Streuli M
Division of Tumor Immunology, Dana-Farber Cancer Institute, 44 Binney Street, Boston, MA 02115, USA.
Curr Opin Cell Biol. 1996 Apr;8(2):182-8. doi: 10.1016/s0955-0674(96)80064-0.
During the past few years, molecular cloning has established the existence of a structurally diverse family of intracellular and transmembrane protein tyrosine phosphatases (PTPases). The importance of PTPases in signaling is best understood in three model systems: the mammalian transmembrane CD45 PTPase, the Drosophila Src homology (SH)2 domain containing corkscrew PTPase and its vertebrate homolog SH-PTP2, and the mouse SH2-domain-containing hematopoietic cell PTPase. Whereas CD45, corkscrew and SH-PTP2 positively regulate tyrosine phosphorylation, the hematopoietic cell PTPase negatively regulates or terminates signaling. Recent data indicate that several transmembrane PTPases mediate cell adhesion, suggesting that they effect adhesion-specific signaling events.
在过去几年中,分子克隆技术证实了细胞内和跨膜蛋白酪氨酸磷酸酶(PTPases)家族在结构上的多样性。PTPases在信号传导中的重要性在三个模型系统中得到了最好的理解:哺乳动物跨膜CD45 PTPase、果蝇含Src同源(SH)2结构域的螺旋状PTPase及其脊椎动物同源物SH-PTP2,以及小鼠含SH2结构域的造血细胞PTPase。虽然CD45、螺旋状蛋白和SH-PTP2正向调节酪氨酸磷酸化,但造血细胞PTPase则负向调节或终止信号传导。最近的数据表明,几种跨膜PTPases介导细胞黏附,这表明它们影响黏附特异性信号事件。