Prenylation of oncogenic human PTPCAAX protein tyrosine phosphatases
Prenylation of oncogenic human PTPCAAX protein tyrosine phosphatases
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DOI：
10.1016/s0304-3835(96)04459-x
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发表时间：
1996-12-20
期刊：
影响因子：
9.7
通讯作者：
Crowell, DN
中科院分区：
文献类型：
--
作者：
Cates, CA;Michael, RL;Crowell, DN
已知许多异戊二烯化蛋白质参与信号转导，但并非所有异戊二烯化蛋白质都已被鉴定。通过体外异戊二烯化筛选，鉴定出与大鼠 PRL-1 和人 OV-1 蛋白酪氨酸磷酸酶基因同源的两种人 cDNA（PTPCAAXI 和 PTPCAAX2）。 PTPCAAXI 和 PTPCAAX2 在体外被哺乳动物法尼基：蛋白转移酶法尼基化，表位标记的 PTPCAAX2 在上皮细胞中被异戊二烯化。上皮细胞中 PTPCAAXI 和 PTPCAAX2 的过度表达导致培养物表型转变和裸鼠肿瘤生长。因此，PTPCAAXI 和 PTPCAAX2 代表了一类新型异戊二烯化致癌蛋白酪氨酸磷酸酶。
Many isoprenylated proteins are known to participate in signal transduction, but not all have been identified. Using an in vitro prenylation screen, two human cDNAs (PTPCAAXI and PTPCAAX2) homologous to the rat PRL-1 and human OV-1 protein tyrosine phosphatase genes were identified. PTPCAAXI and PTPCAAX2 were farnesylated in vitro by mammalian farnesyl:protein transferase, and epitope-tagged PTPCAAX2 was prenylated in epithelial cells. Overexpression of PTPCAAXI and PTPCAAX2 in epithelial cells caused a transformed phenotype in culture and tumor growth in nude mice. Thus, PTPCAAXI and PTPCAAX2 represent a novel class of isoprenylated, oncogenic protein tyrosine phosphatases.