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Volumn 44, Issue 1, 2012, Pages 132-138

Differential regulation of PML-RARα stability by the ubiquitin ligases SIAH1/SIAH2 and TRIAD1

Author keywords

PML RAR ; Proteasomal degradation; SIAH; TRIAD1; UBCH8; Ubiquitinylating enzymes

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN BETA; CD11B ANTIGEN; MESSENGER RNA; ONCOPROTEIN; PROMYELOCYTIC LEUKEMIA RETINOIC ACID RECEPTOR ALPHA FUSION PROTEIN; SEVEN IN ABSENTIA HOMOLOG 1; SEVEN IN ABSENTIA HOMOLOG 2; TWO RING FINGERS AND DOUBLE RING FINGER LINKED 1 UBIQUITIN LIGASE; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME 8; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 83555176243     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2011.10.008     Document Type: Article
Times cited : (20)

References (51)
  • 4
    • 66149154321 scopus 로고    scopus 로고
    • The PRC1 Polycomb group complex interacts with PLZF/RARA to mediate leukemic transformation
    • H. Boukarabila, A.J. Saurin, E. Batsche, N. Mossadegh, M. van Lohuizen, and A.P. Otte The PRC1 Polycomb group complex interacts with PLZF/RARA to mediate leukemic transformation Genes Dev 23 2009 1195 1206
    • (2009) Genes Dev , vol.23 , pp. 1195-1206
    • Boukarabila, H.1    Saurin, A.J.2    Batsche, E.3    Mossadegh, N.4    Van Lohuizen, M.5    Otte, A.P.6
  • 5
    • 63849220435 scopus 로고    scopus 로고
    • PML nuclear bodies in the pathogenesis of acute promyelocytic leukemia: Active players or innocent bystanders?
    • N.J. Brown, M. Ramalho, E.W. Pedersen, E. Moravcsik, E. Solomon, and D. Grimwade PML nuclear bodies in the pathogenesis of acute promyelocytic leukemia: active players or innocent bystanders? Front Biosci 14 2009 1684 1707
    • (2009) Front Biosci , vol.14 , pp. 1684-1707
    • Brown, N.J.1    Ramalho, M.2    Pedersen, E.W.3    Moravcsik, E.4    Solomon, E.5    Grimwade, D.6
  • 7
    • 77955709330 scopus 로고    scopus 로고
    • Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation
    • M. Buchwald, K. Pietschmann, J.P. Müller, F.D. Böhmer, T. Heinzel, and O.H. Krämer Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation Leukemia 24 2010 1412 1421
    • (2010) Leukemia , vol.24 , pp. 1412-1421
    • Buchwald, M.1    Pietschmann, K.2    Müller, J.P.3    Böhmer, F.D.4    Heinzel, T.5    Krämer, O.H.6
  • 8
    • 66749092056 scopus 로고    scopus 로고
    • From top to bottom: The two faces of HIPK2 for regulation of the hypoxic response
    • M.A. Calzado, L. De La Vega, E. Munoz, and M.L. Schmitz From top to bottom: the two faces of HIPK2 for regulation of the hypoxic response Cell Cycle 8 2009 1659 1664
    • (2009) Cell Cycle , vol.8 , pp. 1659-1664
    • Calzado, M.A.1    De La Vega, L.2    Munoz, E.3    Schmitz, M.L.4
  • 9
    • 2442643942 scopus 로고    scopus 로고
    • Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors
    • DOI 10.1038/ni1066
    • T.H. Chuang, and R.J. Ulevitch Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors Nat Immunol 5 2004 495 502 (Pubitemid 38660461)
    • (2004) Nature Immunology , vol.5 , Issue.5 , pp. 495-502
    • Chuang, T.-H.1    Ulevitch, R.J.2
  • 10
    • 42649105840 scopus 로고    scopus 로고
    • Proteasome inhibitors: A therapeutic strategy for haematological malignancy
    • DOI 10.2741/3005
    • L.J. Crawford, B. Walker, and A.E. Irvine Proteasome inhibitors: a therapeutic strategy for haematological malignancy Front Biosci 13 2008 4285 4296 (Pubitemid 351599684)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.11 , pp. 4285-4296
    • Crawford, L.J.-A.1    Walker, B.2    Irvine, A.E.3
  • 14
    • 0242389807 scopus 로고    scopus 로고
    • C/EBPβ: A major PML-RARA-responsive gene in retinoic acid-induced differentiation of APL cells
    • DOI 10.1093/emboj/cdg556
    • E. Duprez, K. Wagner, H. Koch, and D.G. Tenen C/EBPbeta: a major PML-RARA-responsive gene in retinoic acid-induced differentiation of APL cells EMBO J 22 2003 5806 5816 (Pubitemid 37408819)
    • (2003) EMBO Journal , vol.22 , Issue.21 , pp. 5806-5816
    • Duprez, E.1    Wagner, K.2    Koch, H.3    Tenen, D.G.4
  • 15
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • DOI 10.1016/0092-8674(94)90340-9
    • J.A. Dyck, G.G. Maul, W.H. Miller Jr., J.D. Chen, A. Kakizuka, and R.M. Evans A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein Cell 76 1994 333 343 (Pubitemid 24046695)
    • (1994) Cell , vol.76 , Issue.2 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 17
    • 1242272073 scopus 로고    scopus 로고
    • The Coiled-coil Domain Is the Structural Determinant for Mammalian Homologues of Drosophila Sina-mediated Degradation of Promyelocytic Leukemia Protein and Other Tripartite Motif Proteins by the Proteasome
    • DOI 10.1074/jbc.M306407200
    • M. Fanelli, A. Fantozzi, P. De Luca, S. Caprodossi, S. Matsuzawa, and M.A. Lazar The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome J Biol Chem 279 2004 5374 5379 (Pubitemid 38220559)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5374-5379
    • Fanelli, M.1    Fantozzi, A.2    De Luca, P.3    Caprodossi, S.4    Matsuzawa, S.-I.5    Lazar, M.A.6    Giuseppe Pelicci, P.7    Minucci, S.8
  • 18
    • 33845926057 scopus 로고    scopus 로고
    • Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding
    • DOI 10.1074/jbc.M604019200
    • C. Fearns, Q. Pan, J.C. Mathison, and T.H. Chuang Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding J Biol Chem 281 2006 34592 34600 (Pubitemid 46036665)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34592-34600
    • Fearns, C.1    Pan, Q.2    Mathison, J.C.3    Chuang, T.-H.4
  • 20
    • 45449087921 scopus 로고    scopus 로고
    • QBase relative quantification framework and software for management and automated analysis of real-time quantitative PCR data
    • J. Hellemans, G. Mortier, A. De Paepe, F. Speleman, and J. Vandesompele qBase relative quantification framework and software for management and automated analysis of real-time quantitative PCR data Genome Biol 8 2007 R19
    • (2007) Genome Biol , vol.8 , pp. 19
    • Hellemans, J.1    Mortier, G.2    De Paepe, A.3    Speleman, F.4    Vandesompele, J.5
  • 21
    • 38949189642 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteasomal degradation in normal and malignant hematopoiesis
    • DOI 10.1016/j.bcmd.2007.07.011, PII S1079979607001751
    • M.L. Heuzé, I. Lamsoul, C. Moog-Lutz, and P.G. Lutz Ubiquitin-mediated proteasomal degradation in normal and malignant hematopoiesis Blood Cells Mol Dis 40 2008 200 210 (Pubitemid 351221377)
    • (2008) Blood Cells, Molecules, and Diseases , vol.40 , Issue.2 , pp. 200-210
    • Heuze, M.L.1    Lamsoul, I.2    Moog-Lutz, C.3    Lutz, P.G.4
  • 22
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • M. Hochstrasser Origin and function of ubiquitin-like proteins Nature 458 2009 422 429
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 23
    • 71549155940 scopus 로고    scopus 로고
    • Siah proteins: Novel drug targets in the Ras and hypoxia pathways
    • C.M. House, A. Moller, and D.D. Bowtell Siah proteins: novel drug targets in the Ras and hypoxia pathways Cancer Res 69 2009 8835 8838
    • (2009) Cancer Res , vol.69 , pp. 8835-8838
    • House, C.M.1    Moller, A.2    Bowtell, D.D.3
  • 24
    • 0032933351 scopus 로고    scopus 로고
    • Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins
    • G. Hu, and E.R. Fearon Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins Mol Cell Biol 19 1999 724 732 (Pubitemid 29018473)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 724-732
    • Hu, G.1    Fearon, E.R.2
  • 25
    • 31444447978 scopus 로고    scopus 로고
    • The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis
    • DOI 10.1016/j.febslet.2005.09.105, PII S0014579306000536
    • J. Huang, L.G. Xu, T. Liu, Z. Zhai, and H.B. Shu The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis FEBS Lett 580 2006 940 947 (Pubitemid 43152318)
    • (2006) FEBS Letters , vol.580 , Issue.3 , pp. 940-947
    • Huang, J.1    Xu, L.-G.2    Liu, T.3    Zhai, Z.4    Shu, H.-B.5
  • 26
    • 79551625633 scopus 로고    scopus 로고
    • Ubiquitin networks in cancer
    • V. Kirkin, and I. Dikic Ubiquitin networks in cancer Curr Opin Genet Dev 21 2011 21 28
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 21-28
    • Kirkin, V.1    Dikic, I.2
  • 27
    • 34548084157 scopus 로고    scopus 로고
    • The survivin isoform survivin-3B is cytoprotective and can function as a chromosomal passenger complex protein
    • S.K. Knauer, C. Bier, P. Schlag, J. Fritzmann, W. Dietmaier, and F. Rodel The survivin isoform survivin-3B is cytoprotective and can function as a chromosomal passenger complex protein Cell Cycle 6 2007 1502 1509
    • (2007) Cell Cycle , vol.6 , pp. 1502-1509
    • Knauer, S.K.1    Bier, C.2    Schlag, P.3    Fritzmann, J.4    Dietmaier, W.5    Rodel, F.6
  • 29
    • 43249104204 scopus 로고    scopus 로고
    • Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARα
    • DOI 10.1096/fj.06-8050com
    • O.H. Krämer, S. Müller, M. Buchwald, S. Reichardt, and T. Heinzel Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARalpha FASEB J 22 2008 1369 1379 (Pubitemid 351656778)
    • (2008) FASEB Journal , vol.22 , Issue.5 , pp. 1369-1379
    • Kramer, O.H.1    Muller, S.2    Buchwald, M.3    Reichardt, S.4    Heinzel, T.5
  • 32
    • 33747586073 scopus 로고    scopus 로고
    • Ubiquitylation in normal and malignant hematopoiesis: Novel therapeutic targets
    • DOI 10.1038/sj.leu.2404319, PII 2404319
    • J.A. Marteijn, J.H. Jansen, and B.A. van der Reijden Ubiquitylation in normal and malignant hematopoiesis: novel therapeutic targets Leukemia 20 2006 1511 1518 (Pubitemid 44264092)
    • (2006) Leukemia , vol.20 , Issue.9 , pp. 1511-1518
    • Marteijn, J.A.F.1    Jansen, J.H.2    Van Der Reijden, B.A.3
  • 33
    • 68749093885 scopus 로고    scopus 로고
    • The ubiquitin ligase TRIAD1 inhibits myelopoiesis through UBCH7 and UBC13 interacting domains
    • J.A. Marteijn, L.T. van der Meer, J.J. Smit, S.M. Noordermeer, W. Wissink, and P. Jansen The ubiquitin ligase TRIAD1 inhibits myelopoiesis through UBCH7 and UBC13 interacting domains Leukemia 23 2009 1480 1489
    • (2009) Leukemia , vol.23 , pp. 1480-1489
    • Marteijn, J.A.1    Van Der Meer, L.T.2    Smit, J.J.3    Noordermeer, S.M.4    Wissink, W.5    Jansen, P.6
  • 36
    • 77952853306 scopus 로고    scopus 로고
    • Histone deacetylases and epigenetic therapies of hematological malignancies
    • C. Mercurio, S. Minucci, and P.G. Pelicci Histone deacetylases and epigenetic therapies of hematological malignancies Pharmacol Res 2010
    • (2010) Pharmacol Res
    • Mercurio, C.1    Minucci, S.2    Pelicci, P.G.3
  • 37
    • 11144322855 scopus 로고    scopus 로고
    • The zinc finger transcription factor Growth factor independence 1 (Gfi1)
    • DOI 10.1016/j.biocel.2004.08.011, PII S1357272504003498
    • T. Möröy The zinc finger transcription factor growth factor independence 1 (GFI1) Int J Biochem Cell Biol 37 2005 541 546 (Pubitemid 40022931)
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , Issue.3 , pp. 541-546
    • Moroy, T.1
  • 38
    • 0032718068 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzymes UBCH7 and UBCH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1
    • T.P. Moynihan, H.C. Ardley, U. Nuber, S.A. Rose, P.F. Jones, and A.F. Markham The ubiquitin-conjugating enzymes UBCH7 and UBCH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1 J Biol Chem 274 1999 30963 30968
    • (1999) J Biol Chem , vol.274 , pp. 30963-30968
    • Moynihan, T.P.1    Ardley, H.C.2    Nuber, U.3    Rose, S.A.4    Jones, P.F.5    Markham, A.F.6
  • 39
    • 77950640292 scopus 로고    scopus 로고
    • Inhibitors of HDACs - Effective drugs against cancer?
    • S. Müller, and O.H. Krämer Inhibitors of HDACs - effective drugs against cancer? Curr Cancer Drug Targets 10 2010 210 228
    • (2010) Curr Cancer Drug Targets , vol.10 , pp. 210-228
    • Müller, S.1    Krämer, O.H.2
  • 40
    • 79960432723 scopus 로고    scopus 로고
    • Herpes simplex virus immediate-early protein ICP0 is targeted by SIAH-1 for proteasomal degradation
    • C.H. Nagel, N. Albrecht, K. Milovic-Holm, L. Mariyanna, B. Keyser, and B. Abel Herpes simplex virus immediate-early protein ICP0 is targeted by SIAH-1 for proteasomal degradation J Virol 85 2011 7644 7657
    • (2011) J Virol , vol.85 , pp. 7644-7657
    • Nagel, C.H.1    Albrecht, N.2    Milovic-Holm, K.3    Mariyanna, L.4    Keyser, B.5    Abel, B.6
  • 41
    • 34548079498 scopus 로고    scopus 로고
    • Therapeutic targeting of nuclear receptor corepressor misfolding in acute promyelocytic leukemia cells with genistein
    • DOI 10.1158/1535-7163.MCT-06-0705
    • A.P. Ng, D.S. Nin, J.H. Fong, D. Venkataraman, C.S. Chen, and M. Khan Therapeutic targeting of nuclear receptor corepressor misfolding in acute promyelocytic leukemia cells with genistein Mol Cancer Ther 6 2007 2240 2248 (Pubitemid 47294752)
    • (2007) Molecular Cancer Therapeutics , vol.6 , Issue.8 , pp. 2240-2248
    • Ng, A.P.P.1    Nin, D.S.2    Fong, J.H.3    Venkataraman, D.4    Chen, C.-S.5    Khan, M.6
  • 43
    • 75649135910 scopus 로고    scopus 로고
    • Deconstructing repression: Evolving models of co-repressor action
    • V. Perissi, K. Jepsen, C.K. Glass, and M.G. Rosenfeld Deconstructing repression: evolving models of co-repressor action Nat Rev Genet 11 2010 109 123
    • (2010) Nat Rev Genet , vol.11 , pp. 109-123
    • Perissi, V.1    Jepsen, K.2    Glass, C.K.3    Rosenfeld, M.G.4
  • 45
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • S. Spange, T. Wagner, T. Heinzel, and O.H. Krämer Acetylation of non-histone proteins modulates cellular signalling at multiple levels Int J Biochem Cell Biol 41 2009 185 198
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Krämer, O.H.4
  • 47
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • J. Vandesompele, K. De Preter, F. Pattyn, B. Poppe, N. Van Roy, and A. De Paepe Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes Genome Biol 3 2002 RESEARCH0034
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6
  • 48
    • 79955772246 scopus 로고    scopus 로고
    • HoxA10 influences protein ubiquitination by activating transcription of ARIH2 - The gene encoding TRIAD1
    • H. Wang, L. Bei, C.A. Shah, E. Horvath, and E.A. Eklund HoxA10 influences protein ubiquitination by activating transcription of ARIH2 - the gene encoding TRIAD1 J Biol Chem 286 2011 16832 16845
    • (2011) J Biol Chem , vol.286 , pp. 16832-16845
    • Wang, H.1    Bei, L.2    Shah, C.A.3    Horvath, E.4    Eklund, E.A.5
  • 49
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells
    • DOI 10.1016/0092-8674(94)90341-7
    • K. Weis, S. Rambaud, C. Lavau, J. Jansen, T. Carvalho, and M. Carmo-Fonseca Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells Cell 76 1994 345 356 (Pubitemid 24046696)
    • (1994) Cell , vol.76 , Issue.2 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejeant, A.8
  • 51
    • 80053234975 scopus 로고    scopus 로고
    • E3 ubiquitin ligase SIAH-1 facilitates poly-ubiquitylation and proteasomal degradation of the hepatitis B viral X protein
    • J. Zhao, C. Wang, J. Wang, X. Yang, N. Diao, and Q. Li E3 ubiquitin ligase SIAH-1 facilitates poly-ubiquitylation and proteasomal degradation of the hepatitis B viral X protein FEBS Lett 2011
    • (2011) FEBS Lett
    • Zhao, J.1    Wang, C.2    Wang, J.3    Yang, X.4    Diao, N.5    Li, Q.6


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