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나노의학 연구단
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Phosphorylated EGFR Dimers Are Not Sufficient to Activate Ras

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Title
Phosphorylated EGFR Dimers Are Not Sufficient to Activate Ras
Author(s)
Samantha I. Liang; Bettina van Lengerich; Kelsie Eichel; Minkwon Cha; David M. Patterson; Tae-Young Yoon; Mark von Zastrow; Natalia Jura; Zev J. Gartner
Publication Date
2018-03
Journal
Cell Reports, v.22, no.10, pp.2593 - 2600
Publisher
Cell Press
Abstract
Growth factor binding to EGFR drives conformational changes that promote homodimerization and transphosphorylation, followed by adaptor recruitment, oligomerization, and signaling through Ras. Whether specific receptor conformations and oligomerization states are necessary for efficient activation of Ras is unclear. We therefore evaluated the sufficiency of a phosphorylated EGFR dimer to activate Ras without growth factor by developing a chemical-genetic strategy to crosslink and "trap'' full-length EGFR homodimers on cells. Trapped dimers become phosphorylated and recruit adaptor proteins at stoichiometry equivalent to that of EGF-stimulated receptors. Surprisingly, these phosphorylated dimers do not activate Ras, Erk, or Akt. In the absence of EGF, phosphorylated dimers do not further oligomerize or reorganize on cell membranes. These results suggest that a phosphorylated EGFR dimer loaded with core signaling adapters is not sufficient to activate Ras and that EGFR ligands contribute to conformational changes or receptor dynamics necessary for oligomerization and efficient signal propagation through the SOS-Ras-MAPK pathway (c) 2018 The Authors.
URI
https://pr.ibs.re.kr/handle/8788114/4634
ISSN
2211-1247
Appears in Collections:
Center for Nanomedicine (나노의학 연구단) > Journal Papers
Files in This Item:
28.Cell Reports 22, 2593-2600, (2018).pdfDownload

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