메뉴 건너뛰기




Volumn 16, Issue 12, 2006, Pages 616-621

ARDent about acetylation and deacetylation in hypoxia signalling

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; ARREST DEFECTIVE 1 ENZYME; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; HYPOXIA INDUCIBLE FACTOR 1; UNCLASSIFIED DRUG;

EID: 33751344759     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2006.10.002     Document Type: Article
Times cited : (33)

References (53)
  • 1
    • 4644370374 scopus 로고    scopus 로고
    • Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslational modifications
    • Brahimi-Horn C., et al. Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslational modifications. Cell. Signal. 17 (2005) 1-9
    • (2005) Cell. Signal. , vol.17 , pp. 1-9
    • Brahimi-Horn, C.1
  • 2
    • 0038037735 scopus 로고    scopus 로고
    • Regulation of angiogenesis by hypoxia: role of the HIF system
    • Pugh C.W., and Ratcliffe P.J. Regulation of angiogenesis by hypoxia: role of the HIF system. Nat. Med. 9 (2003) 677-684
    • (2003) Nat. Med. , vol.9 , pp. 677-684
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 3
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza G.L. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 3 (2003) 721-732
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 4
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signalling in cancer and approaches to enforce tumour regression
    • Pouyssegur J., et al. Hypoxia signalling in cancer and approaches to enforce tumour regression. Nature 441 (2006) 437-443
    • (2006) Nature , vol.441 , pp. 437-443
    • Pouyssegur, J.1
  • 6
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation
    • Jeong J.W., et al. Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. Cell 111 (2002) 709-720
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1
  • 7
    • 0033837634 scopus 로고    scopus 로고
    • Regulation of gene expression by transcription factor acetylation
    • Bannister A.J., and Miska E.A. Regulation of gene expression by transcription factor acetylation. Cell. Mol. Life Sci. 57 (2000) 1184-1192
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1184-1192
    • Bannister, A.J.1    Miska, E.A.2
  • 8
    • 0041848257 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic N-terminal acetyltransferase subunits
    • Polevoda B., and Sherman F. Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem. Biophys. Res. Commun. 308 (2003) 1-11
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 1-11
    • Polevoda, B.1    Sherman, F.2
  • 9
    • 0023426588 scopus 로고
    • The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus
    • Whiteway M., et al. The yeast ARD1 gene product is required for repression of cryptic mating-type information at the HML locus. Mol. Cell. Biol. 7 (1987) 3713-3722
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3713-3722
    • Whiteway, M.1
  • 10
    • 0022407123 scopus 로고
    • The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways
    • Whiteway M., and Szostak J.W. The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 43 (1985) 483-492
    • (1985) Cell , vol.43 , pp. 483-492
    • Whiteway, M.1    Szostak, J.W.2
  • 11
    • 0141640821 scopus 로고    scopus 로고
    • The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
    • Gautschi M., et al. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol. Cell. Biol. 23 (2003) 7403-7414
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7403-7414
    • Gautschi, M.1
  • 12
    • 0034494265 scopus 로고    scopus 로고
    • Genetic manipulation indicates that ARD1 is an essential N(infinity)-acetyltransferase in Trypanosoma brucei
    • Ingram A.K., et al. Genetic manipulation indicates that ARD1 is an essential N(infinity)-acetyltransferase in Trypanosoma brucei. Mol. Biochem. Parasitol. 111 (2000) 309-317
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 309-317
    • Ingram, A.K.1
  • 13
    • 0344663967 scopus 로고    scopus 로고
    • Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila
    • Williams B.C., et al. Two putative acetyltransferases, san and deco, are required for establishing sister chromatid cohesion in Drosophila. Curr. Biol. 13 (2003) 2025-2036
    • (2003) Curr. Biol. , vol.13 , pp. 2025-2036
    • Williams, B.C.1
  • 14
    • 15944413192 scopus 로고    scopus 로고
    • Identification and characterization of the human ARD1-NATH protein acetyltransferase complex
    • Arnesen T., et al. Identification and characterization of the human ARD1-NATH protein acetyltransferase complex. Biochem. J. 386 (2005) 433-443
    • (2005) Biochem. J. , vol.386 , pp. 433-443
    • Arnesen, T.1
  • 15
    • 33744971921 scopus 로고    scopus 로고
    • Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex
    • Arnesen T., et al. Induction of apoptosis in human cells by RNAi-mediated knockdown of hARD1 and NATH, components of the protein N-alpha-acetyltransferase complex. Oncogene 25 (2006) 4350-4360
    • (2006) Oncogene , vol.25 , pp. 4350-4360
    • Arnesen, T.1
  • 16
    • 20544431636 scopus 로고    scopus 로고
    • Analysis of ARD1 function in hypoxia response using retroviral RNA interference
    • Fisher T.S., et al. Analysis of ARD1 function in hypoxia response using retroviral RNA interference. J. Biol. Chem. 280 (2005) 17749-17757
    • (2005) J. Biol. Chem. , vol.280 , pp. 17749-17757
    • Fisher, T.S.1
  • 17
    • 33744979048 scopus 로고    scopus 로고
    • Characterization of hARD2, a processed hARD1 gene duplicate encoding a human protein N-alpha-acetyltransferase
    • Arnesen T., et al. Characterization of hARD2, a processed hARD1 gene duplicate encoding a human protein N-alpha-acetyltransferase. BMC Biochem. 7 (2006) 13
    • (2006) BMC Biochem. , vol.7 , pp. 13
    • Arnesen, T.1
  • 18
    • 0028222543 scopus 로고
    • Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae
    • Tribioli C., et al. Isolation of new genes in distal Xq28: transcriptional map and identification of a human homologue of the ARD1 N-acetyl transferase of Saccharomyces cerevisiae. Hum. Mol. Genet. 3 (1994) 1061-1067
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1061-1067
    • Tribioli, C.1
  • 19
    • 29644438345 scopus 로고    scopus 로고
    • Characterization of ARD1 variants in mammalian cells
    • Kim S.H., et al. Characterization of ARD1 variants in mammalian cells. Biochem. Biophys. Res. Commun. 340 (2006) 422-427
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 422-427
    • Kim, S.H.1
  • 20
    • 33746491112 scopus 로고    scopus 로고
    • Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1
    • Sanchez-Puig N., and Fersht A.R. Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1. Protein Sci. 15 (2006) 1968-1976
    • (2006) Protein Sci. , vol.15 , pp. 1968-1976
    • Sanchez-Puig, N.1    Fersht, A.R.2
  • 21
    • 24744460523 scopus 로고    scopus 로고
    • Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1alpha and is not induced by hypoxia or HIF
    • Bilton R., et al. Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1alpha and is not induced by hypoxia or HIF. J. Biol. Chem. 280 (2005) 31132-31140
    • (2005) J. Biol. Chem. , vol.280 , pp. 31132-31140
    • Bilton, R.1
  • 22
    • 0141925607 scopus 로고    scopus 로고
    • An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development
    • Sugiura N., et al. An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development. J. Biol. Chem. 278 (2003) 40113-40120
    • (2003) J. Biol. Chem. , vol.278 , pp. 40113-40120
    • Sugiura, N.1
  • 23
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1alpha
    • Arnesen T., et al. Interaction between HIF-1alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1alpha. FEBS Lett. 579 (2005) 6428-6432
    • (2005) FEBS Lett. , vol.579 , pp. 6428-6432
    • Arnesen, T.1
  • 24
    • 33645322383 scopus 로고    scopus 로고
    • Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1
    • Yoo Y.G., et al. Metastasis-associated protein 1 enhances stability of hypoxia-inducible factor-1alpha protein by recruiting histone deacetylase 1. EMBO J. 25 (2006) 1231-1241
    • (2006) EMBO J. , vol.25 , pp. 1231-1241
    • Yoo, Y.G.1
  • 25
    • 33746776975 scopus 로고    scopus 로고
    • Effect of connective tissue growth factor on hypoxia-inducible factor 1alpha degradation and tumor angiogenesis
    • Chang C.C., et al. Effect of connective tissue growth factor on hypoxia-inducible factor 1alpha degradation and tumor angiogenesis. J. Natl. Cancer Inst. 98 (2006) 984-995
    • (2006) J. Natl. Cancer Inst. , vol.98 , pp. 984-995
    • Chang, C.C.1
  • 26
    • 4944248618 scopus 로고    scopus 로고
    • Berberine inhibits HIF-1alpha expression via enhanced proteolysis
    • Lin S., et al. Berberine inhibits HIF-1alpha expression via enhanced proteolysis. Mol. Pharmacol. 66 (2004) 612-619
    • (2004) Mol. Pharmacol. , vol.66 , pp. 612-619
    • Lin, S.1
  • 27
    • 33749006252 scopus 로고    scopus 로고
    • Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1{alpha}
    • Qian D.Z., et al. Class II histone deacetylases are associated with VHL-independent regulation of hypoxia-inducible factor 1{alpha}. Cancer Res. 66 (2006) 8814-8821
    • (2006) Cancer Res. , vol.66 , pp. 8814-8821
    • Qian, D.Z.1
  • 28
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha
    • Fath D.M., et al. Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J. Biol. Chem. 281 (2006) 13612-13619
    • (2006) J. Biol. Chem. , vol.281 , pp. 13612-13619
    • Fath, D.M.1
  • 29
    • 33645236747 scopus 로고    scopus 로고
    • Purified recombinant hARD1 does not catalyse acetylation of Lys(532) of HIF-1alpha fragments in vitro
    • Murray-Rust T.A., et al. Purified recombinant hARD1 does not catalyse acetylation of Lys(532) of HIF-1alpha fragments in vitro. FEBS Lett. 580 (2006) 1911-1918
    • (2006) FEBS Lett. , vol.580 , pp. 1911-1918
    • Murray-Rust, T.A.1
  • 30
    • 0034663894 scopus 로고    scopus 로고
    • Mechanism of regulation of the hypoxia-inducible factor-1alpha by the von Hippel-Lindau tumor suppressor protein
    • Tanimoto K., et al. Mechanism of regulation of the hypoxia-inducible factor-1alpha by the von Hippel-Lindau tumor suppressor protein. EMBO J. 19 (2000) 4298-4309
    • (2000) EMBO J. , vol.19 , pp. 4298-4309
    • Tanimoto, K.1
  • 31
    • 27944445890 scopus 로고    scopus 로고
    • Differential responses of two degradation domains of HIF-1alpha to hypoxia and iron deficiency
    • Lee K.H., et al. Differential responses of two degradation domains of HIF-1alpha to hypoxia and iron deficiency. Biochimie 88 (2006) 163-169
    • (2006) Biochimie , vol.88 , pp. 163-169
    • Lee, K.H.1
  • 32
    • 0346059588 scopus 로고    scopus 로고
    • Phorbol ester stimulates the nonhypoxic induction of a novel hypoxia-inducible factor 1alpha isoform: implications for tumor promotion
    • Chun Y.S., et al. Phorbol ester stimulates the nonhypoxic induction of a novel hypoxia-inducible factor 1alpha isoform: implications for tumor promotion. Cancer Res. 63 (2003) 8700-8707
    • (2003) Cancer Res. , vol.63 , pp. 8700-8707
    • Chun, Y.S.1
  • 33
    • 85047699941 scopus 로고    scopus 로고
    • Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling
    • Deroanne C.F., et al. Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. Oncogene 21 (2002) 427-436
    • (2002) Oncogene , vol.21 , pp. 427-436
    • Deroanne, C.F.1
  • 34
    • 0035048449 scopus 로고    scopus 로고
    • Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes
    • Kim M.S., et al. Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes. Nat. Med. 7 (2001) 437-443
    • (2001) Nat. Med. , vol.7 , pp. 437-443
    • Kim, M.S.1
  • 35
    • 31544464120 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with histone deacetylase inhibitors: the hydroxamic acid derivative LBH589
    • Qian D.Z., et al. Targeting tumor angiogenesis with histone deacetylase inhibitors: the hydroxamic acid derivative LBH589. Clin. Cancer Res. 12 (2006) 634-642
    • (2006) Clin. Cancer Res. , vol.12 , pp. 634-642
    • Qian, D.Z.1
  • 36
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • Bolden J.E., et al. Anticancer activities of histone deacetylase inhibitors. Nat. Rev. Drug Discov. 5 (2006) 769-784
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 769-784
    • Bolden, J.E.1
  • 37
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S., and Pelicci P.G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 6 (2006) 38-51
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 38
    • 0035887011 scopus 로고    scopus 로고
    • FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity
    • Mahon P.C., et al. FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. Genes Dev. 15 (2001) 2675-2686
    • (2001) Genes Dev. , vol.15 , pp. 2675-2686
    • Mahon, P.C.1
  • 39
    • 4744368147 scopus 로고    scopus 로고
    • Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity
    • Kato H., et al. Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity. J. Biol. Chem. 279 (2004) 41966-41974
    • (2004) J. Biol. Chem. , vol.279 , pp. 41966-41974
    • Kato, H.1
  • 40
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P., et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J. Biol. Chem. 280 (2005) 26729-26734
    • (2005) J. Biol. Chem. , vol.280 , pp. 26729-26734
    • Bali, P.1
  • 41
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • Isaacs J.S., et al. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J. Biol. Chem. 277 (2002) 29936-29944
    • (2002) J. Biol. Chem. , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1
  • 42
    • 33644780111 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1{alpha}
    • Kong X., et al. Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1{alpha}. Mol. Cell. Biol. 26 (2006) 2019-2028
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2019-2028
    • Kong, X.1
  • 43
    • 27844514169 scopus 로고    scopus 로고
    • Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression
    • Kasper L.H., et al. Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression. EMBO J. 24 (2005) 3846-3858
    • (2005) EMBO J. , vol.24 , pp. 3846-3858
    • Kasper, L.H.1
  • 44
    • 0036673950 scopus 로고    scopus 로고
    • NATH, a novel gene overexpressed in papillary thyroid carcinomas
    • Fluge O., et al. NATH, a novel gene overexpressed in papillary thyroid carcinomas. Oncogene 21 (2002) 5056-5068
    • (2002) Oncogene , vol.21 , pp. 5056-5068
    • Fluge, O.1
  • 45
    • 0037024449 scopus 로고    scopus 로고
    • Serological identification and expression analysis of gastric cancer-associated genes
    • Line A., et al. Serological identification and expression analysis of gastric cancer-associated genes. Br. J. Cancer 86 (2002) 1824-1830
    • (2002) Br. J. Cancer , vol.86 , pp. 1824-1830
    • Line, A.1
  • 46
    • 27744441053 scopus 로고    scopus 로고
    • Expression of N-acetyl transferase human and human arrest defective 1 proteins in thyroid neoplasms
    • Arnesen T., et al. Expression of N-acetyl transferase human and human arrest defective 1 proteins in thyroid neoplasms. Thyroid 15 (2005) 1131-1136
    • (2005) Thyroid , vol.15 , pp. 1131-1136
    • Arnesen, T.1
  • 47
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald A.F., and Landsman D. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22 (1997) 154-155
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 48
    • 0024461828 scopus 로고
    • Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast
    • Mullen J.R., et al. Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J. 8 (1989) 2067-2075
    • (1989) EMBO J. , vol.8 , pp. 2067-2075
    • Mullen, J.R.1
  • 49
    • 0026605888 scopus 로고
    • ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity
    • Park E.C., and Szostak J.W. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 11 (1992) 2087-2093
    • (1992) EMBO J. , vol.11 , pp. 2087-2093
    • Park, E.C.1    Szostak, J.W.2
  • 50
    • 33645757829 scopus 로고    scopus 로고
    • Cloning and characterization of hNAT5/hSAN: An evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex
    • Arnesen T., et al. Cloning and characterization of hNAT5/hSAN: An evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex. Gene 371 (2006) 291-295
    • (2006) Gene , vol.371 , pp. 291-295
    • Arnesen, T.1
  • 51
    • 33751328013 scopus 로고    scopus 로고
    • HIF-1alpha & ARD1: enemies, friends or neither
    • Arnesen T. HIF-1alpha & ARD1: enemies, friends or neither. Nat. Rev. Cancer 6 (2006) 249
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 249
    • Arnesen, T.1
  • 52
    • 30744449235 scopus 로고    scopus 로고
    • Angiogenesis as a therapeutic target
    • Ferrara N., and Kerbel R.S. Angiogenesis as a therapeutic target. Nature 438 (2005) 967-974
    • (2005) Nature , vol.438 , pp. 967-974
    • Ferrara, N.1    Kerbel, R.S.2
  • 53
    • 0037334578 scopus 로고    scopus 로고
    • Angiogenesis in hematologic malignancies
    • Moehler T.M., et al. Angiogenesis in hematologic malignancies. Crit. Rev. Oncol. Hematol. 45 (2003) 227-244
    • (2003) Crit. Rev. Oncol. Hematol. , vol.45 , pp. 227-244
    • Moehler, T.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.