-
Something wrong with this record ?
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
Language English Country England, Great Britain
NLK
Free Medical Journals
from 1996 to 6 months ago
Medline Complete (EBSCOhost)
from 1998-01-01 to 1 year ago
Wiley Online Library (archiv)
from 1996-01-01 to 2012-12-31
Wiley Free Content
from 1996 to 6 months ago
PubMed
16629900
Knihovny.cz E-resources
- MeSH
- Models, Biological MeSH
- CHO Cells MeSH
- Phosphorylation MeSH
- HeLa Cells MeSH
- Immunoblotting MeSH
- Radiation, Ionizing MeSH
- Cricetinae MeSH
- Humans MeSH
- Mitosis * physiology drug effects MeSH
- Molecular Sequence Data MeSH
- Nocodazole pharmacology metabolism MeSH
- CDC2 Protein Kinase * metabolism MeSH
- Protein Kinases genetics chemistry metabolism MeSH
- Recombinant Proteins genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Serine genetics metabolism MeSH
- Transfection MeSH
- Ultraviolet Rays MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Humans MeSH
- Animals 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.
- 000
- 00000naa a2200000 a 4500
- 001
- bmc14076865
- 003
- CZ-PrNML
- 005
- 20141024120147.0
- 007
- ta
- 008
- 141024s2006 enk f 000 0|eng||
- 009
- AR
- 035 __
- $a (PubMed)16629900
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a enk
- 100 1_
- $a Shiromizu, T. $u Division of Biochemistry, Aichi Cancer Center Research Institute, Nagoya, Aichi 464-8681, Japan.
- 245 10
- $a Regulation of mitotic function of Chk1 through phosphorylation at novel sites by cyclin-dependent kinase 1 (Cdk1) / $c T Shiromizu, H Goto, Y Tomono, J Bartek, G Totsukawa, A Inoko, M Nakanishi, F Matsumura, M Inagaki
- 520 9_
- $a 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.
- 590 __
- $a bohemika - dle Pubmed
- 650 02
- $a sekvence aminokyselin $7 D000595
- 650 02
- $a zvířata $7 D000818
- 650 12
- $a proteinkinasa CDC2 $x metabolismus $7 D016203
- 650 02
- $a CHO buňky $7 D016466
- 650 02
- $a křečci praví $7 D006224
- 650 02
- $a HeLa buňky $7 D006367
- 650 02
- $a lidé $7 D006801
- 650 02
- $a imunoblotting $7 D015151
- 650 02
- $a mitóza $x fyziologie $x účinky léků $7 D008938
- 650 12
- $a mitóza $7 D008938
- 650 02
- $a biologické modely $7 D008954
- 650 02
- $a molekulární sekvence - údaje $7 D008969
- 650 02
- $a nokodazol $x farmakologie $x metabolismus $7 D015739
- 650 02
- $a fosforylace $7 D010766
- 650 02
- $a proteinkinasy $x genetika $x chemie $x metabolismus $7 D011494
- 650 02
- $a ionizující záření $7 D011839
- 650 02
- $a rekombinantní proteiny $x genetika $x metabolismus $7 D011994
- 650 02
- $a serin $x genetika $x metabolismus $7 D012694
- 650 02
- $a transfekce $7 D014162
- 650 02
- $a ultrafialové záření $7 D014466
- 700 1_
- $a Goto, H.
- 700 1_
- $a Tomono, Y.
- 700 1_
- $a Bártek, Jiří, $d 1953- $7 xx0046271
- 700 1_
- $a Totsukawa, G.
- 700 1_
- $a Inoko, A.
- 700 1_
- $a Nakanishi, M.
- 700 1_
- $a Matsumura, F.
- 700 1_
- $a Inagaki, M.
- 773 0_
- $t Genes to Cells $x 1356-9597 $g Roč. 11, č. 5 (2006), s. 477-485 $p Genes Cells $w MED00007231
- 773 0_
- $p Genes Cells $g 11(5):477-85, 2006 May $x 1356-9597
- 910 __
- $a ABA008 $y 4 $z 0
- 990 __
- $a 20141024115836 $b ABA008
- 991 __
- $a 20141024120148 $b ABA008
- 999 __
- $a ok $b bmc $g 1044950 $s 875818
- BAS __
- $a 3
- BMC __
- $a 2006 $b 11 $c 5 $d 477-485 $x MED00007231 $i 1356-9597 $m Genes to cells $n Genes Cells
- LZP __
- $a NLK 2014-1/lp
