The forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 alpha by a von Hippel-Lindau protein-independent mechanism (Q24302271)

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English	The forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 alpha by a von Hippel-Lindau protein-independent mechanism	scientific article

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scholarly article

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The forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 alpha by a von Hippel-Lindau protein-independent mechanism (English)

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Forkhead box O4

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GOA release 2020-03-11

negative regulation of angiogenesis

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GOA release 2020-03-11

author name string

Tracy Tzu-Ling Tang

1

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Laurence A Lasky

2

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language of work or name

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publication date

8 August 2003

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Journal of Biological Chemistry

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278

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32

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30125-35

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Signalling through the lipid products of phosphoinositide-3-OH kinase

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

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Cellular signaling: pivoting around PDK-1.

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Direct control of the Forkhead transcription factor AFX by protein kinase B

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Negative regulation of the forkhead transcription factor FKHR by Akt.

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Regulation of nuclear translocation of forkhead transcription factor AFX by protein kinase B

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

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Forkhead transcription factors are critical effectors of cell death and cell cycle arrest downstream of PTEN.

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

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The forkhead transcription factor AFX activates apoptosis by induction of the BCL-6 transcriptional repressor

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

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Protein kinase B/Akt-mediated phosphorylation promotes nuclear exclusion of the winged helix transcription factor FKHR1

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Forkhead transcription factor FKHR-L1 modulates cytokine-dependent transcriptional regulation of p27(KIP1).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

FOXO proteins regulate tumor necrosis factor-related apoptosis inducing ligand expression. Implications for PTEN mutation in prostate cancer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

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Cell cycle inhibition by FoxO forkhead transcription factors involves downregulation of cyclin D.

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

A novel mechanism of gene regulation and tumor suppression by the transcription factor FKHR.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

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Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

HIF-1 and mechanisms of hypoxia sensing

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Signal transduction to hypoxia-inducible factor 1

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein

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https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteasomal degradation irrespective of its subcellular localization: nucleus or cytoplasm

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma

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Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

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HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

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Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

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Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

21 January 2018

A conserved family of prolyl-4-hydroxylases that modify HIF

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302042200

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C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

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HER2 (neu) signaling increases the rate of hypoxia-inducible factor 1alpha (HIF-1alpha) synthesis: novel mechanism for HIF-1-mediated vascular endothelial growth factor expression

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Phosphatidylinositol 3-kinase signaling mediates angiogenesis and expression of vascular endothelial growth factor in endothelial cells

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Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling

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Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase

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Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation

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TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation

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A new Smurf in the village

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The aryl hydrocarbon receptor complex

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Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1

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An essential role for p300/CBP in the cellular response to hypoxia

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Cross-talk between the aryl hydrocarbon receptor and hypoxia inducible factor signaling pathways. Demonstration of competition and compensation

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The Id proteins and angiogenesis

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Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation

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Identifiers

10.1074/JBC.M302042200

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