PRESENCE OF AN SH2 DOMAIN IN THE ACTIN-BINDING PROTEIN TENSIN
PRESENCE OF AN SH2 DOMAIN IN THE ACTIN-BINDING PROTEIN TENSIN
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DOI：
10.1126/science.1708917
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发表时间：
1991-05-03
期刊：
影响因子：
56.9
通讯作者：
CHEN, LB
中科院分区：
文献类型：
--
作者：
DAVIS, S;LU, ML;CHEN, LB
报道了编码90kodalton的张力蛋白片段的互补DNA的分子克隆。张力蛋白是焦点接触和其他膜下细胞骨架结构的肌动蛋白结合成分。推导的氨基酸序列显示存在一个Src同源2(SH2)结构域。该结构域由许多信号转导蛋白所共有，包括非受体酪氨酸激酶，如Abl、Fps、Src和Src家族成员，转化蛋白Crk，磷脂酶C-伽马-L，PI-3(磷脂酰肌醇)激酶和鸟苷三磷酸酶激活蛋白(GAP)。与在Src、Crk和Abl中发现的SH2结构域一样，张力蛋白的SH2结构域与v-src转化细胞中的一些含磷酸酪氨酸的蛋白特异结合。紧张素也被发现在酪氨酸残基上被磷酸化。这些发现表明，通过同时具有肌动蛋白结合和磷酸酪氨酸结合的活性，张力蛋白本身也是酪氨酸激酶的靶标，可能将信号转导途径与细胞骨架联系起来。
The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported. The derived amino acid sequence revealed the presence of a Src homology 2 (SH2) domain. This domain is shared by a number of signal transduction proteins including nonreceptor tyrosine kinases such as Abl, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-gamma-l, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Abl, the SH2 domain of tensin bound specifically to a number of phosphotyrosine-containing proteins from v-src-transformed cells. Tensin was also found to be phosphorylated on tyrosine residues. These findings suggest that by possessing both actin-binding and phosphotyrosine-binding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.