ΔNp73 Modulates Nerve Growth Factor-Mediated Neuronal Differentiation through Repression of TrkA

Zhang, Jin; Chen, Xinbin

doi:10.1128/mcb.02112-06

Cited by 23 publications

(18 citation statements)

References 54 publications

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“…We also showed that TAp73 physically interacted with HDAC1 (Fig. 4, G and H, lanes 3), consistent with previous report (57). Next, we determined whether HDAC1 knockdown would affect the association between TAp73 and Hsp90.…”

Section: Hdac1 Knockdown Induces Hyperacetylation Of Hsp90 and Disrupsupporting

confidence: 74%

TAp73 Protein Stability Is Controlled by Histone Deacetylase 1 via Regulation of Hsp90 Chaperone Function

Zhang

Chen

2013

Journal of Biological Chemistry

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Background: Regulation of p73 by HDAC inhibitor or individual HDAC has not been elucidated. Results: HDAC1 inhibition inactivates Hsp90 and disrupts its binding to TAp73, thereby targeting p73 for proteasomal degradation. Conclusion: HDAC1 is a critical regulator of TAp73 protein stability. Significance: Our data shed a light on a novel regulation of TAp73 protein stability by HDAC1-Hsp90 chaperone complex.

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Section: Hdac1 Knockdown Induces Hyperacetylation Of Hsp90 and Disrupsupporting

confidence: 74%

TAp73 Protein Stability Is Controlled by Histone Deacetylase 1 via Regulation of Hsp90 Chaperone Function

Zhang

Chen

2013

Journal of Biological Chemistry

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“…Cell culture and cell line generation RKO, MCF7, HCT116, p21-null HCT116, and p53-null HCT116 cells were cultured in DMEM (Invitrogen) supplemented with 10% fetal bovine serum (Hyclone) as previously described (Zhang and Chen 2007). p53…”

Section: Plasmidsmentioning

confidence: 99%

“…Western blot analysis was performed as previously described (Zhang and Chen 2007). Cell lysates suspended in 23 SDS sample buffer were resolved by SDS-PAGE, transferred to a nitrocellulose membrane, and probed with the indicated antibodies.…”

Section: Western Blot Analysis and Immunoprecipitationmentioning

confidence: 99%

“…The immunoreactive bands were visualized by enhanced chemiluminescence (Pierce) and quantified by densitometry with the software LabWorks (UVP). The immunoprecipitation assay was performed as previously described (Zhang and Chen 2007). Briefly, cells were lysed in 0.2% Triton lysis buffer (25 mM Tris at pH 7.4, 25 mM NaCl, 0.2% Triton X-100) supplemented with 100 mg/mL proteinase inhibitor cocktail followed by incubation with 1 mg of antibody or control IgG.…”

Section: Western Blot Analysis and Immunoprecipitationmentioning

confidence: 99%

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Glycogen synthase kinase 3 promotes p53 mRNA translation via phosphorylation of RNPC1

Zhang

Chen

et al. 2013

Genes Dev.

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The RNPC1 RNA-binding protein, also called Rbm38, is a target of p53 and a repressor of p53 mRNA translation. Thus, the p53-RNPC1 loop is critical for modulating p53 tumor suppression, but it is not clear how the loop is regulated. Here, we showed that RNPC1 is phosphorylated at Ser195 by glycogen synthase kinase 3 (GSK3). We also showed that GSK3 promotes p53 mRNA translation through phosphorylation of RNPC1. Interestingly, we found that the phosphor-mimetic mutant S195D and the deletion mutant D189-204, which lacks the GSK3 phosphorylation site, are unable to repress p53 mRNA translation due to loss of interaction with eukaryotic translation factor eIF4E on p53 mRNA. Additionally, we found that phosphorylated RNPC1, RNPC1-S195D, and RNPC1(D189-204) promote p53 mRNA translation through interaction with eukaryotic translation factor eIF4G, which then facilitates the assembly of the eIF4F complex on p53 mRNA. Furthermore, we showed that upon inhibition of the phosphatidylinositol 3-kinase (PI3K)-Akt pathway, GSK3 is activated, leading to increased RNPC1 phosphorylation and increased p53 expression in a RNPC1-dependent manner. Together, we postulate that the p53-RNPC1 loop can be explored to increase or decrease p53 activity for cancer therapy.

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“…RKO, MCF7, HCT116, H1299, and SW480 cells were cultured as described (Zhang and Chen 2007). Primary MEFs were cultured in DMEM supplemented with 10% fetal bovine serum.…”

Section: Cell Culturementioning

confidence: 99%

Translational repression of p53 by RNPC1, a p53 target overexpressed in lymphomas

Zhang¹,

Cho²,

Shu³

et al. 2011

Genes Dev.

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117

183

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The p53 pathway is critical for tumor suppression, as the majority of human cancer has a faulty p53. Here, we identified RNPC1, a p53 target and a RNA-binding protein, as a critical regulator of p53 translation. We showed that ectopic expression of RNPC1 inhibited, whereas knockdown of RNPC1 increased, p53 translation under normal and stress conditions. We also showed that RNPC1 prevented cap-binding protein eIF4E from binding p53 mRNA via its C-terminal domain for physical interaction with eIF4E, and its N-terminal domain for binding p53 mRNA. Consistent with this, we found that RNPC1 directly binds to p53 59 and 39untranslated regions (UTRs). Importantly, we showed that RNPC1 inhibits ectopic expression of p53 in a dose-dependent manner via p53 59 or 39 UTR. Moreover, we showed that loss of RNPC1 in mouse embryonic fibroblasts increased the level of p53 protein, leading to enhanced premature senescence in a p53-dependent manner. Finally, to explore the clinical relevance of our finding, we showed that RNPC1 was frequently overexpressed in dog lymphomas, most of which were accompanied by decreased expression of wild-type p53. Together, we identified a novel p53-RNPC1 autoregulatory loop, and our findings suggest that RNPC1 plays a role in tumorigenesis by repressing p53 translation.

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ΔNp73 Modulates Nerve Growth Factor-Mediated Neuronal Differentiation through Repression of TrkA

Cited by 23 publications

References 54 publications

TAp73 Protein Stability Is Controlled by Histone Deacetylase 1 via Regulation of Hsp90 Chaperone Function

TAp73 Protein Stability Is Controlled by Histone Deacetylase 1 via Regulation of Hsp90 Chaperone Function

Glycogen synthase kinase 3 promotes p53 mRNA translation via phosphorylation of RNPC1

Translational repression of p53 by RNPC1, a p53 target overexpressed in lymphomas

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