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Regulation of mitotic function of Chk1 through phosphorylation at novel sites by cyclin-dependent kinase 1 (Cdk1)
T Shiromizu, H Goto, Y Tomono, J Bartek, G Totsukawa, A Inoko, M Nakanishi, F Matsumura, M Inagaki
Jazyk angličtina Země Anglie, Velká Británie
NLK
Free Medical Journals
od 1996 do Před 6 měsíci
Medline Complete (EBSCOhost)
od 1998-01-01 do Před 1 rokem
Wiley Online Library (archiv)
od 1996-01-01 do 2012-12-31
Wiley Free Content
od 1996 do Před 6 měsíci
PubMed
16629900
Knihovny.cz E-zdroje
- MeSH
- biologické modely MeSH
- CHO buňky MeSH
- fosforylace MeSH
- HeLa buňky MeSH
- imunoblotting MeSH
- ionizující záření MeSH
- křečci praví MeSH
- lidé MeSH
- mitóza * fyziologie účinky léků MeSH
- molekulární sekvence - údaje MeSH
- nokodazol farmakologie metabolismus MeSH
- proteinkinasa CDC2 * metabolismus MeSH
- proteinkinasy genetika chemie metabolismus MeSH
- rekombinantní proteiny genetika metabolismus MeSH
- sekvence aminokyselin MeSH
- serin genetika metabolismus MeSH
- transfekce MeSH
- ultrafialové záření MeSH
- zvířata MeSH
- Check Tag
- křečci praví MeSH
- lidé MeSH
- zvířata MeSH
Chk1 is phosphorylated at Ser317 and Ser345 by ATR in response to stalled replication and genotoxic stresses. This Chk1 activation is thought to play critical roles in the prevention of premature mitosis. However, the behavior of Chk1 in mitosis remains largely unknown. Here we reported that Chk1 was phosphorylated in mitosis. The reduction of this phosphorylation was observed at the metaphase-anaphase transition. Two-dimensional phosphopeptide mapping revealed that Chk1 phosphorylation sites in vivo were completely overlapped with the in vitro sites by cyclin-dependent protein kinase (Cdk) 1 or by p38 MAP kinase. Ser286 and Ser301 were identified as novel phosphorylation sites on Chk1. Treatment with Cdk inhibitor butyrolactone I induced the reduction of Chk1-S301 phosphorylation, although treatment with p38-specific inhibitor SB203580 or siRNA did not. In addition, ionizing radiation (IR) or ultraviolet (UV) light did not induce Chk1 phosphorylation at Ser317 and Ser345 in nocodazole-arrested mitotic cells. These observations imply the regulation of mitotic Chk1 function through Chk1 phosphorylation at novel sites by Cdk1.
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