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Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding.

Abstract：

:Epidermal growth factor (EGF) receptor monomers and noncovalently associated dimers were isolated by sucrose density gradient centrifugation, and their respective binding and autophosphorylation activities were determined. We find that monomers are low-affinity receptors and dimers are high-affinity receptors. In the absence of EGF, dimers exhibit a 4-fold higher autophosphorylation activity than do monomers. Addition of EGF increases autophosphorylation on monomers an average of 4.8-fold but has a minimal effect on autophosphorylation of dimers. Furthermore, EGF binding shifts the receptor monomer-dimer equilibrium to the dimer form. We conclude that EGF stimulates in vitro receptor autophosphorylation by inducing kinase-inactive receptor monomers to associate and form receptor dimers, in which conformation the autophosphorylation activity is enhanced.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Böni-Schnetzler M,Pilch PF

doi

10.1073/pnas.84.22.7832

subject

Has Abstract

pub_date

1987-11-01 00:00:00

pages

7832-6

issue

22

eissn

0027-8424

issn

1091-6490

journal_volume

84

pub_type

杂志文章

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