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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
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B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A

机译:B细胞受体相关蛋白α4直接对蛋白磷酸酶2A的催化亚基显示雷帕霉素敏感结合

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摘要

Recently, TAP42 was isolated as a high copy suppressor of sit4~-a yeast phosphatase related to protein phosphatase 2A (PP2A). TAP42 is related to the murine α4 protein, which was discovered independently by its association with Ig-α in the B cell receptor complex. Herein we show that a glutathione S-transferase (GST)-α 4 fusion protein bound the catalytic subunit (C) of human PP2A from monomeric or multimeric preparations of PP2A in a "pull-down" assay. In an overlay assay, the GST-α4 protein bound to the phosphor- ylated and unphosphorylated forms of C that were separated in two-dimensional gels and immobilized on filters. The results show direct and exclusive binding of α4 to C.
机译:最近,分离出TAP42作为sit4-与蛋白质磷酸酶2A(PP2A)有关的酵母磷酸酶的高拷贝抑制剂。 TAP42与鼠类α4蛋白有关,该蛋白是通过与B细胞受体复合物中的Ig-α结合而独立发现的。本文中我们显示了谷胱甘肽S-转移酶(GST)-α4融合蛋白在“下拉”测定法中结合了来自PP2A单体或多聚制剂的人PP2A催化亚基(C)。在覆盖分析中,GST-α4蛋白与C的磷酸化和未磷酸化形式结合,后者在二维凝胶中分离并固定在滤膜上。结果表明α4直接和排他地结合到C。

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