Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro.

Barrett RM; Colnaghi R; Wheatley SP

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Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro.

机译：survivin的BIR域中的苏氨酸48对于其有丝分裂和抗凋亡活性至关重要，并且在体外可被CK2磷酸化。

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In this study we report that the protein kinase CK2 phosphorylates survivin specifically on threonine 48 (T48) within its BIR domain, and that T48 is critical to both the mitotic and anti-apoptotic roles of survivin. Interestingly, during mitosis T48 mutants localise normally, but are unable to support cell growth when endogenous survivin is removed by siRNA. In addition, while overexpression of survivin normally confers inhibition of TRAIL-mediated apoptosis, this protection is abolished by mutation of T48. Furthermore in interphase cells depletion of endogenous survivin causes redistribution of T48 mutants from the cytoplasm to the nucleus and treatment of cells expressing survivin-GFP with the CK2 inhibitor TBB phenocopies this nuclear redistribution. Finally, we show T48 mutants have increased affinity for borealin, and that this association and cell proliferation can be restored by introduction of a second mutation at T97. To our knowledge these data are the first to identify T48 as a key regulatory site on survivin, and CK2 as a mediator of its mitotic and anti-apoptotic functions.

机译：在这项研究中，我们报道蛋白激酶CK2在其BIR域内的苏氨酸48（T48）上特异性磷酸化survivin，并且T48对survivin的有丝分裂和抗凋亡作用均至关重要。有趣的是，在有丝分裂过程中，T48突变体可以正常定位，但是当内源性survivin被siRNA去除时，则无法支持细胞生长。此外，尽管survivin的过表达通常可以抑制TRAIL介导的细胞凋亡，但这种保护作用会因T48的突变而被取消。此外，在相间细胞中，内源性survivin的耗竭会导致T48突变体从细胞质重新分布到细胞核，并用CK2抑制剂TBB处理表达survivin-GFP的细胞，这种表型复制了这种细胞核重新分布。最后，我们显示T48突变体增加了对北方蛋白的亲和力，并且可以通过在T97引入第二个突变来恢复这种关联和细胞增殖。据我们所知，这些数据是第一个将T48识别为survivin的关键调控位点，而CK2则是其有丝分裂和抗凋亡功能的介质。

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《Cell cycle》 |2011年第3期|共11页
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Barrett RM; Colnaghi R; Wheatley SP;
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中图分类细胞生物学;
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1. Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro. [J] . Barrett RM, Colnaghi R, Wheatley SP Cell cycle . 2011,第3期

机译：survivin的BIR域中的苏氨酸48对于其有丝分裂和抗凋亡活性至关重要，并且在体外可被CK2磷酸化。
2. Phosphorylation of survivin at threonine 34 inhibits its mitotic function and enhances its cytoprotective activity. [J] . Barrett RM, Osborne TP, Wheatley SP Cell cycle . 2009,第2期

机译：苏氨酸34上的survivin磷酸化可抑制其有丝分裂功能并增强其细胞保护活性。
3. Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro. [J] . J Chung, R H Chen, J Blenis Molecular and Cellular Biology . 1991,第4期

机译：pp90rsk和独特的蛋白丝氨酸/苏氨酸激酶活性的协调调节，可在体外使重组pp90rsk磷酸化。
4. Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro [O] . Rachel MA Barrett, Rita Colnaghi, Sally P Wheatley 2011

机译：survivin的BIR结构域中的苏氨酸48对于其有丝分裂和抗凋亡活性至关重要并且可以在体外被CK2磷酸化
5. Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro [O] . Barrett, Rachel MA, Colnaghi, Rita, Wheatley, Sally P 2011

机译：survivin的BIR结构域中的苏氨酸48对于其有丝分裂和抗凋亡活性至关重要，并且可以在体外被CK2磷酸化

Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro.

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