Journal
CHEMISTRY & BIOLOGY
Volume 22, Issue 6, Pages 776-784Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2015.05.008
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Funding
- N.I.H. [GM 83257, F32 GM087092]
- NIH Training Grant in Biophysics [5T32GM008283-28]
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Binding of transforming growth factor a (TGF-alpha) to the epidermal growth factor receptor (EGFR) extracellular domain is encoded through the formation of a unique antiparallel coiled coil within the juxtamembrane segment. This new coiled coil is an insideout'' version of the coiled coil formed in the presence of epidermal growth factor (EGF). A third, intermediary coiled-coil interface is formed in the juxtamembrane region when EGFR is stimulated with betacellulin. The seven growth factors that activate EGFR in mammalian systems (EGF, TGF-alpha, epigen, epiregulin, betacellulin, heparin-binding EGF, and amphiregulin) fall into distinct categories in which the structure of the coiled coil induced within the juxtamembrane region correlates with cell state. The observation that coiled-coil state tracks with the downstream signaling profiles for each ligand provides evidence for growth factor functional selectivity by EGFR. Encoding growth factor identity in alternative coiled-coil rotamers provides a simple and elegant method for communicating chemical information across the plasma membrane.
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