PARTICIPATION OF TYROSINE PHOSPHORYLATION IN THE CYTOPATHIC EFFECT OF HUMAN-IMMUNODEFICIENCY-VIRUS .1.

被引：103

作者：

COHEN, DI ^{[1
]}

TANI, Y ^{[1
]}

TIAN, H ^{[1
]}

BOONE, E ^{[1
]}

SAMELSON, LE ^{[1
]}

LANE, HC ^{[1
]}

机构：

[1] NICHHD,CELL BIOL & METAB BRANCH,BETHESDA,MD 20892

来源：

SCIENCE | 1992年 / 256卷 / 5056期

关键词：

D O I：

10.1126/science.1570514

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Protein tyrosine phosphorylation is a common mechanism of signaling in pathways that regulate T cell receptor-mediated cell activation, cell proliferation, and the cell cycle. Because human immunodeficiency virus (HIV) is thought to affect normal cell signaling, tyrosine phosphorylation may be associated with HIV cytopathicity. In both HIV-infected cells and transfected cells that stably express HIV envelope glycoproteins undergoing HIVgp41-induced cell fusion, a 30-kilodalton protein was phosphorylated on tyrosine with kinetics similar to those of syncytium formation and cell death. When tyrosine phosphorylation was inhibited by the protein tyrosine kinase inhibitor herbimycin A, envelope-mediated syncytium formation was coordinately reduced. These studies show that specific intracellular signals, which apparently participate in cytopathicity, are generated by HIV and suggest strategies by which the fusion process might be interrupted.

引用

页码：542 / 545

页数：4

共 41 条

[21] BINDING OF HTLV-III/LAV TO T4+ T-CELLS BY A COMPLEX OF THE 110K VIRAL PROTEIN AND THE T4 MOLECULE [J].