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首页> 外文期刊>Molecular and Cellular Biology >Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro.
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Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro.

机译：pp90rsk和独特的蛋白丝氨酸/苏氨酸激酶活性的协调调节，可在体外使重组pp90rsk磷酸化。

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Protein kinase assays that use recombinant pp90rsk as a substrate were developed in an attempt to identify growth-regulated enzymes responsible for the phosphorylation and activation of pp90rsk S6 phosphotransferase activity. With this assay we have ientified a pp60v-src-, growth factor-, phorbol ester-, and vanadate-regulated serine/threonine protein kinase activity that is not related to two other cofactor-independent, growth-regulated protein kinases, pp70-S6 protein kinase and pp90rsk. The pp90rsk-protein kinase activity (referred to as rsk-kinase) is also not related to cofactor-dependent signal transducing protein kinases such as the cyclic AMP-dependent protein kinases, members of the protein kinase C family, or other Ca2(+)-dependent protein kinases. In vitro, partially purified rsk-kinase phosphorylates several of the sites (serine and threonine) that are phosphorylated in growth-stimulated cultured cells. A detailed examination of the mitogen-regulated activation kinetics of rsk-kinase and pp90rsk activities demonstrated that they are coordinately regulated. In addition, protein kinase C is not absolutely required for epidermal and fibroblast growth factor-stimulated activation of rsk-kinase, whereas, like pp90rsk, platelet-derived growth factor- and vanadate-stimulated rsk-kinase activity exhibits a greater dependence on protein kinase C-mediated signal transduction. The characterization and future purification of the rsk-kinase(s) will improve our understanding of the early signaling events regulating cell growth.
机译：开发了使用重组pp90rsk作为底物的蛋白激酶测定法，以试图鉴定负责pp90rsk S6磷酸转移酶活性的磷酸化和激活的生长调节酶。通过这种测定，我们确定了pp60v-src-，生长因子-，佛波酯和钒酸盐调节的丝氨酸/苏氨酸蛋白激酶活性，这与其他两个非辅因子非依赖性，生长调节的蛋白激酶pp70-S6不相关蛋白激酶和pp90rsk。 pp90rsk蛋白激酶活性（称为rsk激酶）也与辅因子依赖性信号转导蛋白激酶（例如环AMP依赖性蛋白激酶，蛋白激酶C家族的成员或其他Ca2 +）无关依赖性蛋白激酶。在体外，部分纯化的rsk激酶会磷酸化一些在生长刺激的培养细胞中被磷酸化的位点（丝氨酸和苏氨酸）。对有丝分裂原调节的rsk激酶和pp90rsk活性的活化动力学的详细检查表明，它们是协同调节的。此外，表皮和成纤维细胞生长因子刺激的rsk激酶活化并非绝对需要蛋白激酶C，而像pp90rsk一样，血小板衍生的生长因子和钒酸盐刺激的rsk激酶活性对蛋白激酶的依赖性更大。 C介导的信号转导。 rsk激酶的特征和未来的纯化将改善我们对调节细胞生长的早期信号事件的理解。

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