Abstract:
:Fluorescence resonance energy transfer (FRET) was used to reveal aspects of the mechanism of signal transduction by epidermal growth factor receptors (EGFR). The superpositions of epidermal growth factor (EGF), transforming growth factor-alpha (TGFalpha) and an antibody fragment (29.1) to the carbohydrate extremity of the receptor's ectodomain as measured by FRET, show that 14% of EGFRs in A431 cells are oligomerized before growth factor binding. After binding growth factor and signaling, these oligomers dissociate before releasing growth factor. Time courses of the FRET-derived distances between constitutively oligomerized EGFRs during signal transduction show a transient structural change in the extracellular domain, which occurs simultaneously with the production of intracellular Ca2+ signals. The FRET measurements also show a slow increase in oligomerization of EGFR monomers after growth factor binding. The structural change found in the extracellular domain of oligomeric EGFRs is similar to that shown by others for EPO, Neu, Fas, and tumor necrosis factor receptors, and may therefore be a common property of the transduction of the receptor-mediated signals.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Martin-Fernandez M,Clarke DT,Tobin MJ,Jones SV,Jones GRdoi
10.1016/S0006-3495(02)75585-9subject
Has Abstractpub_date
2002-05-01 00:00:00pages
2415-27issue
5eissn
0006-3495issn
1542-0086pii
S0006-3495(02)75585-9journal_volume
82pub_type
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