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Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor.

Abstract：

:To our knowledge, no structural study to date has characterized, in an intact receptor, the coupling of conformational change in extracellular domains through a single-pass transmembrane domain to conformational change in cytoplasmic domains. Here we examine such coupling, and its unexpected complexity, using nearly full-length epidermal growth factor receptor (EGFR) and negative-stain EM. The liganded, dimeric EGFR ectodomain can couple both to putatively active, asymmetrically associated kinase dimers and to putatively inactive, symmetrically associated kinase dimers and monomers. Inhibitors that stabilize the active or inactive conformation of the kinase active site, as well as mutations in the kinase dimer interface and a juxtamembrane phosphorylation site, shift the equilibrium among the three kinase association states. This coupling of one conformation of an activated receptor ectodomain to multiple kinase-domain arrangements reveals previously unanticipated complexity in transmembrane signaling and facilitates regulation of receptor function in the juxtamembrane and cytoplasmic environments.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Mi LZ,Lu C,Li Z,Nishida N,Walz T,Springer TA

doi

10.1038/nsmb.2092

subject

Has Abstract

pub_date

2011-08-07 00:00:00

pages

984-9

issue

9

eissn

1545-9993

issn

1545-9985

pii

nsmb.2092

journal_volume

18

pub_type

杂志文章

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