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首页> 外文期刊>The FEBS journal >Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation
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Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation

机译：基本同源物的增强子在核基质处与支架附着因子B相互作用以调节SR蛋白磷酸化

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摘要

Scaffold attachment factor B1 (SAFB1) is an integral component of the nuclear matrix of vertebrate cells. It binds to DNA on scaffold/matrix attachment region elements, as well as to RNA and a multitude of different proteins, affecting basic cellular activities such as transcription, splicing and DNA damage repair. In the present study, we show that enhancer of rudimentary homologue (ERH) is a new molecular partner of SAFB1 and its 70% homologous paralogue, scaffold attachment factor B2 (SAFB2). ERH interacts directly in the nucleus with the C-terminal Arg-Gly-rich region of SAFB1/2 and co-localizes with it in the insoluble nuclear fraction. ERH, a small ubiquitous protein with striking homology among species and a unique structure, has also been implicated in fundamental cellular mechanisms. Our functional analyses suggest that the SAFB/ERH interaction does not affect SAFB1/2 function in transcription (e.g. as oestrogen receptor a co-repressors), although it reverses the inhibition exerted by SAFB1/2 on the splicing kinase SR protein kinase 1 (SRPK1), which also binds on the C-terminus of SAFB1/2. Accordingly, ERH silencing decreases lamin B receptor and SR protein phosphorylation, which are major SRPK1 substrates, further substantiating the role of SAFB1 and SAFB2 in the co-ordination of nuclear function.
机译：支架附着因子B1（SAFB1）是脊椎动物细胞核基质的整体组分。它与支架/基质附着区域元素的DNA结合，以及RNA和多种不同的蛋白质，影响碱性细胞活性，例如转录，剪接和DNA损伤修复。在本研究中，我们表明，基本同源物（ERH）的增强剂是SAFB1的新分子伴侣及其70％同源级级级级级蛋黄，支架附着因子B2（SAFB2）。 ERH直接在核中与SAFB1 / 2的C-末端甲醇富核区域相互作用，并在不溶性核级分中与其共定。 ERH，一种小普遍存在的蛋白质，具有醒目的物种和独特的结构，也涉及基本的细胞机制。我们的功能分析表明，SAFB / ERH相互作用不会影响转录中的SAFB1 / 2功能（例如作为雌激素受体是共压缩机），尽管它逆转SAFB1 / 2在剪接激酶SR蛋白激酶1上施加的抑制（SRPK1 ），也结合SAFB1 / 2的C末端。因此，ERH沉默降低了Lamin B受体和Sr蛋白磷酸化，其是主要的SRPK1基材，进一步证实了SAFB1和SAFB2在核功能的协调中的作用。

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