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首页> 外文期刊>Molecular and Cellular Biology >Deletion of the kinase insert sequence of the platelet-derived growth factor beta-receptor affects receptor kinase activity and signal transduction.
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Deletion of the kinase insert sequence of the platelet-derived growth factor beta-receptor affects receptor kinase activity and signal transduction.

机译：血小板衍生的生长因子β-受体的激酶插入序列的删除影响受体激酶活性和信号转导。

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摘要

A characteristic feature of the platelet-derived growth factor (PDGF) beta-receptor is the presence of an insert sequence in the protein tyrosine kinase domain. A receptor mutant which lacks the entire insert of 98 amino acids was expressed in CHO cells, and its functional characteristics were compared with those of the wild-type receptor. The mutant receptor bound PDGF-BB with high affinity and mediated internalization and degradation of the ligand with efficiency similar to that of the wild-type receptor but did not transduce a mitogenic signal. It was found to display a decreased autophosphorylation after ligand stimulation and had a decreased ability to phosphorylate exogenous substrates; phosphofructokinase was not phosphorylated at all, whereas a peptide substrate was phosphorylated, albeit at a lower rate compared with phosphorylation by the wild-type receptor. Furthermore, the mutant receptor did not mediate actin reorganization but mediated an increase in c-fos expression. The data indicate that the insert in the kinase domain of the PDGF beta-receptor is important for the substrate specificity or catalytic efficiency of the kinase; the deletion of the insert interferes with the transduction of some, but not all, of the signals that arise after activation of the receptor.
机译：血小板衍生的生长因子（PDGF）β受体的特征是蛋白质酪氨酸激酶域中存在插入序列。在CHO细胞中表达了一个缺少98个氨基酸的完整插入片段的受体突变体，并将其功能特性与野生型受体的功能特性进行了比较。突变受体以高亲和力结合PDGF-BB，并以与野生型受体相似的效率介导配体的内化和降解，但不转导有丝分裂信号。发现在配体刺激后其自身磷酸化降低，对外部底物磷酸化的能力也降低。磷酸果糖激酶根本不被磷酸化，而肽底物被磷酸化，尽管与野生型受体的磷酸化相比速率较低。此外，突变受体不介导肌动蛋白重组，但介导c-fos表达的增加。数据表明，PDGFβ-受体的激酶结构域中的插入片段对激酶的底物特异性或催化效率很重要。插入物的缺失会干扰受体激活后产生的一些但不是全部信号的转导。

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