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

• Type of Material: Article
• Authors: Erik R. Kline, Emory University; John Shupe, Emory University; Melissa Gilbert-Ross, Emory University; Wei Zhou, Emory University; Adam I Marcus, Emory University
• Language: English
• Date: 2013-06-14
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
• Final Published Version (URL): http://www.jbc.org/content/288/24/17663
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 288
• Issue: 24
• Start Page: 17663
• End Page: 17674
• Grant/Funding Information: 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.).
• Keywords: Imaging; Cell Motility; Adhesion; Epithelial Mesenchymal Transition; Cell Migration; Focal Adhesion Kinase; LKB1
• Research Categories: Health Sciences, Oncology

Abstract

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.