真核生物翻译起始因子4E的磷酸化在Src转化的细胞系中增加。
Phosphorylation of eukaryotic translation initiation factor 4E is increased in Src-transformed cell lines.
作者信息
Frederickson R M, Montine K S, Sonenberg N
机构信息
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
出版信息
Mol Cell Biol. 1991 May;11(5):2896-900. doi: 10.1128/mcb.11.5.2896-2900.1991.
Abstract
Eukaryotic initiation factor 4F (eIF-4F) is a three-subunit complex that binds the 5' cap structure (m7GpppX, where X is any nucleotide) of eukaryotic mRNAs. This factor facilitates ribosome binding by unwinding the secondary structure in the mRNA 5' noncoding region. The limiting component of the 4F complex is believed to be the 24-kDa cap-binding phosphoprotein, eIF-4E. In this report, we describe the phosphorylation of eIF-4E in response to expression of the tyrosine kinase oncoproteins pp60v-src and pp60c-src527F. The results suggest that eIF-4E functions as a downstream target of the phosphorylation cascade induced by tyrosine-specific protein kinases as well as by effectors of the mitogenic response.
摘要
真核生物起始因子4F（eIF-4F）是一种三聚体复合物，它能结合真核生物mRNA的5'帽结构（m7GpppX，其中X为任意核苷酸）。该因子通过解开mRNA 5'非编码区的二级结构来促进核糖体结合。4F复合物的限速成分被认为是24 kDa的帽结合磷蛋白eIF-4E。在本报告中，我们描述了eIF-4E在酪氨酸激酶癌蛋白pp60v-src和pp60c-src527F表达时的磷酸化情况。结果表明，eIF-4E作为酪氨酸特异性蛋白激酶以及有丝分裂原反应效应物诱导的磷酸化级联反应的下游靶点发挥作用。
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Phosphorylation of eukaryotic translation initiation factor 4E is increased in Src-transformed cell lines.真核生物翻译起始因子4E的磷酸化在Src转化的细胞系中增加。
Mol Cell Biol. 1991 May;11(5):2896-900. doi: 10.1128/mcb.11.5.2896-2900.1991.
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