Isolation of a Drosophila genomic sequence homologous to the kinase domain of the human insulin receptor and detection of the phosphorylated Drosophila receptor with an anti-peptide antibody.
Isolation of a Drosophila genomic sequence homologous to the kinase domain of the human insulin receptor and detection of the phosphorylated Drosophila receptor with an anti-peptide antibody.
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DOI：
10.1073/pnas.83.13.4710
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发表时间：
1986-07
影响因子：
11.1
通讯作者：
L. Petruzzelli;Roman Herrera;Renee ARENAS-GARCIAt;Rafael FERNANDEZt;Morris J. BIRNBAUMt;Ora M. ROSENt
中科院分区：
文献类型：
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作者：
L. Petruzzelli;Roman Herrera;Renee ARENAS-GARCIAt;Rafael FERNANDEZt;Morris J. BIRNBAUMt;Ora M. ROSENt
已分离出果蝇基因组片段，其推导的氨基酸序列与人胰岛素受体激酶结构域的氨基酸序列惊人地同源。果蝇的DNA与11-腺苷酸酶的mRNA杂交，这是最突出的8至12小时的胚胎。针对在果蝇序列中保守的人胰岛素受体激酶结构域中的序列制备的抗肽抗体免疫沉淀单个95-kDa果蝇蛋白，其酪氨酸残基上的磷酸化依赖于胰岛素。我们的结论是，DNA序列是果蝇胰岛素受体的激酶结构域和95 kDa的磷蛋白是该受体的自磷酸化β亚基。结果是兼容与我们以前的报告表明一个特定的胰岛素结合的果蝇糖蛋白和胰岛素依赖性酪氨酸蛋白激酶，其活动是最大的胚胎发育过程中。这些观察表明胰岛素依赖性蛋白酪氨酸磷酸化在胚胎发生过程中的作用。
A Drosophila genomic fragment has been isolated with a deduced amino acid sequence that is strikingly homologous to that of the kinase domain of the human insulin receptor. The Drosophila DNA hybridizes with an 11-kilobase mRNA that is most prominent in 8- to 12-hr embryos. An anti-peptide antibody prepared to a sequence in the human insulin receptor kinase domain that is conserved in the Drosophila sequence immunoprecipitates a single 95-kDa Drosophila protein whose phosphorylation on tyrosine residues is dependent on insulin. We conclude that the DNA sequence is that of the kinase domain of the Drosophila insulin receptor and that the 95-kDa phosphoprotein is the autophosphorylated beta subunit of that receptor. The results are compatible with our previous reports demonstrating a specific insulin-binding Drosophila glycoprotein and an insulin-dependent tyrosine protein kinase whose activity is greatest during embryogenesis. The observations suggest a role for insulin-dependent protein tyrosine phosphorylation during embryogenesis.