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首页> 外文期刊>Molecular and Cellular Biology >Ser-3 is important for regulating Mos interaction with and stimulation of mitogen-activated protein kinase kinase.
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Ser-3 is important for regulating Mos interaction with and stimulation of mitogen-activated protein kinase kinase.

机译：Ser-3对于调节Mos与促分裂原活化的蛋白激酶激酶的相互作用和刺激很重要。

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Mos is a germ cell-specific serine/threonine protein kinase that activates mitogen-activated protein kinase (MAPK) through MAPK kinase (MKK). In Xenopus oocytes, Mos synthesis is required for progesterone-induced activation of MAPK and maturation promoting factor. Injection of Mos or active MAPK causes mitotic arrest in early embryos, suggesting that Mos also acts via MKK and MAPK to induce the arrest of unfertilized eggs in metaphase of meiosis II. We have investigated whether Mos activity is regulated by phosphorylation. Previous studies have identified Ser-3 as the principal autophosphorylation site. We show that Mos interacts with the catalytic domain of MKK in a Saccharomyces cerevisiae two-hybrid test. Acidic substitutions of the sites phosphorylated by Mos in MKK reduce the interaction, implying that the complex may dissociate after phosphorylation of MKK by Mos. Furthermore, the Mos-MKK interaction requires Mos kinase activity, suggesting that Mos autophosphorylation may be involved in the interaction. Substitution of Ser-3 of Mos with Ala reduces the interaction with MKK and also reduces both the activation of MKK by Mos in vitro and cleavage arrest induced by Mos fusion protein in Xenopus embryos. By contrast, substitution of Ser-3 by Glu, an acidic amino acid that mimics phosphoserine, fosters the Mos interaction with MKK and permits activation of MKK in vitro and Mos-induced cleavage arrest. Moreover, the Glu-3 substitution increases the interaction of a kinase-inactive Mos mutant with MKK. Taken together, these results suggest that an important step in Mos activation involves the phosphorylation at Ser-3, which promotes Mos interaction with and activation of MKK.
机译：Mos是一种生殖细胞特异性丝氨酸/苏氨酸蛋白激酶，可通过MAPK激酶（MKK）激活有丝分裂原激活的蛋白激酶（MAPK）。在非洲爪蟾卵母细胞中，Mos合成是孕激素诱导的MAPK激活和成熟促进因子所必需的。注射Mos或活跃的MAPK会导致早期胚胎的有丝分裂停滞，这表明Mos还通过MKK和MAPK起作用，在减数分裂II中期诱导未受精卵的停滞。我们研究了Mos活性是否受磷酸化调节。先前的研究已确定Ser-3为主要的自磷酸化位点。我们表明，在啤酒酵母两杂交试验中，Mos与MKK的催化结构域相互作用。 Mos在MKK中磷酸化的位点的酸性取代降低了相互作用，这意味着在Mos将MKK磷酸化后，复合物可能会解离。此外，Mos-MKK相互作用需要Mos激酶活性，这表明Mos自磷酸化作用可能与该相互作用有关。用Ala取代Mos的Ser-3减少了与MKK的相互作用，同时还减少了Mos在体外对MKK的激活以及在非洲爪蟾胚胎中由Mos融合蛋白诱导的裂解停滞。相比之下，Ser-3被Glu（一种模拟磷酸丝氨酸的酸性氨基酸）取代，促进了Mos与MKK的相互作用，并允许MKK在体外活化和Mos诱导的裂解停滞。此外，Glu-3取代增加了激酶失活的Mos突变体与MKK的相互作用。综上所述，这些结果表明，Mos活化的一个重要步骤涉及Ser-3处的磷酸化，该磷酸化促进Mos与MKK相互作用并激活MKK。

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