Nuclear protein tyrosine kinases.

Nuclear protein tyrosine kinases.
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核蛋白酪氨酸激酶。

DOI:
10.1016/0968-0004(94)90114-7
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发表时间:
1994
影响因子:
13.8
通讯作者:
Wang,JY
Wang,JY
中科院分区:
生物学1区
文献类型:
--
作者:
Wang,JY

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蛋白质酪氨酸磷酸化在细胞外信号转导中起重要作用。原型蛋白酪氨酸激酶位于质膜上,并与结合细胞外因子的受体偶联。因此,蛋白质酪氨酸磷酸化以前被认为只发生在细胞质中。然而,最近发现几种细胞质酪氨酸激酶进入细胞核;并且已经发现驻留的核蛋白,例如RNA聚合酶II的催化亚基,在酪氨酸上被磷酸化。核酪氨酸激酶可参与转录、细胞周期和可能的其他核过程的调节。其ldnase结构域中Thr和Tyr残基的磷酸化7。活化的MAPK可以通过尚未确定的机制进入某些细胞类型的细胞核8。细胞质含Y(P)蛋白质核转位的发现可以部分解释生长激素9或胰岛素样生长因子-1(IGF-1)I刺激后细胞核总Y(P)水平升高的观察结果。由于一些细胞质含Y(P)的蛋白质是核转位的靶点,核Y(P)水平的升高不一定表明核酪氨酸激酶的活化。
Protein tyrosine phosphorylation plays an important role in the transduction of extracellular signals. The prototypical protein tyrosine kinases are localized at the plasma membrane and are coupled to receptors that bind extracellular factors. Thus, protein tyrosine phosphorylation was previously thought to occur only in the cytoplasm. However, several cytoplasmic tyrosine kinases have recently been found to enter the nucleus; and resident nuclear proteins, such as the catalytic subunit of RNA polymerase II, have been found to be phosphorylated on tyrosine. Nuclear tyrosine kinases may participate in the regulation of transcription, the cell cycle and possibly other nuclear processes. the phosphorylation of a Thr and a Tyr residue in its ldnase domain 7. The activated MAPK could enter the nucleus in certain cell types through an as yet undefined mechanism 8. Discovery of the nuclear translocation of cytoplasmic Y (P)-containing proteins may explain, in part, the observations that the overall nuclear Y (P) level increases following stimulation with growth hormone 9 or insulin-like growth factor-1 (IGF-1) I. With the knowledge that some cytoplasmic Y (P)-containing proteins are targeted for nuclear translocation, a rise in the nuclear Y (P) level does not necessarily indicate the activation of nuclear tyrosine kinases.
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影响因子: 56.9
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