Author
Listed:
- Adam Byron
(Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Present address: Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XR, UK)
- 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
Present address: Turku Centre for Biotechnology, University of Turku, Turku 20520, Finland)
- 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
Wyss Institute for Biologically Inspired Engineering, Harvard University)
- Matthew J. Stroud
(Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester
Present address: School of Medicine, University of California, San Diego, La Jolla, California 92093-0613C, USA)
- Christopher S. Chen
(Boston University
Wyss Institute for Biologically Inspired Engineering, Harvard 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)
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.
Suggested Citation
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 & Martin J. Humphrie, 2015.
"A proteomic approach reveals integrin activation state-dependent control of microtubule cortical targeting,"
Nature Communications, Nature, vol. 6(1), pages 1-14, May.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7135
DOI: 10.1038/ncomms7135
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