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. ORCID: https://orcid.org/0000-0003-3618-238X, 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. ORCID: https://orcid.org/0000-0002-3292-2064 and Robinson, Stephen D. ORCID: https://orcid.org/0000-0002-6606-7588 (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
Depositing User:	Pure Connector
Date Deposited:	10 May 2018 08:30
Last Modified:	30 Dec 2022 01:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/67002
DOI:	10.15252/embr.201744578

Actions (login required)

View Item