A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting

Adam Byron, Janet A. Askari, Jonathan D. Humphries, Guillaume Jacquemet, Ewa J. Koper, Stacey Warwood, Colin K. Choi, Matthew J. Stroud, Christopher S. Chen, David Knight and Martin J. Humphries ()
Additional contact information
Adam Byron: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Janet A. Askari: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Jonathan D. Humphries: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Guillaume Jacquemet: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Ewa J. Koper: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Stacey Warwood: Biological Mass Spectrometry Core Facility, Faculty of Life Sciences, University of Manchester
Colin K. Choi: Boston University
Matthew J. Stroud: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Christopher S. Chen: Boston University
David Knight: Biological Mass Spectrometry Core Facility, Faculty of Life Sciences, University of Manchester
Martin J. Humphries: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester

Nature Communications, 2015, vol. 6, issue 1, 1-14

Abstract: Abstract Integrin activation, which is regulated by allosteric changes in receptor conformation, enables cellular responses to the chemical, mechanical and topological features of the extracellular microenvironment. A global view of how activation state converts the molecular composition of the region proximal to integrins into functional readouts is, however, lacking. Here, using conformation-specific monoclonal antibodies, we report the isolation of integrin activation state-dependent complexes and their characterization by mass spectrometry. Quantitative comparisons, integrating network, clustering, pathway and image analyses, define multiple functional protein modules enriched in a conformation-specific manner. Notably, active integrin complexes are specifically enriched for proteins associated with microtubule-based functions. Visualization of microtubules on micropatterned surfaces and live cell imaging demonstrate that active integrins establish an environment that stabilizes microtubules at the cell periphery. These data provide a resource for the interrogation of the global molecular connections that link integrin activation to adhesion signalling.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms7135 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7135

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms7135

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().