KIS is a protein kinase with an RNA recognition motif
KIS is a protein kinase with an RNA recognition motif
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DOI：
10.1074/jbc.272.37.23151
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发表时间：
1997-09-12
影响因子：
4.8
通讯作者：
Sobel, A
中科院分区：
文献类型：
--
作者：
Maucuer, A;Ozon, S;Sobel, A
蛋白质磷酸化参与RNA加工的多个步骤和蛋白质表达的调节，我们在这里首次鉴定了具有RNP型RNA识别基序的丝氨酸/苏氨酸激酶：KIS。我们最初通过与stathmin的相互作用在双杂交筛选中分离出KIS，stathmin是一种小的磷蛋白，在不同细胞内信号传导途径的中继和整合中发挥一般作用。KIS一级序列的测定表明，KIS是由一个与已知激酶同源性很小的激酶核心和一个含有特征性RNA识别基序的C-末端结构域并置而成，该识别基序与剪接因子U2 AF的C-末端基序具有有趣的同源性。它也在体外磷酸化其他经典的底物，如髓鞘碱性蛋白和突触蛋白，但不是组蛋白，抑制其自磷酸化活性。免疫荧光和生化分析表明，KIS在HEK 293成纤维细胞中过表达部分靶向细胞核。总之，这些结果表明KIS可能通过相关因子的磷酸化来控制RNA的运输和/或剪接。
Protein phosphorylation is involved at multiple steps of RNA processing and in the regulation of protein expression, We present here the first identification of a serine/threonine kinase that possesses an RNP-type RNA recognition motif: KIS. We originally isolated KIS in a two-hybrid screen through its interaction with stathmin, a small phosphoprotein proposed to play a general role in the relay and integration of diverse intracellular signaling pathways. Determination of the primary sequence of KIS shows that it is formed by the juxtaposition of a kinase core with little homology to known kinases and a C-terminal domain that contains a characteristic RNA recognition motif with an intriguing homology to the C-terminal motif of the splicing factor U2AF, KIS produced in bacteria has an autophosphorylating activity and phosphorylates stathmin on serine residues. It also phosphorylates in vitro other classical substrates such as myelin basic protein and synapsin but not histones that inhibit its autophosphorylating activity, Immunofluorescence and biochemical analyses indicate that KIS overexpressed in HEK293 fibroblastic cells is partly targetted to the nucleus. Altogether, these results suggest the implication of KIS in the control of trafficking and/or splicing of RNAs probably through phosphorylation of associated factors.