A direct interaction between fascin and microtubules contributes to adhesion dynamics and cell migration.

Abstract

Fascin is an actin-binding and bundling protein that is highly upregulated in most epithelial cancers. Fascin promotes cell migration and adhesion dynamics in vitro and tumour cell metastasis in vivo. However, potential non-actin bundling roles for fascin remain unknown. Here, we show for the first time that fascin can directly interact with the microtubule cytoskeleton and that this does not depend upon fascin-actin bundling. Microtubule binding contributes to fascin-dependent control of focal adhesion dynamics and cell migration speed. We also show that fascin forms a complex with focal adhesion kinase (FAK, also known as PTK2) and Src, and that this signalling pathway lies downstream of fascin-microtubule association in the control of adhesion stability. These findings shed light on new non actin-dependent roles for fascin and might have implications for the design of therapies to target fascin in metastatic disease.

• Authors: Giulia Villari, Asier Jayo, Jennifer Zanet, Briana Fitch, Bryan Serrels, Margaret Frame, Brian M Stramer, Benjamin T Goult, Maddy Parsons
• Journal: Journal of cell science (J Cell Sci) Vol. 128 Issue 24 Pg. 4601-14 (Dec 15 2015) ISSN: 1477-9137 [Electronic] England
• PMID: 26542021 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: © 2015. Published by The Company of Biologists Ltd.

Chemical References

• Carrier Proteins
• Microfilament Proteins
• fascin
• Focal Adhesion Kinase 1
• PTK2 protein, human

Topics

• Carrier Proteins (genetics, metabolism)
• Cell Adhesion (physiology)
• Cell Movement (physiology)
• Focal Adhesion Kinase 1 (genetics, metabolism)
• HeLa Cells
• Humans
• Microfilament Proteins (genetics, metabolism)
• Microtubules (genetics, metabolism)