OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha (Q24295172)

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Patrick C Mahon

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Jane Oh

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Brian Kelly

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Balaji Krishnamachary

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Mia Pearson

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Denise A Chan

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Amato J Giaccia

Expression of hypoxia-inducible factor 1? in brain tumors

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language of work or name

English

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publication date

18 February 2005

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published in

Molecular Cell

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volume

17

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issue

4

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page(s)

503-12

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cites work

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

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Ca2+-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma

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

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Regulation of angiogenesis by hypoxia: role of the HIF system

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Targeting HIF-1 for cancer therapy

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HIF-1 as a target for drug development

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Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

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HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

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

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Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor

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Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

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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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Hypoxia Response Elements in the Aldolase A, Enolase 1, and Lactate Dehydrogenase A Gene Promoters Contain Essential Binding Sites for Hypoxia-inducible Factor 1

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

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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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YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins

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A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta

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Role of prolyl hydroxylation in oncogenically stabilized hypoxia-inducible factor-1alpha

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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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Hypoxia up-regulates prolyl hydroxylase activity: a feedback mechanism that limits HIF-1 responses during reoxygenation

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

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HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia

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Genomic organization of the OS-9 gene amplified in human sarcomas

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Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines

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How oxygen makes its presence felt

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FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

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7 January 2021

Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension

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

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