p42-MAP kinase is activated in EGF-stimulated interphase but not in metaphase-arrested HeLa cells.
p42-MAP kinase is activated in EGF-stimulated interphase but not in metaphase-arrested HeLa cells.
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p42-MAP 激酶在 EGF 刺激的间期中被激活，但在中期停滞的 HeLa 细胞中不被激活。
DOI：
10.1016/s0014-5793(98)01685-8
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发表时间：
1999
期刊：
影响因子：
3.5
通讯作者：
Gomez-Cambronero,J
中科院分区：
文献类型：
--
作者：
Gomez-Cambronero,J
已知响应于不适当的纺锤体形成而产生的细胞信号导致细胞停滞在细胞周期的中期（M）。我们在这里报告，42 kDa的MAPK（ERK 2）的亚型酪氨酸磷酸化和激活响应表皮生长因子（EGF）在间期，但不是在M-逮捕HeLa细胞。然而，基础水平的活动M-逮捕的细胞高于间期，虽然整体酪氨酰磷酸化的内容是小的。此外，EGF受体及其相关蛋白GTP酶激活蛋白和磷脂酶C在M-阻滞细胞中磷酸化的程度低于它们在间期。这意味着，尽管其基础活性水平高，但在有丝分裂中响应EGF的MAPK活化的稀缺性源于受体和邻近蛋白的磷酸化的早期损伤。这些结果的生物学意义强调了在细胞分裂时保持细胞免受细胞外信号影响的重要性。
It is known that cellular signals produced in response to an inappropriate spindle formation cause the cell to be arrested at metaphase (M) in the cell cycle. We report here that the 42-kDa isoform of MAPK (ERK2) was tyrosyl-phosphorylated and activated in response to epidermal growth factor (EGF) in interphase but not in M-arrested HeLa cells. However, the basal level of activity of M-arrested cells was higher than that of interphase, although the overall tyrosyl phosphorylation content was small. Further, the EGF receptor and its associated proteins GTPase-activating protein and phospholipase C were phosphorylated in M-arrested cells to a lower extent than they were in interphase. This implies that in spite of its high level of basal activity, the scarcity of MAPK activation in mitosis in response to EGF stems from an early impairment of phosphorylation of the receptor and neighboring proteins. The biological significance of these results underlies the importance of keeping the cell sheltered from extracellular signals when it undergoes division.