Adachi M, Sekiya M, Miyachi T, Matsuno K, Hinoda Y, Imai K, Yachi A
Department of Internal Medicine Section 1, Sapporo Medical College, Japan.
FEBS Lett. 1992 Dec 21;314(3):335-9. doi: 10.1016/0014-5793(92)81500-l.
Protein-tyrosine phosphorylation and dephosphorylation are directly associated with cellular growth, signal transduction, and neoplastic transformation. Here we report the isolation of a complementary DNA (cDNA) clone encoding a novel protein-tyrosine phosphatase (PTP) from a human T cell PEER cDNA library. The predicted open reading frame encodes a approximately 68-kDa protein composed of 593 amino acids which contains two src-homology region 2's (SH2 domains) at the N terminus; this PTP is designated as SH-PTP3. Northern blot analysis revealed that SH-PTP3 mRNA was expressed throughout many tissues and the transcriptional size was consistent at about 6.0 kb. As with other SH2 domains in src-family kinases, the SH2 domains of SH-PTP3 may play a crucial role in interactions with tyrosine phosphorylated signaling proteins, including itself and protein tyrosine kinases (PTKs), to regulate targets' enzyme activity.
蛋白质酪氨酸磷酸化和去磷酸化与细胞生长、信号转导及肿瘤转化直接相关。在此，我们报告从人T细胞PEER cDNA文库中分离出一个编码新型蛋白质酪氨酸磷酸酶（PTP）的互补DNA（cDNA）克隆。预测的开放阅读框编码一个由593个氨基酸组成的约68 kDa蛋白质，其在N端含有两个src同源区域2（SH2结构域）；此PTP被命名为SH-PTP3。Northern印迹分析显示SH-PTP3 mRNA在许多组织中均有表达，转录大小约为6.0 kb且保持一致。与src家族激酶中的其他SH2结构域一样，SH-PTP3的SH2结构域可能在与酪氨酸磷酸化信号蛋白（包括其自身和蛋白质酪氨酸激酶（PTK））相互作用以调节靶标酶活性方面发挥关键作用。
