Journal
Nature Communications
Publication Date
2016
Volume
7
Inclusive Pages
13307
Document Type
Open Access Publication
DOI
10.1038/ncomms13307
Rights and Permissions
L.J. Pike, et al. 31 October 2016. EGFR oligomerization organizes kinase-active dimers into competent signalling platforms. Nature communications. Art. No. 13307. DOI: 10.1038/ncomms13307. http://www.nature.com/articles/ncomms13307
Recommended Citation
Pike, Linda J. and et al, "EGFR oligomerization organizes kinase-active dimers into competent signalling platforms." Nature Communications. 7, 13307. (2016).
https://digitalcommons.wustl.edu/open_access_pubs/5391
Supplementary Figures 1-14, Supplementary Methods and Supplementary References.
ncomms13307-s2.mov (11938 kB)
Single particle tracking of EGFR on live CHO cells at 37°C. CHO cells stably expressing 105 wild type EGFR/cell were treated with a 4 nM CF640R fluorophore-conjugated Affibody solution at 37°C and tracked as previously described7. The multiple steps during photobleaching shown by individual spots indicate that receptors form high order oligomers prior to the EGF stimulus.
ncomms13307-s3.mov (7303 kB)
Single particle tracking of EGFR on live CHO cells at 37°C. CHO cells stably expressing 105 wild type EGFR/cell were treated with a 4 nM CF640R fluorophore-conjugated EGF solution at 37°C, and tracked as previously described7. The multiple steps photobleaching shown by individual spots indicate that receptors also move in clusters larger than dimers after the EGF stimulus.
ncomms13307-s4.txt (10233 kB)