A SERINE KINASE REGULATES INTRACELLULAR-LOCALIZATION OF SPLICING FACTORS IN THE CELL CYCLE
A SERINE KINASE REGULATES INTRACELLULAR-LOCALIZATION OF SPLICING FACTORS IN THE CELL CYCLE
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DOI：
10.1038/369678a0
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发表时间：
1994-06-23
期刊：
影响因子：
64.8
通讯作者：
FU, XD
中科院分区：
文献类型：
--
作者：
GUI, JF;LANE, WS;FU, XD
小的核核糖核蛋白颗粒（snRNP）和含有富含丝氨酸/丝氨酸结构域的非snRNP剪接因子（SR蛋白）集中在间期细胞核中的“斑点”中（1）。据信，核斑点作为剪接因子的储存位点，而剪接发生在新生转录本上（2）。剪接因子在转录抑制（3，4）或病毒感染（5）的反应中重新分布，细胞核斑点在有丝分裂过程中分解并改革（6）。我们现在已经鉴定并克隆了一种激酶SRPK 1，它受细胞周期调节，对SR蛋白具有特异性;这种激酶与秀丽隐杆线虫激酶和裂殖酵母激酶Dsk 1相关（参考文献7）。SRPK 1特异性地诱导核斑点的分解，并且高水平的SRPK 1在体外抑制剪接。我们的研究结果表明，SRPK 1 mag有一个核心的作用，在剪接的监管网络，控制在间期细胞的剪接因子的核内分布，并在有丝分裂过程中的核斑点的重组。
Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP splicing factors containing a serine/arginine-rich domain (SR proteins) concentrate in 'speckles' in the nucleus of interphase cells(1). It is believed that nuclear speckles act as storage sites for splicing factors while splicing occurs on nascent transcripts(2). Splicing factors redistribute in response to transcription inhibition(3,4) or viral infection(5), and nuclear speckles break down and reform as cells progress through mitosis(6). We have now identified and cloned a kinase, SRPK1, which is regulated by the cell cycle and is specific for SR proteins; this kinase is related to a Caenorhabditis elegans kinase and to the fission yeast kinase Dsk1 (ref. 7). SRPK1 specifically induces the disassembly of nuclear speckles, and a high level of SRPK1 inhibits splicing in vitro. Our results indicate that SRPK1 mag have a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells, and the reorganization of nuclear speckles during mitosis.