EXPRESSION CLONING OF THE TGF-BETA TYPE-II RECEPTOR, A FUNCTIONAL TRANSMEMBRANE SERINE THREONINE KINASE
EXPRESSION CLONING OF THE TGF-BETA TYPE-II RECEPTOR, A FUNCTIONAL TRANSMEMBRANE SERINE THREONINE KINASE
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DOI：
10.1016/0092-8674(92)90152-3
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发表时间：
1992-02-21
期刊：
影响因子：
64.5
通讯作者：
LODISH, HF
中科院分区：
文献类型：
--
作者：
LIN, HY;WANG, XF;LODISH, HF
用表达克隆的方法克隆了一个编码转化生长因子-βII型受体蛋白的基因。当将克隆的cDNA导入COS细胞时，可导致约80kd的蛋白过表达，该蛋白可与放射性碘标记的转化生长因子-β1特异性结合。过量的转化生长因子-β1以剂量依赖的方式竞争放射性碘标记的转化生长因子-β1的结合，并且比转化生长因子-β-2更有效。预测的受体结构包括一个富含半胱氨酸的胞外区，一个疏水性的跨膜区，和一个预测的细胞质丝氨酸/苏氨酸激酶结构域。在大肠杆菌中表达的含有II型受体胞内结构域的嵌合蛋白在体外可以在丝氨酸和苏氨酸残基上磷酸化，表明II型受体的胞质结构域是一种功能激酶。这一结果暗示丝氨酸/苏氨酸磷酸化是转化生长因子-β受体介导的信号转导的一个重要机制。
A cDNA encoding the TGF-beta type II receptor protein has been isolated by an expression cloning strategy. The cloned cDNA, when transfected into COS cells, leads to overexpression of an approximately 80 kd protein that specifically binds radioiodinated TGF-beta-1. Excess TGF-beta-1 competes for binding of radioiodinated TGF-beta-1 in a dose-dependent manner and is more effective than TGF-beta-2. The predicted receptor structure includes a cysteine-rich extracellular domain, a single hydrophobic transmembrane domain, and a predicted cytoplasmic serine/threonine kinase domain. A chimeric protein containing the intracellular domain of the type II receptor and expressed in E. coli can phosphorylate itself on serine and threonine residues in vitro, indicating that the cytoplasmic domain of the type II receptor is a functional kinase. This result implicates serine/threonine phosphorylation as an important mechanism of TGF-beta receptor-mediated signaling.