Sakaguchi A Y, Sylvia V L, Martinez L, Smith E A, Han E S, Lalley P A, Shows T B, Choudhury G G
Department of Cellular and Structural Biology, University of Texas Health Science Center, San Antonio 78284.
Genomics. 1992 Jan;12(1):151-4. doi: 10.1016/0888-7543(92)90418-r.
Phosphorylation of proteins on tyrosine is crucially involved in signal transduction and mitogenesis and is regulated by both kinases and phosphatases. Recently, a number of soluble and transmembrane receptor-linked protein tyrosine phosphatases (PTPase) have been characterized. Among these is a 48.4-kDa PTPase encoded by a cDNA isolated from a T-lymphocyte library by low-stringency screening with probes derived from placental PTPase 1B. A human T-cell PTPase (PTPT) cDNA and somatic cell hybrids were used to assign a PTPT gene to conserved syntentic groups on human chromosome 18 and on mouse chromosome 18. Two unlinked sequences, one on human chromosome 1, were also detected.
蛋白质酪氨酸磷酸化在信号转导和有丝分裂中至关重要，并受激酶和磷酸酶的调控。最近，已对许多可溶性和跨膜受体相关蛋白酪氨酸磷酸酶（PTPase）进行了表征。其中有一种48.4 kDa的PTPase，由从T淋巴细胞文库中通过用源自胎盘PTPase 1B的探针进行低严格度筛选分离出的cDNA编码。利用人T细胞PTPase（PTPT）cDNA和体细胞杂种，将PTPT基因定位到人18号染色体和小鼠18号染色体上保守的同线群。还检测到两个不连锁的序列，一个位于人1号染色体上。
