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Antibody-induced dimerization activates the epidermal growth factor receptor tyrosine kinase

Spaargaren, M, Defize, L H, Boonstra, J, de Laat, S W·1991·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)52357-7
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Abstract

The relationship between epidermal growth factor receptor (EGF-R) protein tyrosine kinase activation and ligand-induced receptor dimerization was investigated using several bivalent anti-EGF-R antibodies directed against various receptor epitopes. In A431 membrane preparations and permeabilized cells, all antibodies were able to activate the EGF-R tyrosine kinase, as measured by EGF-R autophosphorylation and phosphorylation of other substrates on tyrosine residues. EGF-R tyrosine kinase activation correlated strongly with the induction of EGF-R dimerization. (i) Both processes specifically occurred in a narrow antibody concentration range; (ii) both processes required the presence of detergent; and (iii) both processes depended on antibody bivalence since monovalent Fab fragments were inactive yet regained full activity after cross-linking by a second bivalent antibody. These data demonstrate that antibody bivalence is essential and sufficient for EGF-R activation and that activation occurs regardless of the EGF-R epitope recognized. Finally, EGF-R dimerization was shown not to depend on receptor autophosphorylation since it still occurred in the absence of ATP. Also, partial inhibition of the tyrosine kinase activity by the specific EGF-R tyrosine kinase inhibitor tyrphostin AG 213 did not affect formation of EGF-R dimers. Taken together these results demonstrate that induction of EGF-R dimerization is sufficient and in case of antibody action, essential, for activation of t…

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  • Antibodies binding to some cell surface receptors result in antibody internalization because dimerization of the receptor is sufficient to activate the receptor, resulting in internalization into endosome and lysosomes.

    “Antibodies binding to some cell surface receptors result in antibody internalization because dimerization of the receptor is sufficient to activate the receptor, resulting in internalization into endosome and lysosomes (37).”

    From LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation (2023) · cites this paper as [37]

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Metadata

Authors
Spaargaren, M., Defize, L. H., Boonstra, J., & de Laat, S. W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1991-01
Volume
266
Issue
3
Pages
1733-1739
ISSN
0021-9258
DOI
10.1016/s0021-9258(18)52357-7
Cited by
70
References
1
Language
en
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