Emory Integrated Cellular Imaging Core and the Emory University Custom Cloning Core Facility for their assistance.

We also thank Dr. Anthea Hammond for editorial assistance. GFP-labeled FAK plasmids were a kind gift from Gregg Gundersen (Columbia University).


Research Funding:

This work was supported, in whole or in part, by National Institutes of Health Grants 1R01CA142858 (to A. I. M.) and PO1 Supplement 3PO1CA116676-05S2 (to A. I. M. and W. Z.), American Cancer Society Research Scholar Grant RSG-08-035-01-CSM (to A. I. M.), and American Cancer Society Postdoctoral Training Grant PF-11-125-01-CSM (to E. R. K.).


  • Cell Migration
  • Cell Motility
  • Epithelial Mesenchymal Transition
  • Focal Adhesion Kinase
  • Imaging
  • LKB1
  • Adhesion

LKB1 Represses Focal Adhesion Kinase (FAK) Signaling via a FAK-LKB1 Complex to Regulate FAK Site Maturation and Directional Persistence


Journal Title:

Journal of Biological Chemistry


Volume 288, Number 24


, Pages 17663-17674

Type of Work:

Article | Final Publisher PDF


Background: LKB1 is a serine/threonine kinase important for cell polarity and motility. Results: LKB1 loss causes focal adhesion kinase hyperactivation and aberrant cell motility. Conclusion: LKB1 represses focal adhesion kinase to regulate its turnover. Significance: This provides information on how LKB1 regulates the cell adhesion pathway during cell motility.

Copyright information:

© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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