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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >MEKK1 PHOSPHORYLATES MEK1 AND MEK2 BUT DOES NOT CAUSE ACTIVATION OF MITOGEN-ACTIVATED PROTEIN KINASE
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MEKK1 PHOSPHORYLATES MEK1 AND MEK2 BUT DOES NOT CAUSE ACTIVATION OF MITOGEN-ACTIVATED PROTEIN KINASE

机译：MEKK1磷酸化MEK1和MEK2不会导致丝裂原活化的蛋白激酶的活化

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摘要

A constitutively active fragment of rat MEK kinase 1 (MEKK1) consisting of only its catalytic domain (MEKK-C) expressed in bacteria quantitatively activates recombinant mitogen-activated protein (MAP) kinase/extracellular signal-regulated protein kinase (ERK) kinases 1 and 2 (MEK1 and MEK2) in vitro. Activation of MEK1 by MEKKI-C is accompanied by phosphorylation of S218 and S222, which are also phosphorylated by the protein kinases c-Mos and Raf-1. MEKK1 has been implicated in regulation of a parallel but distinct cascade that leads to phosphorylation of N terminal sites on c-Jun; thus, its role in the MAP kinase pathway has been questioned. However, in addition to its capacity to phosphorylate MEK1 in vitro, MEKK-C interacts with MEK1 in the two-hybrid system, and expression of mouse MEK1 or MEKK-C in mammalian cells causes constitutive activation of both MEK1 and MEK2. Neither cotransfected nor endogenous ERK2 is highly activated by MEKK1 compared to its stimulation by epidermal growth factor in spite of significant activation of endogenous MEK. Thus, other as Set undefined mechanisms may be involved in determining information flow through the MAP kinase and related pathways. [References: 24]
机译：大鼠MEK激酶1（MEKK1）的组成型活性片段仅由其在细菌中表达的催化结构域（MEKK-C）组成，可定量激活重组促分裂原活化蛋白（MAP）激酶/细胞外信号调节蛋白激酶（ERK）激酶1和2（MEK1和MEK2）在体外。 MEKKI-C对MEK1的激活伴随有S218和S222的磷酸化，它们也被蛋白激酶c-Mos和Raf-1磷酸化。 MEKK1参与调节平行但不同的级联反应，导致c-Jun上N末端位点的磷酸化。因此，其在MAP激酶途径中的作用受到质疑。然而，除了其在体外使MEK1磷酸化的能力外，MEKK-C在双杂交系统中还与MEK1相互作用，并且小鼠MEK1或MEKK-C在哺乳动物细胞中的表达引起MEK1和MEK2的组成性激活。尽管通过内源性MEK的显着活化，但与经表皮生长因子刺激相比，MEKK1均未高度共转化或内源性ERK2活化。因此，在确定通过MAP激酶和相关途径的信息流时可能涉及其他未定义的机制。 [参考：24]

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