The β3‐integrin endothelial adhesome regulates microtubule‐dependent cell migration

Atkinson, Samuel J., Gontarczyk, Aleksander M., Alghamdi, Abdullah A. A., Ellison, Tim S., Johnson, Robert T., Fowler, Wesley J., Kirkup, Benjamin M., Silva, Bernardo C., Harry, Bronwen E., Schneider, Jochen G., Weilbaecher, Katherine N., Mogensen, Mette M., Bass, Mark D., Parsons, Maddy, Edwards, Dylan R. and Robinson, Stephen D. (2018) The β3‐integrin endothelial adhesome regulates microtubule‐dependent cell migration. EMBO Reports, 19 (6). ISSN 1469-221X

Preview

PDF (Accepted manuscript) - Accepted Version Download (42MB) | Preview

Abstract

Integrin β3 is seen as a key anti-angiogenic target for cancer treatment due to its expression on neovasculature, but the role it plays in the process is complex; whether it is pro- or anti-angiogenic depends on the context in which it is expressed. To understand precisely β3’s role in regulating integrin adhesion complexes in endothelial cells, we characterised, by mass spectrometry, the β3-dependent adhesome. We show that depletion of β3-integrin in this cell type leads to changes in microtubule behaviour that control cell migration. β3-integrin regulates microtubule stability in endothelial cells through Rcc2/Anxa2 driven control of active Rac1 localisation. Our findings reveal that angiogenic processes, both in vitro and in vivo, are more sensitive to microtubule targeting agents when β3-integrin levels are reduced

Item Type:	Article
Uncontrolled Keywords:	adhesive,endothelial,integrins,microtubules,sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups:	Faculty of Science > Research Groups > Cells and Tissues Faculty of Medicine and Health Sciences > Research Groups > Cancer Studies
Depositing User:	Pure Connector
Date Deposited:	10 May 2018 08:30
Last Modified:	28 Mar 2025 08:41
URI:	https://ueaeprints.uea.ac.uk/id/eprint/67002
DOI:	10.15252/embr.201744578

Downloads

Actions (login required)

View Item