Abstract:
:Ligand-induced receptor dimerization has traditionally been viewed as the key event in transmembrane signalling by epidermal growth factor receptors (EGFRs). Here we show that the Caenorhabditis elegans EGFR orthologue LET-23 is constitutively dimeric, yet responds to its ligand LIN-3 without changing oligomerization state. SAXS and mutational analyses further reveal that the preformed dimer of the LET-23 extracellular region is mediated by its domain II dimerization arm and resembles other EGFR extracellular dimers seen in structural studies. Binding of LIN-3 induces only minor structural rearrangements in the LET-23 dimer to promote signalling. Our results therefore argue that EGFR can be regulated by allosteric changes within an existing receptor dimer--resembling signalling by insulin receptor family members, which share similar extracellular domain compositions but form covalent dimers.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Freed DM,Alvarado D,Lemmon MAdoi
10.1038/ncomms8380subject
Has Abstractpub_date
2015-06-10 00:00:00pages
7380issn
2041-1723pii
ncomms8380journal_volume
6pub_type
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