Evolution of Gab family adaptor proteins.
Evolution of Gab family adaptor proteins.
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Gab 家族接头蛋白的进化。
DOI：
10.1016/s0378-1119(03)00505-5
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发表时间：
2003
期刊：
影响因子：
3.5
通讯作者：
Thackeray,JustinR
中科院分区：
文献类型：
--
作者：
Abbeyquaye,Tetteh;Riesgo-Escovar,Juan;Raabe,Thomas;Thackeray,JustinR
Gab/dos/Soc-1蛋白形成参与受体酪氨酸激酶信号传导的多接头/支架蛋白家族。为了进一步了解Gab家族，特别是果蝇Dos蛋白，我们从Drosophila pseudobscura和Drosophila virilis中分离了一个dos同源物，并将其基因结构和蛋白质序列与Gab家族的其他成员进行了比较。两个保守的内含子的存在证实了dos和gab基因是直向的，但秀丽隐杆线虫的dos或gab基因没有明确的保守内含子。然而，系统发育分析表明，Gab-1可能代表Gab家族的一个分歧成员。除了在所有Gab家族成员中保守性良好的PH结构域之外，蛋白质显示出低水平的序列保守性。在所有Gab家族成员中，可能与酪氨酸磷酸酶的Src同源2（SH 2）结构域结合的两个酪氨酸在C末端是保守的;还鉴定了Dos中的另外两个潜在的SH 2结合位点，以及可能与其他蛋白质中的SH 3或EVH 1结构域结合的几个富含脯氨酸的序列。哺乳动物Gab的一个主要伴侣是磷脂酶C-γ（PLC-γ）; PLC-γ-SH 3：：Dos相互作用的遗传和生物化学测试均为阴性，表明如果果蝇PLC-γ与Dos结合，它必须间接或通过SH 2-磷酸酪氨酸相互作用来实现。
The Gab/dos/Soc-1 proteins form a family of multi-adaptor/scaffolding proteins involved in receptor tyrosine kinase signaling. To further understanding of the Gab family and the Drosophila Dos protein in particular, we isolated a dos homolog from both Drosophila pseudoobscura and Drosophila virilis and compared their gene structures and protein sequences with the rest of the Gab family. The presence of two conserved introns confirmed that the dos and gab genes are orthologous, but the Caenorhabditis elegans soc-1 gene had no unambiguously conserved introns with either dos or gab. However, phylogenetic analysis suggests that soc-1 probably represents a divergent member of the Gab family. Apart from the PH domain, which is well conserved in all Gab family members, the proteins show a low level of sequence conservation. Two tyrosines that probably bind to the Src Homology 2 (SH2) domains of a tyrosine phosphatase in all Gab family members are conserved at the C-terminal end; two other potential SH2-binding sites in Dos were also identified, as well as several proline rich sequences that might bind to SH3 or EVH1 domains in other proteins. A major partner for mammalian Gab is phospholipase C-γ (PLC-γ); genetic and biochemical tests for a PLC-γ-SH3::Dos interaction were negative, indicating that if Drosophila PLC-γ binds to Dos, it must do so indirectly or through an SH2-phosphotyrosine interaction.
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影响因子：
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作者：
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影响因子：
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作者：
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