RBM17 与 U2SURP 和 CHERP 相互作用，调节 RNA 处理蛋白的表达和剪接。
RBM17 Interacts with U2SURP and CHERP to Regulate Expression and Splicing of RNA-Processing Proteins.
机构信息
Program in Developmental Biology, Baylor College of Medicine, Houston, TX 77030, USA; Jan and Dan Duncan Neurological Research Institute at Texas Children's Hospital, Houston, TX 77030, USA.
Jan and Dan Duncan Neurological Research Institute at Texas Children's Hospital, Houston, TX 77030, USA; Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA.
出版信息
Cell Rep. 2018 Oct 16;25(3):726-736.e7. doi: 10.1016/j.celrep.2018.09.041.
RNA splicing entails the coordinated interaction of more than 150 proteins in the spliceosome, one of the most complex of the cell's molecular machines. We previously discovered that the RNA-binding motif protein 17 (RBM17), a component of the spliceosome, is essential for survival and cell maintenance. Here, we find that it interacts with the spliceosomal factors U2SURP and CHERP and that they reciprocally regulate each other's stability, both in mouse and in human cells. Individual knockdown of each of the three proteins induces overlapping changes in splicing and gene expression of transcripts enriched for RNA-processing factors. Our results elucidate the function of RBM17, U2SURP, and CHERP and link the activity of the spliceosome to the regulation of downstream RNA-binding proteins. These data support the hypothesis that, beyond driving constitutive splicing, spliceosomal factors can regulate alternative splicing of specific targets.
RNA 剪接需要剪接体中超过 150 种蛋白质的协调相互作用，剪接体是细胞内最复杂的分子机器之一。我们之前发现，剪接体的组成部分 RNA 结合基序蛋白 17（RBM17）对于生存和细胞维持是必不可少的。在这里，我们发现它与剪接体因子 U2SURP 和 CHERP 相互作用，并且它们在小鼠和人类细胞中相互调节彼此的稳定性。这三种蛋白质中的每一种的单独敲低都会诱导富含 RNA 处理因子的转录本的剪接和基因表达的重叠变化。我们的结果阐明了 RBM17、U2SURP 和 CHERP 的功能，并将剪接体的活性与下游 RNA 结合蛋白的调节联系起来。这些数据支持这样一种假设，即除了驱动组成性剪接之外，剪接体因子还可以调节特定靶标的可变剪接。
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