THE NONCATALYTIC SRC HOMOLOGY REGION-2 SEGMENT OF ABL TYROSINE KINASE BINDS TO TYROSINE-PHOSPHORYLATED CELLULAR PROTEINS WITH HIGH-AFFINITY
THE NONCATALYTIC SRC HOMOLOGY REGION-2 SEGMENT OF ABL TYROSINE KINASE BINDS TO TYROSINE-PHOSPHORYLATED CELLULAR PROTEINS WITH HIGH-AFFINITY
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DOI：
10.1073/pnas.88.2.627
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发表时间：
1991-01-01
影响因子：
11.1
通讯作者：
BALTIMORE, D
中科院分区：
文献类型：
--
作者：
MAYER, BJ;JACKSON, PK;BALTIMORE, D
参与细胞增殖调控的几种蛋白质含有共同的非催化结构域，src同源区2（SH2）。我们使用细菌表达的abl蛋白酪氨酸激酶的SH2结构域来评估该结构域结合细胞蛋白的能力。abl SH2特异性结合许多酪氨酸磷酸化的蛋白质，这些蛋白质来自于在过滤结合试验中被酪氨酸激酶癌基因转化的细胞，并且在溶液中特异性结合这些蛋白质的子集。SH2探针结合几乎完全酪氨酸磷酸化的蛋白质，并通过细胞蛋白质的去磷酸化消除结合。游离磷酸酪氨酸可部分破坏SH2结合，表明磷酸酪氨酸直接参与结合相互作用。这些结果表明，SH2结构域足以赋予直接的，高亲和力的磷酸酪氨酸依赖性结合蛋白质，并建议SH2结构域在细胞信号传导途径中的一般作用。
Several proteins implicated in the regulation of cell proliferation contain a common noncatalytic domain, src homology region 2 (SH2). We have used the bacterially expressed SH2 domain of abl protein-tyrosine kinase to evaluate the ability of this domain to bind to cellular proteins. abl SH2 specifically bound to a number of tyrosine-phosphorylated proteins from cells transformed by tyrosine kinase oncogenes in a filter-binding assay and to a subset of those proteins in solution. The SH2 probe bound almost exclusively to tyrosine-phosphorylated proteins, and binding was eliminated by dephosphorylation of cell proteins. Free phosphotyrosine could partially disrupt SH2 binding, suggesting that phosphotyrosine is directly involved in the binding interaction. These results demonstrate that an SH2 domain is sufficient to confer direct, high-affinity phosphotyrosine-dependent binding to proteins and suggest a general role for SH2 domains in cellular signaling pathways.