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Titolo:
DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding
Autore:
Zeng, Y; Piwnica-Worms, H;
Indirizzi:
Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USAWashington Univ St Louis MO USA 63110 l & Physiol, St Louis, MO 63110 USA Washington Univ, Sch Med, Howard Hughes Med Inst, St Louis, MO 63110 USA Washington Univ St Louis MO USA 63110 es Med Inst, St Louis, MO 63110 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 11, volume: 19, anno: 1999,
pagine: 7410 - 7419
SICI:
0270-7306(199911)19:11<7410:DDARCI>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CYCLE REGULATION; PHOSPHORYLATES HUMAN CDC25C; PROTEIN-KINASE; SCHIZOSACCHAROMYCES-POMBE; TYROSINE PHOSPHORYLATION; HUMAN WEE1; SERINE KINASE; HUMAN MYT1; S-PHASE; CHK1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Piwnica-Worms, H Washington Univ, Sch Med, Dept Cell Biol & Physiol, Box 8228,660 S Euclid Ave, St Louis, MO 63110 USA Washington Univ Box 8228,660 SEuclid Ave St Louis MO USA 63110
Citazione:
Y. Zeng e H. Piwnica-Worms, "DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding", MOL CELL B, 19(11), 1999, pp. 7410-7419

Abstract

In fission yeast as well as in higher eukaryotic organisms, entry into mitosis is delayed in cells containing damaged or unreplicated DNA. This is accomplished in part by maintaining the Cdc25 phosphatase in a phosphorylatedform that binds 14-3-3 proteins, In this study, me generated a mutant of fission yeast Cdc25 that is severely impaired in its ability to bind 14-3-3 proteins. Loss of both the DNA damage and replication checkpoints was observed in fission yeast cells expressing the 14-3-3 binding mutant. These findings indicate that 14-3-3 binding to Cdc25 is required for fission yeast cells to arrest their cell cycle in response to DNA damage and replication blocks. Furthermore, the 14-3-3 binding mutant localized almost exclusively to the nucleus, unlike wild-type Cdc25 which localized to both the cytoplasmand the nucleus. Nuclear accumulation of wild-type Cdc25 was observed whenfission yeast cells were treated with leptomycin B, indicating that Cdc25 is actively exported from the nucleus. Nuclear exclusion of wild-type Cdc25was observed upon overproduction of Rad 24, one of the two fission yeast 14-3-3 proteins, indicating that one function of Rad 24 is to keep Cdc25 outof the nucleus. In support of this conclusion, Rad 24 overproduction did not alter the nuclear location of the 14-3-3 binding mutant. These results indicate that 14-3-3 binding contributes to the nuclear exclusion of Cdc25 and that the nuclear exclusion of Cdc25 is required for a normal checkpoint response to both damaged and unreplicated DNA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 00:44:35