Pin1 modulates ERα levels in breast cancer through inhibition of phosphorylation-dependent ubiquitination and degradation

No abstract is available for this paper.

• Publication year

  2014

• Venue

  Oncogene

• Publication date

  2014-03-13

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/onc.2013.78PMID 23542176PMCID PMC3815749
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Phosphorylation of Estrogen Receptor α at serine 118 directs recruitment of promoter complexes and gene-specific transcription.

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• Pin1 Catalyzes Conformational Changes of Thr-187 in p27Kip1 and Mediates Its Stability through a Polyubiquitination Process*

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• Systematic Mapping of Posttranslational Modifications in Human Estrogen Receptor-α with Emphasis on Novel Phosphorylation Sites*S

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• Proline cis/trans-Isomerase Pin1 Regulates Peroxisome Proliferator-activated Receptor γ Activity through the Direct Binding to the Activation Function-1 Domain*

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• Phosphorylation of activation function-1 regulates proteasome-dependent nuclear mobility and E6-associated protein ubiquitin ligase recruitment to the estrogen receptor beta.

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• E6-associated protein (E6-AP) is a dual function coactivator of steroid hormone receptors

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• Cdk2 and Pin1 negatively regulate the transcriptional corepressor SMRT

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• Estrogen receptor α is a putative substrate for the BRCA1 ubiquitin ligase

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• A Functional Serine 118 Phosphorylation Site in Estrogen Receptor-α Is Required for Down-Regulation of Gene Expression by 17β-Estradiol and 4-Hydroxytamoxifen

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• MUC1 oncoprotein stabilizes and activates estrogen receptor alpha.

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• Deregulated estrogen receptor alpha expression in mammary epithelial cells of transgenic mice results in the development of ductal carcinoma in situ.

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• Differential Regulation of Estrogen-Inducible Proteolysis and Transcription by the Estrogen Receptor α N Terminus

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• Pin1 links the activities of c-Abl and p300 in regulating p73 function.

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• Increases in estrogen receptor‐α concentration in breast cancer cells promote serine 118/104/106‐independent AF‐1 transactivation and growth in the absence of estrogen

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• Ligand‐dependent switching of ubiquitin–proteasome pathways for estrogen receptor

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• Modeling breast cancer in vivo and ex vivo reveals an essential role of Pin1 in tumorigenesis

  2004cited by this paper
• Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling.

  2003cited by this paper
• Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA.

  2003cited by this paper
• Estrogen receptor phosphorylation.

  2003cited by this paper
• Various phosphorylation pathways, depending on agonist and antagonist binding to endogenous estrogen receptor alpha (ERalpha), differentially affect ERalpha extractability, proteasome-mediated stability, and transcriptional activity in human breast cancer cells.

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• Nuclear receptors: integration of multiple signalling pathways through phosphorylation.

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• How the ubiquitin–proteasome system controls transcription

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• Regulation of Estrogen Receptor α-mediated Transcription by a Direct Interaction with Protein Phosphatase 2A*

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• The prolyl isomerase Pin1 in breast development and cancer

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• Various Phosphorylation Pathways, Depending on Agonist and Antagonist Binding to Endogenous Estrogen Receptor α (ERα), Differentially Affect ERα Extractability, Proteasome-Mediated Stability, and Transcriptional Activity in Human Breast Cancer Cells

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• The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response

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• Role of Pin1 in the Regulation of p53 Stability and p21 Transactivation, and Cell Cycle Checkpoints in Response to DNA Damage*

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• Pinning down proline-directed phosphorylation signaling.

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• Loss of Pin1 function in the mouse causes phenotypes resembling cyclin D1-null phenotypes

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• Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method.

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