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

机译:表皮生长因子受体和gp185erbB-2的近膜区域决定了信号转导的特异性。

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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.
机译:表皮生长因子受体(EGFR)和gp185erbB-2是紧密相关的酪氨酸激酶。尽管有广泛的序列和结构同源性,这两种受体在与促有丝分裂信号通路耦合的能力上仍显示出数量和质量上的差异。通过使用EGFR和erbB-2之间的嵌合分子,我们发现负责有丝分裂信号转导特异性的决定因素位于任一受体酪氨酸激酶结构域的氨基末端一半。在EGFR中,该亚结构域内的突变分析表明,残基660至667的缺失损害了受体的有丝分裂活性,而不影响其酪氨酸激酶特性。因此,该序列可能有助于EGFR激酶对底物识别的特异性。

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