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American Society for Microbiology, Molecular and Cellular Biology, 6(11), p. 3191-3202, 1991

DOI: 10.1128/mcb.11.6.3191-3202.1991

American Society for Microbiology, Molecular and Cellular Biology, 6(11), p. 3191-3202, 1991

DOI: 10.1128/mcb.11.6.3191

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The juxtamembrane regions of the epidermal growth factor receptor and gp185erbB-2 determine the specificity of signal transduction.

Journal article published in 1991 by O. Segatto, F. Lonardo, D. Wexler, F. Fazioli, Jh H. Pierce, Dp P. Bottaro ORCID, M. F. White, P. P. Di Fiore, Pp Difiore
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The epidermal growth factor receptor (EGFR) and gp185erbB-2 are closely related tyrosine kinases. Despite extensive sequence and structural homology, these two receptors display quantitative and qualitative differences in their ability to couple with mitogenic signalling pathways. By using chimeric molecules between EGFR and erbB-2, we found that the determinants responsible for the specificity of mitogenic signal transduction are located in the amino-terminal half of the tyrosine kinase domain of either receptor. In the EGFR, mutational analysis within this subdomain revealed that deletion of residues 660 to 667 impaired receptor mitogenic activity without affecting its tyrosine kinase properties. This sequence is therefore likely to contribute to the specificity of substrate recognition by the EGFR kinase.