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Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases

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title

Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases (English)

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Gregg L Semenza

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author name string

Kiichi Hirota

series ordinal

1

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language of work or name

English

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publication date

9 December 2005

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published in

Biochemical and Biophysical Research Communications

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volume

338

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page(s)

610-6

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issue

1

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cites work

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

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Sequence determinants in hypoxia-inducible factor-1alpha for hydroxylation by the prolyl hydroxylases PHD1, PHD2, and PHD3.

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Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases

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Siah2 regulates stability of prolyl-hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia

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Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1 alpha is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP.

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Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway

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Nitric Oxide Induces Hypoxia-inducible Factor 1 Activation That Is Dependent on MAPK and Phosphatidylinositol 3-Kinase Signaling

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Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation

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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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FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

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Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing

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Hypoxia-inducible factor 1alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations

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Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor

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

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Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha

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Nitric oxide reverses desferrioxamine- and hypoxia-evoked HIF-1alpha accumulation--implications for prolyl hydroxylase activity and iron

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Oxygen sensing requires mitochondrial ROS but not oxidative phosphorylation

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Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing

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Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway

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The use of dioxygen by HIF prolyl hydroxylase (PHD1)

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Models for oxygen sensing in yeast: implications for oxygen-regulated gene expression in higher eucaryotes

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

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Role of nitric oxide in the regulation of HIF-1alpha expression during hypoxia

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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

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

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

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Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

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A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

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Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension

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Inhibition of hypoxia-inducible factor 1 activity by nitric oxide donors in hypoxia

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Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha

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Hypoxia-inducible factor 1, a master transcription factor of cellular hypoxic gene expression.

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Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

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DOI

10.1016/J.BBRC.2005.08.193

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PubMed ID

16154531

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ResearchGate publication ID

7607360

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(Q28271592)

Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl hydroxylases

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