黏着斑激酶与 p53 蛋白的相互作用。
FAK and p53 protein interactions.
机构信息
Department of Surgical Oncology, Roswell Park Cancer Institute, Elm and Carlton Streets, Buffalo, NY 14263, USA.
出版信息
Anticancer Agents Med Chem. 2011 Sep;11(7):617-9. doi: 10.2174/187152011796817619.
Focal Adhesion Kinase plays a major role in cell adhesion, motility, survival, proliferation, metastasis, angiogenesis and lymphangiogenesis. In 2004, we have cloned the promoter sequence of FAK and found that p53 inhibits its activity (BBA, v. 1678, 2004). In 2005, we were the first group to show that FAK and p53 proteins directly interact in the cells (JBC, v. 280, 2005). We have shown that FAK and p53 proteins interact in the cytoplasm and in the nucleus by immunoprecipitation, pull-down and confocal microscopy assays. We have shown that FAK inhibited activity of p53 with the transcriptional targets: p21, Bax and Mdm-2 through protein-protein interactions. We identified the 7 amino-acid site in p53 that is involved in interaction with FAK protein. The present review will discuss the interaction of FAK and p53 proteins and discuss the mechanism of FAK-p53 loop regulation: inhibition of FAK promoter activity by p53 protein and also inhibition of p53 transcriptional activity by FAK protein.
黏着斑激酶在细胞黏附、运动、存活、增殖、转移、血管生成和淋巴管生成中发挥重要作用。2004 年，我们克隆了黏着斑激酶的启动子序列，发现 p53 抑制其活性（BBA，第 1678 卷，2004 年）。2005 年，我们首次证明黏着斑激酶和 p53 蛋白在细胞内直接相互作用（JBC，第 280 卷，2005 年）。通过免疫沉淀、下拉和共聚焦显微镜检测，我们证明黏着斑激酶和 p53 蛋白在细胞质和细胞核中相互作用。我们证明黏着斑激酶通过蛋白-蛋白相互作用抑制 p53 的转录靶标：p21、Bax 和 Mdm-2 的活性。我们确定了 p53 中与黏着斑激酶蛋白相互作用的 7 个氨基酸位点。本综述将讨论黏着斑激酶和 p53 蛋白的相互作用，并讨论黏着斑激酶-p53 循环调节的机制：p53 蛋白抑制黏着斑激酶启动子活性，以及黏着斑激酶蛋白抑制 p53 的转录活性。
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