文章基本信息

标题：Tyrosine phosphorylation is a signal for the trafficking of pp85, an 85-kDa phosphorylated polypeptide associated with phosphatidylinositol kinase activity.
本地全文：下载
作者：B Cohen ; M Yoakim ; H Piwnica-Worms 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1990
卷号：87
期号：12
页码：4458-4462
DOI：10.1073/pnas.87.12.4458
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A family of 85/86-kDa (85K/86K) polypeptides closely linked to phosphatidylinositol kinase activity is found in polyoma middle-sized tumor antigen (MTAg)/pp60c-src complexes. MTAg and the 85-kDa phosphoprotein (pp85) could be reassociated in solution, or on blots, after denaturation with SDS. Results from such experiments focus attention on phosphorylation in controlling intracellular sorting and activation of pp85. Tyrosine phosphorylation seems important for recruitment of pp85 from cytosol to membrane. By blotting, pp85 is substantially cytosolic, whereas that recognized by anti-phosphotyrosine antibody is almost exclusively in membranes. Tyrosine phosphorylation also determined association of pp85 with MTAg. Manipulation of MTAg tyrosine phosphorylation, for example, by expressing MTAg using baculovirus vectors in the absence or presence of pp60c-src, dramatically affects reassociation. Finally, tyrosine phosphorylation appears to be involved in release of pp85 from MTAg, since vanadate increased its rate of dissociation.