STABLE ASSOCIATION OF ACTIVATED PP60SRC WITH 2 TYROSINE-PHOSPHORYLATED CELLULAR PROTEINS
STABLE ASSOCIATION OF ACTIVATED PP60SRC WITH 2 TYROSINE-PHOSPHORYLATED CELLULAR PROTEINS
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DOI：
10.1128/mcb.9.9.3951
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发表时间：
1989-09-01
影响因子：
5.3
通讯作者：
PARSONS, JT
中科院分区：
文献类型：
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作者：
REYNOLDS, AB;KANNER, SB;PARSONS, JT
我们在鸡胚细胞中鉴定了两种相对分子质量为130，000（pp 130）和110，000（pp 110）道尔顿的含磷酸酪氨酸的细胞蛋白，它们与pp 60 v-src和鸡pp 60 c-src的活化形式（pp 60527 F）共免疫沉淀。大多数，如果不是所有的酪氨酸磷酸化形式的pp 130和pp 110可以免疫沉淀与任何几个src蛋白特异性单克隆抗体针对至少三个空间上不同的表位裂解物。因此，在用磷酸酪氨酸特异性抗体的免疫印迹上检测到的超过15种突出的磷蛋白中，pp 130和pp 110被src蛋白特异性免疫沉淀选择性地去除，并且它们在免疫沉淀物中的存在似乎是由于与活化的src蛋白的直接相互作用。诱导不同形态表型的SRC蛋白变体在它们与PP 130和PP 110或单独与PP 110形成洗涤剂稳定复合物的能力方面发生改变。突变src蛋白，肉豆蔻酰化缺陷，表现出增加的酪氨酸磷酸化和协会与pp 110。src同源区A盒（pp 60 dl 92/52 F）或B盒（pp 60 dl 155/527 F）突变的src变体的表达诱导pp 130和pp 110磷酸化的差异，以及它们与变体src蛋白的关联的变化。B-box区域内的序列似乎是必要的稳定的复合物形成与pp 130和pp 110，并可能参与活化的src蛋白与细胞底物的相互作用。
We have identified two phosphotyrosine-containing cellular proteins with relative molecular masses of 130,000 (pp130) and 110,000 (pp110) daltons in chicken embryo cells that coimmunoprecipitated with pp60v-src and activated forms of chicken pp60c-src (pp60527F). Most if not all of the tyrosine-phosphorylated forms of pp130 and pp110 could be immunoprecipitated from lysates with any of several src protein-specific monoclonal antibodies directed against at least three spatially distinct epitopes. Consequently, of the more than 15 prominent phosphoproteins detected on immunoblots with phosphotyrosine-specific antibodies, pp130 and pp110 were selectively removed by src protein-specific immunoprecipitation, and their presence in the immunoprecipitates appears to have been due to a direct interaction with activated src proteins. src protein variants that induce different morphological phenotypes were altered in their ability to form detergent-stable complexes with pp130 and pp110 or with pp110 alone. Mutant src proteins, defective for myristylation, showed increased tyrosine phosphorylation of and association with pp110. Expression of src variants with mutations in the A box (pp60dl92/52F) or B box (pp60dl155/527F) of the src homology region induced differences in phosphorylation of pp130 and pp110, as well as changes in their association with variant src proteins. Sequences within the B-box region appeared to be necessary for stable complex formation with pp130 and pp110 and may be involved in the interaction of activated src proteins with cellular substrates.