YB-1 as a Cell Cycle-regulated Transcription Factor Facilitating Cyclin A and Cyclin B1 Gene Expression

Jürchott, Karsten; Bergmann, Stephan; Stein, Ulrike; Walther, Wolfgang; Janz, Martin; Manni, Isabella; Piaggio, Giulia; Fietze, Ellen; Dietel, Manfred; Royer, Hans Dieter

doi:10.1074/jbc.m212966200

Cited by 195 publications

(223 citation statements)

References 56 publications

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“…This view is supported by recent evidence that shows an accumulation of proteolytically cleaved YB-1 species in various cancer tissues (Sorokin et al, 2005). These truncated YB-1 proteins carry the CSD but lack the C-terminal cytoplasmic retention domain and therefore localize to the cell nucleus (Stenina et al, 2001;Jurchott et al, 2003;. The mechanism by which nuclear YB-1 contributes to oncogenesis is not known but may be related to the transcriptional and chromosomal regulatory activities of nuclear YB-1 (Bader, 2006).…”

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confidence: 75%

Phosphorylation by Akt disables the anti-oncogenic activity of YB-1

Bader

Vogt

2007

Oncogene

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The Y box-binding protein 1 (YB-1) is a DNA/RNAbinding protein that regulates mRNA transcription and translation. It is a major component of free messenger ribonucleoprotein particles and, at higher concentrations, blocks protein synthesis. In chicken embryo fibroblasts, overexpression of YB-1 confers a specific resistance to oncogenic cellular transformation by phosphoinositide 3-kinase (PI3K) or Akt/PKB. Recent studies have identified YB-1 as a direct substrate of Akt. The functional significance of Akt-mediated phosphorylation remains largely unknown. We generated YB-1 mutants in the Akt phosphorylation consensus sequence to explore the effect of phosphorylated YB-1 in PI3K-induced transformation. In contrast to wild-type YB-1, the phosphomimetic S99E mutant no longer interferes with cellular transformation. This mutant has reduced affinity for the cap of mRNAs and fails to inhibit cap-dependent translation. The data suggest that phosphorylation by Akt disables the inhibitory activity of YB-1 and thereby enhances the translation of transcripts that are necessary for oncogenesis. Overexpression of wild-type YB-1 overrides inactivation by Akt and maintains inhibition of protein synthesis and resistance to transformation.

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confidence: 75%

Phosphorylation by Akt disables the anti-oncogenic activity of YB-1

Bader

Vogt

2007

Oncogene

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“…Notwithstanding these observations, nuclear translocation of YB1 has been shown to occur in a cell cycle stagedependent fashion, occurring only at the G 1 /S phase boundary, 52 that it is dependent on binding to the splicing factor SRp30c, 53 and as mentioned above, it requires Aktdependent phosphorylation. 46 Rationalization of these separate observations has yet to occur, but an association with cell cycle stage could be a possible link.…”

Section: The Y-box-binding Protein Yb1mentioning

confidence: 96%

Some p53-binding proteins that can function as arbiters of life and death

2006

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Four sets of p53-binding proteins are discussed in this review. These are the E2F family, the ASPP family, Y-boxbinding protein YB1, and the prolyl isomerase Pin1. Each appears to play a role in the decision by p53 to induce an arrest of cell proliferation or apoptosis and they may also be independent markers of cancer. Their activities appear to be linked with the cell cycle and they may also interact with each other. In this review, the properties of each protein class are discussed as well as how they affect p53 functions. A model is proposed as to how their activities might be coordinated.

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“…The YB-1 protein has been previously reported to be predominantly located in the cytoplasm in normal and tumor cells throughout the cell cycle (in association with an anchoring protein in the cytoplasm at a binding site on the C-terminal tail domain), but the protein is known to translocate into the nucleus during the G 1 to S phase transition. 20,21 Zhang et al 22 have further demonstrated that nuclear localization of YB-1 requires wild-type p53.…”

Section: Discussionmentioning

confidence: 99%

Y-Box-binding protein-1 is a promising predictive marker of radioresistance and chemoradioresistance in nasopharyngeal cancer

et al. 2009

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The Y-Box-binding protein-1, a member of the cold-shock domain DNA-and RNA-binding protein superfamily, is known to mediate chemoresistance. The aim of this study was to determine the expression of Y-Box- Y-Box-binding protein-1 immunostaining was observed to be predominantly cytoplasmic. A higher recurrence of nasopharyngeal cancer was found in patients whose tissues had increased Y-Box-binding protein-1 expression (Po0.001). The Cox proportionate hazard regression model also established that high Y-Box-binding protein-1 immunoreactivity was significantly correlated with increased risk (2.13 times) of recurrence as compared to low Y-Box-binding protein-1 immunoreactivity (P ¼ 0.01). Within groups of patients treated by radiotherapy or chemoradiotherapy, recurrent cases had significantly higher Y-Box-binding protein-1 expression than nonrecurrent cases (Po0.001 and P ¼ 0.0035, respectively). These data suggest that Y-Box-binding protein-1 expression has clinicopathological significance with potential as a predictive marker of recurrence in nasopharyngeal cancer patients who undergo radiotherapy or chemoradiotherapy.

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YB-1 as a Cell Cycle-regulated Transcription Factor Facilitating Cyclin A and Cyclin B1 Gene Expression

Cited by 195 publications

References 56 publications

Phosphorylation by Akt disables the anti-oncogenic activity of YB-1

Phosphorylation by Akt disables the anti-oncogenic activity of YB-1

Some p53-binding proteins that can function as arbiters of life and death

Y-Box-binding protein-1 is a promising predictive marker of radioresistance and chemoradioresistance in nasopharyngeal cancer

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