应激诱导ALG-2、RBM22和hSlu7亚细胞分布。
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贾诺维兹，米卡拉克，克列布斯J
应激诱导ALG-2、RBM22和hSlu7亚细胞分布。
生物化学学报，2011年5月;1813(5):1045-9。doi: 10.1016 / j.bbamcr.2010.11.010。Epub 2010 11月29日。
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21122810 (PubMed视图］
- 摘要
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ALG-2是细胞质中高度保守的钙结合蛋白，属于penta-EF手蛋白家族。最近，我们发现ALG-2与高度保守的剪接体核蛋白RBM22相互作用(Montaville et al.)。Biochim。Biophys。学报1763,1335,2006;克雷布斯,Biochim。Biophys。学报1793,979,2009)。在表达这两种蛋白的NIH 3T3细胞中，由于与RBM22-EGFP相互作用，大量ALG-2mRFP被转运到细胞核。hSlu7是另一种剪接体核蛋白，已知在酵母中与RBM22相互作用，已被证明在细胞应激条件下可转移到细胞质。 Here we provide evidence that the 2 spliceosomal proteins differ significantly in their subcellular distributions under stress conditions, and that RBM22 enhances the cytoplasmic translocation of hSlu7 under stress, especially a stress induced by thapsigargin. On the other hand, in NIH 3T3 cells expressing RBM22-EGFP and ALG-2-mRFP, ALG-2 remains translocated into the nucleus under both stress conditions, i.e. heat shock or treatment with thapsigargin. We could further demonstrate that these stress conditions had a different influence on the splicing pattern of XBP-1, a marker for the unfolded protein response indicating that ER stress may play a role in stress-induced translocation of spliceosomal proteins. The article is part of a Special Issue entitled: 11th European Symposium on Calcium.