Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation (Q28216594)

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Moon Kyoung Bae

2

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Mee Young Ahn

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Se Hee Kim

4

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Tae Kwon Sohn

5

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Myung Ho Bae

6

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Mi Ae Yoo

7

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Eun Joo Song

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Kyu Won Kim

Jab1 interacts directly with HIF-1alpha and regulates its stability

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language of work or name

English

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publication date

27 November 2002

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published in

Cell

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volume

111

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page(s)

709-20

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issue

5

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cites work

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Regulation of gene expression by transcription factor acetylation

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

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Regulation of activity of the transcription factor GATA-1 by acetylation

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Transcription factor Sp3 is regulated by acetylation

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

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

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A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development

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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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Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

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Expression and characterization of hypoxia-inducible factor (HIF)-3alpha in human kidney: suppression of HIF-mediated gene expression by HIF-3alpha

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

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P/CAF-mediated acetylation regulates the function of the basic helix-loop-helix transcription factor TAL1/SCL

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CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 at functionally important sites

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Genetic manipulation indicates that ARD1 is an essential N(alpha)-acetyltransferase in Trypanosoma brucei

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

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

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

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Histone acetylases and deacetylases in cell proliferation

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Acetylation: a regulatory modification to rival phosphorylation?

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

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Regulation of E2F1 activity by acetylation

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

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

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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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p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-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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Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program

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Regulation of mammalian O2 homeostasis by hypoxia-inducible factor 1

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HIF-1: mediator of physiological and pathophysiological responses to hypoxia

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ATF-2 and C/EBPalpha can form a heterodimeric DNA binding complex in vitro. Functional implications for transcriptional regulation

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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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Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae

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Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling.

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Acetylation and modulation of erythroid Krüppel-like factor (EKLF) activity by interaction with histone acetyltransferases

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