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DOS是一种新型的含pleckstrin同源结构域的蛋白质,是果蝇中sevenless和Ras1之间信号转导所必需的。

DOS, a novel pleckstrin homology domain-containing protein required for signal transduction between sevenless and Ras1 in Drosophila.

作者信息

Raabe T, Riesgo-Escovar J, Liu X, Bausenwein B S, Deak P, Maröy P, Hafen E

机构信息

Theodor Boveri Institut für Biowissenschaften, Lehstuhl für Genetik, Universität Würzburg, Federal Republic of Germany.

出版信息

Cell. 1996 Jun 14;85(6):911-20. doi: 10.1016/s0092-8674(00)81274-x.

Abstract

The specification of the R7 photoreceptor cell in the developing eye of Drosophila is dependent upon activation of the Sevenless (SEV) receptor tyrosine kinase. By screening for mutations that suppress signaling via a constitutively activated SEV protein, we have identified a novel gene, daughter of sevenless (dos). DOS is required not only for signal transduction via SEV but also in other receptor tyrosine kinase signaling pathways throughout development. The presence of an amino-terminally located pleckstrin homology domain and many potential tyrosine phosphorylation sites suggests that DOS functions as an adaptor protein able to interact with multiple signaling molecules. Our genetic analysis demonstrates that DOS functions upstream of Ras1 and defines a signaling pathway that is independent of direct binding of the DRK SH2/SH3 adaptor protein to the SEV receptor tyrosine kinase.

摘要

果蝇发育中的眼睛里R7光感受器细胞的特化依赖于Sevenless(SEV)受体酪氨酸激酶的激活。通过筛选抑制经由组成型激活的SEV蛋白进行信号传导的突变,我们鉴定出一个新基因——sevenless之女(dos)。DOS不仅在整个发育过程中通过SEV进行信号转导时是必需的,在其他受体酪氨酸激酶信号通路中也是必需的。氨基端存在的pleckstrin同源结构域以及许多潜在的酪氨酸磷酸化位点表明,DOS作为一种衔接蛋白发挥作用,能够与多种信号分子相互作用。我们的遗传分析表明,DOS在Ras1的上游发挥作用,并定义了一条独立于DRK SH2/SH3衔接蛋白与SEV受体酪氨酸激酶直接结合的信号通路。

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