کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1963462 1058424 2015 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Serine–Threonine Kinase 38 regulates CDC25A stability and the DNA damage-induced G2/M checkpoint
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Serine–Threonine Kinase 38 regulates CDC25A stability and the DNA damage-induced G2/M checkpoint
چکیده انگلیسی


• STK38 phosphorylates CDC25A at Ser-76 in vivo and in vitro.
• Phosphorylation of Ser-76 regulates CDC25A stability.
• STK38 modulates DNA-damage-induced G2/M checkpoint activation.

Cells respond to DNA damage by activating protein kinase-mediated signaling pathways that promote cell-cycle arrest, DNA repair, or apoptosis. A key regulator of cell-cycle arrest is the CDC25A (cell division cycle 25 homologue A) phosphatase. CDC25A normally plays a pivotal role in regulating the G1/S and G2/M transitions by dephosphorylating and activating cyclin/cyclin-dependent kinase (CDK) complexes; however, CDC25A is specifically degraded in response to DNA damage. Here, we demonstrate that the depletion of serine–threonine kinase 38 (STK38) prevents the DNA-damage-induced degradation of CDC25A and subsequent G2 arrest, and that STK38 directly phosphorylates CDC25A at Ser-76, resulting in CDC25A's degradation. Taken together, these results indicate that the STK38-mediated phosphorylation of CDC25A at Ser-76 and the subsequent degradation of CDC25A are required to promote DNA damage-induced G2/M checkpoint activation.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 27, Issue 8, August 2015, Pages 1569–1575
نویسندگان
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