Altering FAK-paxillin interactions reduces adhesion, migration and invasion processes.
Focal adhesion kinase (FAK) plays an important role in signal transduction pathways initiated at sites of integrin-mediated cell adhesion to the extracellular matrix. Thus, FAK is involved in many aspects of the metastatic process including adhesion, migration and invasion. Recently, several small m...
Main Authors: | Thérèse B Deramaudt, Denis Dujardin, Fanny Noulet, Sophie Martin, Romain Vauchelles, Ken Takeda, Philippe Rondé |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3958421?pdf=render |
Similar Items
-
Inhibiting FAK–Paxillin Interaction Reduces Migration and Invadopodia-Mediated Matrix Degradation in Metastatic Melanoma Cells
by: Antoine Mousson, et al.
Published: (2021-04-01) -
Hyperphosphorylated FAK Delocalizes from Focal Adhesions to Membrane Ruffles
by: Abdelkader Hamadi, et al.
Published: (2010-01-01) -
Nudel and FAK as antagonizing strength modulators of nascent adhesions through paxillin.
by: Yongli Shan, et al.
Published: (2009-05-01) -
Paxillin and Focal Adhesion Kinase (FAK) Regulate Cardiac Contractility in the Zebrafish Heart.
by: Sofia Hirth, et al.
Published: (2016-01-01) -
Ganoderiol A-enriched extract suppresses migration and adhesion of MDA-MB-231 cells by inhibiting FAK-SRC-paxillin cascade pathway.
by: Guo-Sheng Wu, et al.
Published: (2013-01-01)