메뉴 건너뛰기




Volumn 142, Issue 3, 2012, Pages 572-581

β-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells

Author keywords

Colorectal Cancer; PML; TCF4; Wnt Signaling

Indexed keywords

BETA CATENIN; NUCLEAR PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN 4; RAN BINDING PROTEIN 2; SUMO PROTEIN; UNCLASSIFIED DRUG;

EID: 84857574310     PISSN: 00165085     EISSN: 15280012     Source Type: Journal    
DOI: 10.1053/j.gastro.2011.11.041     Document Type: Article
Times cited : (31)

References (47)
  • 1
    • 0030592517 scopus 로고    scopus 로고
    • Lessons from hereditary colorectal cancer
    • K.W. Kinzler, B. Vogelstein Lessons from hereditary colorectal cancer Cell 87 1996 159 170
    • (1996) Cell , vol.87 , pp. 159-170
    • Kinzler, K.W.1    Vogelstein, B.2
  • 2
    • 0030949463 scopus 로고    scopus 로고
    • Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC
    • P.J. Morin, A.B. Sparks, V. Korinek Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC Science 275 1997 1787 1790
    • (1997) Science , vol.275 , pp. 1787-1790
    • Morin, P.J.1    Sparks, A.B.2    Korinek, V.3
  • 3
    • 0032521433 scopus 로고    scopus 로고
    • Mutational analysis of the APC/beta-catenin/Tcf pathway in colorectal cancer
    • A.B. Sparks, P.J. Morin, B. Vogelstein Mutational analysis of the APC/beta-catenin/Tcf pathway in colorectal cancer Cancer Res 58 1998 1130 1134
    • (1998) Cancer Res , vol.58 , pp. 1130-1134
    • Sparks, A.B.1    Morin, P.J.2    Vogelstein, B.3
  • 4
    • 0033992481 scopus 로고    scopus 로고
    • The yin-yang of TCF/beta-catenin signaling
    • N. Barker, P.J. Morin, H. Clevers The yin-yang of TCF/beta-catenin signaling Adv Cancer Res 77 2000 1 24
    • (2000) Adv Cancer Res , vol.77 , pp. 1-24
    • Barker, N.1    Morin, P.J.2    Clevers, H.3
  • 6
    • 20444503830 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 is a component of the oncogenic T-cell factor-4/beta-catenin complex
    • M. Idogawa, T. Yamada, K. Honda Poly(ADP-ribose) polymerase-1 is a component of the oncogenic T-cell factor-4/beta-catenin complex Gastroenterology 128 2005 1919 1936
    • (2005) Gastroenterology , vol.128 , pp. 1919-1936
    • Idogawa, M.1    Yamada, T.2    Honda, K.3
  • 7
    • 33847011050 scopus 로고    scopus 로고
    • Ku70 and poly(ADP-ribose) polymerase-1 competitively regulate beta-catenin and T-cell factor-4-mediated gene transactivation: Possible linkage of DNA damage recognition and Wnt signaling
    • M. Idogawa, M. Masutani, M. Shitashige Ku70 and poly(ADP-ribose) polymerase-1 competitively regulate beta-catenin and T-cell factor-4-mediated gene transactivation: possible linkage of DNA damage recognition and Wnt signaling Cancer Res 67 2007 911 918
    • (2007) Cancer Res , vol.67 , pp. 911-918
    • Idogawa, M.1    Masutani, M.2    Shitashige, M.3
  • 8
    • 26844516084 scopus 로고    scopus 로고
    • Beta-catenin interacts with the FUS proto-oncogene product and regulates pre-mRNA splicing
    • S. Sato, M. Idogawa, K. Honda beta-catenin interacts with the FUS proto-oncogene product and regulates pre-mRNA splicing Gastroenterology 129 2005 1225 1236
    • (2005) Gastroenterology , vol.129 , pp. 1225-1236
    • Sato, S.1    Idogawa, M.2    Honda, K.3
  • 9
    • 33947302281 scopus 로고    scopus 로고
    • Involvement of splicing factor-1 in beta-catenin/T-cell factor-4-mediated gene transactivation and pre-mRNA splicing
    • M. Shitashige, Y. Naishiro, M. Idogawa Involvement of splicing factor-1 in beta-catenin/T-cell factor-4-mediated gene transactivation and pre-mRNA splicing Gastroenterology 132 2007 1039 1054
    • (2007) Gastroenterology , vol.132 , pp. 1039-1054
    • Shitashige, M.1    Naishiro, Y.2    Idogawa, M.3
  • 10
    • 25444455299 scopus 로고    scopus 로고
    • E-cadherin regulates the association between beta-catenin and actinin-4
    • Y. Hayashida, K. Honda, M. Idogawa E-cadherin regulates the association between beta-catenin and actinin-4 Cancer Res 65 2005 8836 8845
    • (2005) Cancer Res , vol.65 , pp. 8836-8845
    • Hayashida, Y.1    Honda, K.2    Idogawa, M.3
  • 11
    • 44649099646 scopus 로고    scopus 로고
    • Regulation of Wnt signaling by the nuclear pore complex
    • 1971 e14
    • M. Shitashige, R. Satow, K. Honda Regulation of Wnt signaling by the nuclear pore complex Gastroenterology 134 2008 1961 1971 1971 e14
    • (2008) Gastroenterology , vol.134 , pp. 1961-1971
    • Shitashige, M.1    Satow, R.2    Honda, K.3
  • 12
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • A. Kakizuka, W.H. Miller Jr, K. Umesono Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML Cell 66 1991 663 674
    • (1991) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller, Jr.W.H.2    Umesono, K.3
  • 13
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • H. de The, C. Lavau, A. Marchio The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR Cell 66 1991 675 684
    • (1991) Cell , vol.66 , pp. 675-684
    • De The, H.1    Lavau, C.2    Marchio, A.3
  • 14
    • 0000237552 scopus 로고    scopus 로고
    • Role of PML in cell growth and the retinoic acid pathway
    • Z.G. Wang, L. Delva, M. Gaboli Role of PML in cell growth and the retinoic acid pathway Science 279 1998 1547 1551
    • (1998) Science , vol.279 , pp. 1547-1551
    • Wang, Z.G.1    Delva, L.2    Gaboli, M.3
  • 16
    • 0033561797 scopus 로고    scopus 로고
    • Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia
    • A. Melnick, J.D. Licht Deconstructing a disease: RARalpha, its fusion partners, and their roles in the pathogenesis of acute promyelocytic leukemia Blood 93 1999 3167 3215
    • (1999) Blood , vol.93 , pp. 3167-3215
    • Melnick, A.1    Licht, J.D.2
  • 17
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • P. Salomoni, P.P. Pandolfi The role of PML in tumor suppression Cell 108 2002 165 170
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 18
    • 54249103056 scopus 로고    scopus 로고
    • Regulation of apoptosis by PML and the PML-NBs
    • R. Bernardi, A. Papa, P.P. Pandolfi Regulation of apoptosis by PML and the PML-NBs Oncogene 27 2008 6299 6312
    • (2008) Oncogene , vol.27 , pp. 6299-6312
    • Bernardi, R.1    Papa, A.2    Pandolfi, P.P.3
  • 19
    • 44849143636 scopus 로고    scopus 로고
    • New insights into the role of PML in tumour suppression
    • P. Salomoni, B.J. Ferguson, A.H. Wyllie New insights into the role of PML in tumour suppression Cell Res 18 2008 622 640
    • (2008) Cell Res , vol.18 , pp. 622-640
    • Salomoni, P.1    Ferguson, B.J.2    Wyllie, A.H.3
  • 20
    • 0033542424 scopus 로고    scopus 로고
    • Expression and role of PML gene in normal adult hematopoiesis: Functional interaction between PML and Rb proteins in erythropoiesis
    • C. Labbaye, M. Valtieri, F. Grignani Expression and role of PML gene in normal adult hematopoiesis: functional interaction between PML and Rb proteins in erythropoiesis Oncogene 18 1999 3529 3540
    • (1999) Oncogene , vol.18 , pp. 3529-3540
    • Labbaye, C.1    Valtieri, M.2    Grignani, F.3
  • 21
    • 0034306019 scopus 로고    scopus 로고
    • The function of PML in p53-dependent apoptosis
    • A. Guo, P. Salomoni, J. Luo The function of PML in p53-dependent apoptosis Nat Cell Biol 2 2000 730 736
    • (2000) Nat Cell Biol , vol.2 , pp. 730-736
    • Guo, A.1    Salomoni, P.2    Luo, J.3
  • 22
    • 33747488399 scopus 로고    scopus 로고
    • PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR
    • R. Bernardi, I. Guernah, D. Jin PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR Nature 442 2006 779 785
    • (2006) Nature , vol.442 , pp. 779-785
    • Bernardi, R.1    Guernah, I.2    Jin, D.3
  • 23
    • 0031791875 scopus 로고    scopus 로고
    • PML is essential for multiple apoptotic pathways
    • Z.G. Wang, D. Ruggero, S. Ronchetti PML is essential for multiple apoptotic pathways Nat Genet 20 1998 266 272
    • (1998) Nat Genet , vol.20 , pp. 266-272
    • Wang, Z.G.1    Ruggero, D.2    Ronchetti, S.3
  • 24
    • 0035142119 scopus 로고    scopus 로고
    • Analysis of the molecular genetics of acute promyelocytic leukemia in mouse models
    • E.M. Rego, P.P. Pandolfi Analysis of the molecular genetics of acute promyelocytic leukemia in mouse models Semin Hematol 38 2001 54 70
    • (2001) Semin Hematol , vol.38 , pp. 54-70
    • Rego, E.M.1    Pandolfi, P.P.2
  • 25
    • 2442568547 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are disorganized in colorectal tumors with total loss of major histocompatibility complex class i expression and LMP7 downregulation
    • C.M. Cabrera, P. Jimenez, A. Concha Promyelocytic leukemia (PML) nuclear bodies are disorganized in colorectal tumors with total loss of major histocompatibility complex class I expression and LMP7 downregulation Tissue Antigens 63 2004 446 452
    • (2004) Tissue Antigens , vol.63 , pp. 446-452
    • Cabrera, C.M.1    Jimenez, P.2    Concha, A.3
  • 26
    • 1342291118 scopus 로고    scopus 로고
    • Loss of the tumor suppressor PML in human cancers of multiple histologic origins
    • C. Gurrieri, P. Capodieci, R. Bernardi Loss of the tumor suppressor PML in human cancers of multiple histologic origins J Natl Cancer Inst 96 2004 269 279
    • (2004) J Natl Cancer Inst , vol.96 , pp. 269-279
    • Gurrieri, C.1    Capodieci, P.2    Bernardi, R.3
  • 27
    • 11144219997 scopus 로고    scopus 로고
    • Physical and functional link of the leukemia-associated factors AML1 and PML
    • L.A. Nguyen, P.P. Pandolfi, Y. Aikawa Physical and functional link of the leukemia-associated factors AML1 and PML Blood 105 2005 292 300
    • (2005) Blood , vol.105 , pp. 292-300
    • Nguyen, L.A.1    Pandolfi, P.P.2    Aikawa, Y.3
  • 28
    • 77953775569 scopus 로고    scopus 로고
    • Traf2- and Nck-interacting kinase is essential for Wnt signaling and colorectal cancer growth
    • M. Shitashige, R. Satow, T. Jigami Traf2- and Nck-interacting kinase is essential for Wnt signaling and colorectal cancer growth Cancer Res 70 2010 5024 5033
    • (2010) Cancer Res , vol.70 , pp. 5024-5033
    • Shitashige, M.1    Satow, R.2    Jigami, T.3
  • 29
    • 33745728153 scopus 로고    scopus 로고
    • Characterization of endogenous human promyelocytic leukemia isoforms
    • W. Condemine, Y. Takahashi, J. Zhu Characterization of endogenous human promyelocytic leukemia isoforms Cancer Res 66 2006 6192 6198
    • (2006) Cancer Res , vol.66 , pp. 6192-6198
    • Condemine, W.1    Takahashi, Y.2    Zhu, J.3
  • 30
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • K. Jensen, C. Shiels, P.S. Freemont PML protein isoforms and the RBCC/TRIM motif Oncogene 20 2001 7223 7233
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 31
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation
    • E. Duprez, A.J. Saurin, J.M. Desterro SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation J Cell Sci 112 1999 381 393
    • (1999) J Cell Sci , vol.112 , pp. 381-393
    • Duprez, E.1    Saurin, A.J.2    Desterro, J.M.3
  • 32
    • 33750447586 scopus 로고    scopus 로고
    • The mechanisms of PML-nuclear body formation
    • T.H. Shen, H.K. Lin, P.P. Scaglioni The mechanisms of PML-nuclear body formation Mol Cell 24 2006 331 339
    • (2006) Mol Cell , vol.24 , pp. 331-339
    • Shen, T.H.1    Lin, H.K.2    Scaglioni, P.P.3
  • 33
    • 51349091041 scopus 로고    scopus 로고
    • Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body formation
    • C. Gao, C.C. Ho, E. Reineke Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body formation Mol Cell Biol 28 2008 5658 5667
    • (2008) Mol Cell Biol , vol.28 , pp. 5658-5667
    • Gao, C.1    Ho, C.C.2    Reineke, E.3
  • 34
    • 11444271001 scopus 로고    scopus 로고
    • Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection
    • M.H. Tatham, S. Kim, E. Jaffray Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection Nat Struct Mol Biol 12 2005 67 74
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 67-74
    • Tatham, M.H.1    Kim, S.2    Jaffray, E.3
  • 35
    • 33646031179 scopus 로고    scopus 로고
    • In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies
    • N. Saitoh, Y. Uchimura, T. Tachibana In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies Exp Cell Res 312 2006 1418 1430
    • (2006) Exp Cell Res , vol.312 , pp. 1418-1430
    • Saitoh, N.1    Uchimura, Y.2    Tachibana, T.3
  • 37
    • 0343776952 scopus 로고    scopus 로고
    • Role of SUMO-1-modified PML in nuclear body formation
    • S. Zhong, S. Muller, S. Ronchetti Role of SUMO-1-modified PML in nuclear body formation Blood 95 2000 2748 2752
    • (2000) Blood , vol.95 , pp. 2748-2752
    • Zhong, S.1    Muller, S.2    Ronchetti, S.3
  • 38
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of p53 activity in nuclear bodies by a specific PML isoform
    • V. Fogal, M. Gostissa, P. Sandy Regulation of p53 activity in nuclear bodies by a specific PML isoform EMBO J 19 2000 6185 6195
    • (2000) EMBO J , vol.19 , pp. 6185-6195
    • Fogal, V.1    Gostissa, M.2    Sandy, P.3
  • 39
    • 1542676904 scopus 로고    scopus 로고
    • MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53
    • H. Zhu, L. Wu, C.G. Maki MDM2 and promyelocytic leukemia antagonize each other through their direct interaction with p53 J Biol Chem 278 2003 49286 49292
    • (2003) J Biol Chem , vol.278 , pp. 49286-49292
    • Zhu, H.1    Wu, L.2    Maki, C.G.3
  • 40
    • 3242726103 scopus 로고    scopus 로고
    • PML regulates p53 stability by sequestering Mdm2 to the nucleolus
    • R. Bernardi, P.P. Scaglioni, S. Bergmann PML regulates p53 stability by sequestering Mdm2 to the nucleolus Nat Cell Biol 6 2004 665 672
    • (2004) Nat Cell Biol , vol.6 , pp. 665-672
    • Bernardi, R.1    Scaglioni, P.P.2    Bergmann, S.3
  • 41
    • 24644522876 scopus 로고    scopus 로고
    • Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
    • C. Fu, K. Ahmed, H. Ding Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3 Oncogene 24 2005 5401 5413
    • (2005) Oncogene , vol.24 , pp. 5401-5413
    • Fu, C.1    Ahmed, K.2    Ding, H.3
  • 42
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • A.M. Ishov, A.G. Sotnikov, D. Negorev PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1 J Cell Biol 147 1999 221 234
    • (1999) J Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3
  • 43
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • V. Lallemand-Breitenbach, M. Jeanne, S. Benhenda Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway Nat Cell Biol 10 2008 547 555
    • (2008) Nat Cell Biol , vol.10 , pp. 547-555
    • Lallemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3
  • 44
    • 38549132438 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells
    • E.L. Reineke, M. Lam, Q. Liu Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells Mol Cell Biol 28 2008 997 1006
    • (2008) Mol Cell Biol , vol.28 , pp. 997-1006
    • Reineke, E.L.1    Lam, M.2    Liu, Q.3
  • 45
    • 0031848068 scopus 로고    scopus 로고
    • Depletion of epithelial stem-cell compartments in the small intestine of mice lacking Tcf-4
    • V. Korinek, N. Barker, P. Moerer Depletion of epithelial stem-cell compartments in the small intestine of mice lacking Tcf-4 Nat Genet 19 1998 379 383
    • (1998) Nat Genet , vol.19 , pp. 379-383
    • Korinek, V.1    Barker, N.2    Moerer, P.3
  • 46
    • 44349166602 scopus 로고    scopus 로고
    • PML targeting eradicates quiescent leukaemia-initiating cells
    • K. Ito, R. Bernardi, A. Morotti PML targeting eradicates quiescent leukaemia-initiating cells Nature 453 2008 1072 1078
    • (2008) Nature , vol.453 , pp. 1072-1078
    • Ito, K.1    Bernardi, R.2    Morotti, A.3
  • 47
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation
    • V. Lallemand-Breitenbach, J. Zhu, F. Puvion Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation J Exp Med 193 2001 1361 1371
    • (2001) J Exp Med , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.