Nature Communications (Oct 2016)
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
- Sarah R. Needham,
- Selene K. Roberts,
- Anton Arkhipov,
- Venkatesh P. Mysore,
- Christopher J. Tynan,
- Laura C. Zanetti-Domingues,
- Eric T. Kim,
- Valeria Losasso,
- Dimitrios Korovesis,
- Michael Hirsch,
- Daniel J. Rolfe,
- David T. Clarke,
- Martyn D. Winn,
- Alireza Lajevardipour,
- Andrew H. A. Clayton,
- Linda J. Pike,
- Michela Perani,
- Peter J. Parker,
- Yibing Shan,
- David E. Shaw,
- Marisa L. Martin-Fernandez
Affiliations
- Sarah R. Needham
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Selene K. Roberts
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Anton Arkhipov
- D.E. Shaw Research
- Venkatesh P. Mysore
- D.E. Shaw Research
- Christopher J. Tynan
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Laura C. Zanetti-Domingues
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Eric T. Kim
- D.E. Shaw Research
- Valeria Losasso
- Computational Science and Engineering Department, Science and Technology Facilities Council, Daresbury Laboratory
- Dimitrios Korovesis
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Michael Hirsch
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Daniel J. Rolfe
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- David T. Clarke
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- Martyn D. Winn
- Computational Science and Engineering Department, Science and Technology Facilities Council, Daresbury Laboratory
- Alireza Lajevardipour
- Centre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of Technology
- Andrew H. A. Clayton
- Centre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of Technology
- Linda J. Pike
- Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine
- Michela Perani
- Division of Cancer Studies, King’s College London, Guy’s Medical School Campus
- Peter J. Parker
- Division of Cancer Studies, King’s College London, Guy’s Medical School Campus
- Yibing Shan
- D.E. Shaw Research
- David E. Shaw
- D.E. Shaw Research
- Marisa L. Martin-Fernandez
- Central Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford
- DOI
- https://doi.org/10.1038/ncomms13307
- Journal volume & issue
-
Vol. 7,
no. 1
pp. 1 – 14
Abstract
Epidermal growth factor receptors have been shown to oligomerise upon binding to their cognate ligands. Here, the authors use biochemical, biophysical and cell biology techniques to analyse the structures of these oligomers, and argue that these formations are required for signalling.
