PP125FAK, A STRUCTURALLY DISTINCTIVE PROTEIN-TYROSINE KINASE ASSOCIATED WITH FOCAL ADHESIONS
PP125FAK, A STRUCTURALLY DISTINCTIVE PROTEIN-TYROSINE KINASE ASSOCIATED WITH FOCAL ADHESIONS
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DOI：
10.1073/pnas.89.11.5192
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发表时间：
1992-06-01
影响因子：
11.1
通讯作者：
PARSONS, JT
中科院分区：
文献类型：
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作者：
SCHALLER, MD;BORGMAN, CA;PARSONS, JT
劳斯肉瘤病毒编码的癌蛋白pp 60 v-src的表达破坏了细胞生长的正常调节，从而导致致癌转化。这一过程需要pp 60 v-src的内在蛋白酪氨酸激酶活性，并与许多细胞蛋白（pp 60 v-src的候选底物）的酪氨酸磷酸化增加有关。我们在这里报告的分离的cDNA编码的蛋白质，pp 125，这是一个主要的含磷酸酪氨酸的蛋白质在未转化的鸡胚细胞，并表现出增加磷酸酪氨酸在pp 60 v-src转化的鸡胚细胞。该cDNA编码一种细胞质蛋白酪氨酸激酶，根据其预测的氨基酸序列和结构，该蛋白酪氨酸激酶是另一个蛋白酪氨酸激酶家族的原型。免疫荧光定位实验表明，pp 125是本地化的粘着斑，因此，我们建议的名称粘着斑激酶。
Expression of the Rous sarcoma virus-encoded oncoprotein, pp60v-src, subverts the normal regulation of cell growth, which results in oncogenic transformation. This process requires the intrinsic protein-tyrosine kinase activity of pp60v-src and is associated with an increase in tyrosine phosphorylation of a number of cellular proteins, candidate substrates for pp60v-src. We report here the isolation of a cDNA encoding a protein, pp125, that is a major phosphotyrosine-containing protein in untransformed chicken embryo cells and exhibits an increase in phosphotyrosine in pp60v-src-transformed chicken embryo cells. This cDNA encodes a cytoplasmic protein-tyrosine kinase which, based upon its predicted amino acid sequence and structure, is the prototype for an additional family of protein-tyrosine kinases. Immunofluorescence localization experiments show that pp125 is localized to focal adhesions; hence, we suggest the name focal adhesion kinase.