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首页> 外文期刊>Molecular and Cellular Biology >Transmembrane glycoprotein gp150 is a substrate for receptor tyrosine phosphatase DPTP10D in Drosophila cells.
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Transmembrane glycoprotein gp150 is a substrate for receptor tyrosine phosphatase DPTP10D in Drosophila cells.

机译：跨膜糖蛋白gp150是果蝇细胞中受体酪氨酸磷酸酶DPTP10D的底物。

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We have begun to explore the downstream signaling pathways of receptor protein tyrosine phosphatases (RPTPs) that control axon guidance decisions in the Drosophila central nervous system. We have focused our studies on the adhesion molecule-like gp150 protein, which binds directly to and is an in vitro substrate for the RPTP DPTP10D. Here we show that gp150 and DPTP10D form stable complexes in Drosophila Schneider 2 (S2) cells and in wild-type larval tissue. We also demonstrate that the DPTP10D cytoplasmic domain is sufficient to confer binding to gp150. gp150 has a short cytoplasmic domain containing four tyrosines, all found within sequences similar to immunoreceptor family tyrosine-based activation motifs (ITAMs). We demonstrate that gp150 is tyrosine phosphorylated in wild-type larvae. In S2 cells, gp150 becomes tyrosine phosphorylated following incubation with PTP inhibitors or upon coexpression of the Dsrc tyrosine kinase. Phosphorylated Dsrc and an unknown 40-kDa phosphoprotein form stable complexes with gp150, thereby implicating them in a putative gp150 signaling pathway. When coexpressed with gp150, either full-length DPTP10D or its cytoplasmic domain mediates gp150 dephosphorylation whereas a catalytically inactive DPTP10D cytoplasmic domain does not. The neural RPTP DPTP99A can also induce gp150 dephosphorylation but does not coimmunoprecipitate with gp150. Taken together, the results suggest that gp150 transduces signals via phosphorylation of its ITAM-like elements. Phosphotyrosines on gp150 might function as binding sites for downstream signaling molecules, thereby initiating a signaling cascade that could be modulated in vivo by RPTPs such as DPTP10D.
机译：我们已经开始探索控制果蝇中枢神经系统中轴突指导决策的受体蛋白酪氨酸磷酸酶（RPTP）的下游信号通路。我们将研究重点放在粘附分子样gp150蛋白上，该蛋白直接与RPTP DPTP10D结合并是其体外底物。在这里，我们显示gp150和DPTP10D在果蝇Schneider 2（S2）细胞和野生型幼虫组织中形成稳定的复合物。我们还证明了DPTP10D胞质域足以赋予与gp150的结合。 gp150有一个短的胞质结构域，包含四个酪氨酸，所有这些序列都在类似于基于免疫受体家族基于酪氨酸的激活基序（ITAM）的序列中发现。我们证明gp150是酪氨酸在野生型幼虫中被磷酸化。在S2细胞中，在与PTP抑制剂孵育后或在共表达Dsrc酪氨酸激酶后，gp150会被酪氨酸磷酸化。磷酸化的Dsrc和未知的40 kDa磷蛋白与gp150形成稳定的复合物，从而将它们牵涉到推定的gp150信号传导途径中。当与gp150共表达时，全长DPTP10D或其胞质结构域介导gp150去磷酸化，而催化失活的DPTP10D胞质结构域不介导。神经RPTP DPTP99A也可以诱导gp150去磷酸化，但不能与gp150共免疫沉淀。两者合计，结果表明gp150通过其ITAM样元件的磷酸化转导信号。 gp150上的磷酸酪氨酸可能充当下游信号分子的结合位点，从而启动信号级联，该级联可被RPTP（例如DPTP10D）在体内调节。

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