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Titolo:
Characterization of an N-terminally truncated cyclin a isoform in mammalian cells
Autore:
Kaufmann, H; Marone, R; Olayioye, MA; Bailey, JE; Fussenegger, M;
Indirizzi:
ETH Honggerberg HPT, Swiss Fed Inst Technol, Inst Biotechnol, CH-8093 Zurich, Switzerland ETH Honggerberg HPT Zurich Switzerland CH-8093 -8093 Zurich, Switzerland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 32, volume: 276, anno: 2001,
pagine: 29987 - 29993
SICI:
0021-9258(20010810)276:32<29987:COANTC>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
HAMSTER OVARY CELLS; DNA-REPLICATION; S-PHASE; EXPRESSION; KINASE; P27(KIP1); GENE; E2F; COMPLEX; CDK2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Fussenegger, M ETH Honggerberg HPT, Swiss Fed Inst Technol, Inst Biotechnol, CH-8093 Zurich, Switzerland ETH Honggerberg HPT Zurich Switzerland CH-8093 witzerland
Citazione:
H. Kaufmann et al., "Characterization of an N-terminally truncated cyclin a isoform in mammalian cells", J BIOL CHEM, 276(32), 2001, pp. 29987-29993

Abstract

Cyclin A is essential for regulating key transitions in the eukaryotic cell cycle including initiation of DNA replication and mitosis. This paper describes the characterization of a truncated cyclin A isoform (cyclin A(t)) in vitro in cultured mammalian cells and in mouse tissues. The presence of cyclin A(t) in specific cell types correlates with the ability of cell extracts to cleave in vitro translated cyclin A. In CHO-K1 cells, cyclin A processing to cyclin A(t) occurs at the N terminus; it does not involve the 26 Sproteasome, nor could it be induced by conditional overexpression of the cyclin-dependent kinase inhibitor p27(Kip1). However, high cell densities lead to increased cyclin A(t) levels. Unlike full-length cyclin A, cyclin A(t) localizes to the cytoplasm, where it binds Cdk2. The data suggest that cyclin A processing occurs in vivo to yield an N-terminally truncated isoformby an unknown mechanism that is regulated by cell density. Differential subcellular localization may provide the first insights into the physiological role of cyclin At.

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Documento generato il 23/09/20 alle ore 21:15:37