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Titolo:
Loss of a protein phosphatase 2A regulatory subunit (Cdc55p) elicits improper regulation of Swe1p degradation
Autore:
Yang, HF; Jiang, W; Gentry, M; Hallberg, RL;
Indirizzi:
Syracuse Univ, Dept Biol, Syracuse, NY 13244 USA Syracuse Univ Syracuse NY USA 13244 iv, Dept Biol, Syracuse, NY 13244 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 21, volume: 20, anno: 2000,
pagine: 8143 - 8156
SICI:
0270-7306(200011)20:21<8143:LOAPP2>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST-CELL CYCLE; SACCHAROMYCES-CEREVISIAE; BUDDING YEAST; MORPHOGENESIS CHECKPOINT; TYROSINE PHOSPHORYLATION; ACTIN CYTOSKELETON; FISSION YEAST; S-PHASE; MITOSIS; KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Hallberg, RL Syracuse Univ, Dept Biol, 411 Lyman Hall, Syracuse, NY 13244 USA Syracuse Univ 411 Lyman Hall Syracuse NY USA 13244 13244 USA
Citazione:
H.F. Yang et al., "Loss of a protein phosphatase 2A regulatory subunit (Cdc55p) elicits improper regulation of Swe1p degradation", MOL CELL B, 20(21), 2000, pp. 8143-8156

Abstract

CDC55 encodes a Saccharomyces cerevisiae protein phosphatase 2A (PP2A) regulatory subunit. cdc55-null cells growing at low temperature exhibit a failure of cytokinesis and produce abnormally elongated buds, but cdc55-null cells producing the cyclin-dependent kinase Cdc28-Y19F, which is unable to beinhibited by Y19 phosphorylation, show a loss of the abnormal morphology. Furthermore, cdc55-null cells exhibit a hyperphosphorylation of Y19. For these reasons, we have examined in wild-type and cdc55-null. cells the levelsand activities of the kinase (Swe1p) and phosphatase (Mih1p) that normallyregulate the extent of Cdc28 Y19 phosphorylation. We find that Mih1p levels are comparable in the two strains, and an estimate of the in vivo and in vitro phosphatase activity of this enzyme in the two cell types indicates no marked differences. By contrast, while Swe1p levels are similar in unsynchronized and S-phase-arrested wild-type and cdc55-null cells, Swe1 kinase is found at elevated levels in mitosis-arrested cdc55-null cells. This excess Swe1p in cdc55-null cells is the result of ectopic stabilization of this protein during G(2) and M, thereby accounting for the accumulation of Swe1pin mitosis arrested cells. We also present evidence indicating that, in cdc55-null cells, misregulated PP2A phosphatase activity is the cause of boththe ectopic stabilization of Swe1p and the production of the morphologically abnormal phenotype.

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Documento generato il 23/01/20 alle ore 03:49:37