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发表时间：
2013
影响因子：
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通讯作者：
M. Whitaker
中科院分区：
文献类型：
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作者：
R. Philipova;M. Whitaker
（2005年）。活性ERK 1在体内被二聚化：双磷酸二聚体产生峰值激酶活性，单磷酸二聚体维持基础ERK 1活性。作者希望纠正他们在绘制图2B时出现的一个错误。修改后的图面板和图例如下所示。(B)海胆胚胎。在第一个有丝分裂细胞周期中，在对应于最大活性（6 min，NEB）和最小活性（未受精，30 min）的时间点，使用抗双磷酸化ERK抗体免疫沉淀活性ERK 1，并使用第二种不同的抗双磷酸化ERK抗体或抗MEK抗体（NEB样品）通过蛋白质印迹法检测。箭头表示ERK 1二聚体。细胞提取物：全细胞提取物富含ERK 1单体，如用抗ERK抗体检测的受精后30分钟细胞提取物的蛋白质印迹所示。有必要加载150 μ g总细胞蛋白，以获得91 kDa的可检测条带，用于与抗双磷酸化ERK抗体免疫沉淀物进行比较。显示了分子量标记物的位置。MAP激酶信号传导途径在整个进化过程中是普遍的和高度保守的（Pouyssegur和Lelands，2003）。在芽殖和分裂酵母中，它控制信息素诱导的交配反应（Choi等人，The same pathway is involved in signal transmission to the nucleus upon mitogenic stimulation of somatic cells（综述参见威尔金森和Millar，2000）。在卵母细胞中，它控制减数分裂和细胞周期，它还参与海胆卵受精后重新进入有丝分裂细胞周期期间的信号转导（Philipova等人，2005 a; Philipova等人，2005 b; Philipova和Whitaker，1998）。蛋白质二聚化已被发现是细胞外信号转导过程中常见的信号基序。对于MAP激酶途径，已经间接显示ERK 2的磷酸化促进体外二聚体的形成。通过使用平衡沉降，Khokhlatchev及其同事已经发现磷酸化的ERK 2在体外主要作为84 kDa物质沉积，而非磷酸化的ERK 2作为较少量的84 kDa和较大量的42 kDa物质的混合物沉积（Khokhlatchev et al.，1998年）。从晶体结构推导出二聚化激酶的模型，
(2005). Active ERK1 is dimerized in vivo: bisphosphodimers generate peak kinase activity and monophosphodimers maintain basal ERK1 activity. The authors would like to correct an error that occurred when they composed Fig. 2B. The revised figure panel and legend are shown below. (B) Sea urchin embryos. Active ERK1 was immunoprecipitated during the first mitotic cell cycle at time points that corresponded to maximum (6 min, NEB) and minimum activity (Unfertilized, 30 min) using an anti-dualphosphorylated ERK antibody and detected by western blotting with a second, different anti-dualphosphorylated ERK antibody or with an anti-MEK antibody (NEB sample). Arrows, active ERK1 dimers. Cell extract: whole-cell extracts are rich in ERK1 monomers as a western blot of a 30 minute post-fertilization cell extract detected with anti-ERK antibody demonstrates. It was necessary to load 150 g total cellular protein in order to obtain a detectable band at 91 kDa for comparison with the anti-dualphosphorylated ERK antibody immunoprecipitate. The positions of molecular mass markers are shown. Introduction The MAP kinase signalling pathway is universal and highly conserved throughout evolution (Pouyssegur and Lenormand, 2003). In budding and fission yeast it controls the pheromone-induced mating response (Choi et al. The same pathway is involved in signal transmission to the nucleus upon mitogenic stimulation of somatic cells (for a review, see Wilkinson and Millar, 2000). In oocytes it controls meiosis and cell cycle It is also involved in signal transduction during re-entry into the mitotic cell cycle after fertilization in sea urchin eggs (Philipova et al., 2005a; Philipova et al., 2005b; Philipova and Whitaker, 1998). Protein dimerization has been found to be a common signalling motif during the transduction of extracellular signals. For MAP kinase pathways, it has been indirectly shown that phosphorylation of ERK2 facilitates the formation of dimers in vitro. By using equilibrium sedimentation, Khokhlatchev and colleagues have found that phosphorylated ERK2 sediments in vitro primarily as an 84 kDa species whereas nonphosphorylated ERK2 sediments as a mixture of a lesser amount of the 84 kDa and a greater amount of the 42 kDa species (Khokhlatchev et al., 1998). A model of dimerized kinase has been deduced from the crystal structure of
影响因子：
2.9
作者：
Mansour, SJ;Candia, JM;Ahn, NG
通讯作者：
Ahn, NG