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许多细胞因子受体尽管缺少激酶结构域,但与配体结合后仍能诱导蛋白质的酪氨酸磷酸化。近年来的研究证明这一过程是由JaK族蛋白质酪氨酸激酶的成员所介导的。Jak激酶通过和受体的近膜区域的相互作用而与之缔合。配体结合引起受体聚合以及Jak的酪氨酸磷酸化和激活,激活的Jak又使受体和STAT蛋白(信号转导物与转录激活剂)磷酸化、后者直接参与基因转录的调控。本文对这一新的胞内信号转导机制作一综述。
Many cytokine receptors, in spite of the absence of a kinase domain, induce tyrosine phosphorylation of the protein upon binding to the ligand. Recent studies have demonstrated that this process is mediated by members of the JaK family of protein tyrosine kinases. Jak kinase associates with it through its interaction with the proximal membrane region of the receptor. Ligand binding causes receptor polymerization and tyrosine phosphorylation and activation of Jak, which in turn phosphorylates receptors and STAT proteins (signal transducers and transcriptional activators), which are directly involved in the regulation of gene transcription. This article reviews the new intracellular signal transduction mechanism.