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Volumn 123, Issue 21, 2014, Pages 3269-3276

MLN4924, an NAE inhibitor, suppresses AKT and mTOR signaling via upregulation of REDD1 in human myeloma cells

Author keywords

[No Author keywords available]

Indexed keywords

BORTEZOMIB; INTERLEUKIN 6; MAMMALIAN TARGET OF RAPAMYCIN; NEDD8 PROTEIN; PEVONEDISTAT; PROTEIN; PROTEIN KINASE B; REDD1 PROTEIN; SOMATOMEDIN C; UNCLASSIFIED DRUG;

EID: 84903218645     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2013-08-521914     Document Type: Article
Times cited : (68)

References (32)
  • 1
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • DOI 10.1146/annurev.biochem.73.011303.074118
    • Johnson ES. Protein modification by SUMO. Annu Rev Biochem. 2004;73:355-382. (Pubitemid 39050373)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 2
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol. 2006;22:159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 3
    • 84868232791 scopus 로고    scopus 로고
    • Ceramide glycosylation by glucosylceramide synthase selectively maintains the properties of breast cancer stem cells
    • Gupta V, Bhinge KN, Hosain SB, et al. Ceramide glycosylation by glucosylceramide synthase selectively maintains the properties of breast cancer stem cells. J Biol Chem. 2012;287(44):37195-37205.
    • (2012) J Biol Chem , vol.287 , Issue.44 , pp. 37195-37205
    • Gupta, V.1    Bhinge, K.N.2    Hosain, S.B.3
  • 4
    • 84863587306 scopus 로고    scopus 로고
    • Regulation of RAS oncogenicity by acetylation
    • Yang MH, Nickerson S, Kim ET, et al. Regulation of RAS oncogenicity by acetylation. Proc Natl Acad Sci U S A. 2012;109(27):10843-10848.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.27 , pp. 10843-10848
    • Yang, M.H.1    Nickerson, S.2    Kim, E.T.3
  • 5
    • 84876434253 scopus 로고    scopus 로고
    • Regulation of c-Myc ubiquitination controls chronic myelogenous leukemia initiation and progression
    • Reavie L, Buckley SM, Loizou E, et al. Regulation of c-Myc ubiquitination controls chronic myelogenous leukemia initiation and progression. Cancer Cell. 2013;23(3):362-375.
    • (2013) Cancer Cell , vol.23 , Issue.3 , pp. 362-375
    • Reavie, L.1    Buckley, S.M.2    Loizou, E.3
  • 6
    • 84858127817 scopus 로고    scopus 로고
    • Emerging regulatory mechanisms in ubiquitin-dependent cell cycle control
    • Mocciaro A, Rape M. Emerging regulatory mechanisms in ubiquitin-dependent cell cycle control. J Cell Sci. 2012;125(Pt 2):255-263.
    • (2012) J Cell Sci , vol.125 , Issue.PART 2 , pp. 255-263
    • Mocciaro, A.1    Rape, M.2
  • 7
    • 84865415118 scopus 로고    scopus 로고
    • Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A
    • Pulvino M, Liang Y, Oleksyn D, et al. Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A. Blood. 2012;120(8):1668-1677.
    • (2012) Blood , vol.120 , Issue.8 , pp. 1668-1677
    • Pulvino, M.1    Liang, Y.2    Oleksyn, D.3
  • 8
    • 0027171066 scopus 로고
    • Ubiquitin pathway involvement in human lymphocyte gamma-irradiation- induced apoptosis
    • Delic J, Morange M, Magdelenat H. Ubiquitin pathway involvement in human lymphocyte gamma-irradiation-induced apoptosis. Mol Cell Biol. 1993;13(8):4875-4883. (Pubitemid 23220393)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.8 , pp. 4875-4883
    • Delic, J.1    Morange, M.2    Magdelenat, H.3
  • 9
    • 84876063227 scopus 로고    scopus 로고
    • Candidate tumor suppressor BTG3 maintains genomic stability by promoting Lys63-linked ubiquitination and activation of the checkpoint kinase CHK1
    • Cheng YC, Lin TY, Shieh SY. Candidate tumor suppressor BTG3 maintains genomic stability by promoting Lys63-linked ubiquitination and activation of the checkpoint kinase CHK1. Proc Natl Acad Sci U S A. 2013;110(15):5993-5998.
    • (2013) Proc Natl Acad Sci U S a , vol.110 , Issue.15 , pp. 5993-5998
    • Cheng, Y.C.1    Lin, T.Y.2    Shieh, S.Y.3
  • 10
    • 84878736561 scopus 로고    scopus 로고
    • NF-κB inhibits osteogenic differentiation of mesenchymal stem cells by promoting b-catenin degradation
    • Chang J, Liu F, Lee M, et al. NF-κB inhibits osteogenic differentiation of mesenchymal stem cells by promoting b-catenin degradation. Proc Natl Acad Sci U S A. 2013;110(23):9469-9474.
    • (2013) Proc Natl Acad Sci U S a , vol.110 , Issue.23 , pp. 9469-9474
    • Chang, J.1    Liu, F.2    Lee, M.3
  • 11
    • 84880573790 scopus 로고    scopus 로고
    • Proteasomal regulation of caspase-8 in cancer cell apoptosis
    • Fiandalo MV, Schwarze SR, Kyprianou N. Proteasomal regulation of caspase-8 in cancer cell apoptosis. Apoptosis. 2013;18(6):766-776.
    • (2013) Apoptosis , vol.18 , Issue.6 , pp. 766-776
    • Fiandalo, M.V.1    Schwarze, S.R.2    Kyprianou, N.3
  • 12
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, et al. An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature. 2009;458(7239):732-736.
    • (2009) Nature , vol.458 , Issue.7239 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3
  • 13
    • 73649110303 scopus 로고    scopus 로고
    • Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: The NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ
    • Brownell JE, Sintchak MD, Gavin JM, et al. Substrate-assisted inhibition of ubiquitin-like protein-activating enzymes: the NEDD8 E1 inhibitor MLN4924 forms a NEDD8-AMP mimetic in situ. Mol Cell. 2010;37(1):102-111.
    • (2010) Mol Cell , vol.37 , Issue.1 , pp. 102-111
    • Brownell, J.E.1    Sintchak, M.D.2    Gavin, J.M.3
  • 14
    • 79954611863 scopus 로고    scopus 로고
    • Inhibition of NEDD8-activating enzyme induces rereplication and apoptosis in human tumor cells consistent with deregulating CDT1 turnover
    • Milhollen MA, Narayanan U, Soucy TA, Veiby PO, Smith PG, Amidon B. Inhibition of NEDD8-activating enzyme induces rereplication and apoptosis in human tumor cells consistent with deregulating CDT1 turnover. Cancer Res. 2011;71(8):3042-3051.
    • (2011) Cancer Res , vol.71 , Issue.8 , pp. 3042-3051
    • Milhollen, M.A.1    Narayanan, U.2    Soucy, T.A.3    Veiby, P.O.4    Smith, P.G.5    Amidon, B.6
  • 15
    • 78650355357 scopus 로고    scopus 로고
    • NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells
    • Lin JJ, Milhollen MA, Smith PG, Narayanan U, Dutta A. NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells. Cancer Res. 2010;70(24):10310-10320.
    • (2010) Cancer Res , vol.70 , Issue.24 , pp. 10310-10320
    • Lin, J.J.1    Milhollen, M.A.2    Smith, P.G.3    Narayanan, U.4    Dutta, A.5
  • 16
    • 79958165085 scopus 로고    scopus 로고
    • Induction of p21-dependent senescence by an NAE inhibitor, MLN4924, as a mechanism of growth suppression
    • Jia L, Li H, Sun Y. Induction of p21-dependent senescence by an NAE inhibitor, MLN4924, as a mechanism of growth suppression. Neoplasia. 2011;13(6):561-569.
    • (2011) Neoplasia , vol.13 , Issue.6 , pp. 561-569
    • Jia, L.1    Li, H.2    Sun, Y.3
  • 17
    • 84863568271 scopus 로고    scopus 로고
    • The Nedd8-activating enzyme inhibitor MLN4924 induces autophagy and apoptosis to suppress liver cancer cell growth
    • Luo Z, Yu G, Lee HW, et al. The Nedd8-activating enzyme inhibitor MLN4924 induces autophagy and apoptosis to suppress liver cancer cell growth. Cancer Res. 2012;72(13):3360-3371.
    • (2012) Cancer Res , vol.72 , Issue.13 , pp. 3360-3371
    • Luo, Z.1    Yu, G.2    Lee, H.W.3
  • 18
    • 84872199770 scopus 로고    scopus 로고
    • Neddylation pathway regulates T-cell function by targeting an adaptor protein Shc and a protein kinase Erk signaling
    • Jin HS, Liao L, Park Y, Liu YC. Neddylation pathway regulates T-cell function by targeting an adaptor protein Shc and a protein kinase Erk signaling. Proc Natl Acad Sci U S A. 2013;110(2):624-629.
    • (2013) Proc Natl Acad Sci U S a , vol.110 , Issue.2 , pp. 624-629
    • Jin, H.S.1    Liao, L.2    Park, Y.3    Liu, Y.C.4
  • 19
    • 84255192100 scopus 로고    scopus 로고
    • Targeting PI3K/mTOR signaling in cancer
    • Emerling BM, Akcakanat A. Targeting PI3K/mTOR signaling in cancer. Cancer Res. 2011;71(24):7351-7359.
    • (2011) Cancer Res , vol.71 , Issue.24 , pp. 7351-7359
    • Emerling, B.M.1    Akcakanat, A.2
  • 20
    • 84869097627 scopus 로고    scopus 로고
    • Proteasome inhibition leads to dephosphorylation and downregulation of protein expression of members of the Akt/mTOR pathway in MCL
    • Hutter G, Zimmermann Y, Rieken M, et al. Proteasome inhibition leads to dephosphorylation and downregulation of protein expression of members of the Akt/mTOR pathway in MCL. Leukemia. 2012;26(11):2442-2444.
    • (2012) Leukemia , vol.26 , Issue.11 , pp. 2442-2444
    • Hutter, G.1    Zimmermann, Y.2    Rieken, M.3
  • 22
    • 33746736820 scopus 로고    scopus 로고
    • 8-Chloro-adenosine inhibits growth at least partly by interfering with actin polymerization in cultured human lung cancer cells
    • Gu YY, Zhang HY, Zhang HJ, Li SY, Ni JH, Jia HT. 8-Chloro-adenosine inhibits growth at least partly by interfering with actin polymerization in cultured human lung cancer cells. Biochem Pharmacol. 2006;72(5):541-550.
    • (2006) Biochem Pharmacol , vol.72 , Issue.5 , pp. 541-550
    • Gu, Y.Y.1    Zhang, H.Y.2    Zhang, H.J.3    Li, S.Y.4    Ni, J.H.5    Jia, H.T.6
  • 24
    • 68249104457 scopus 로고    scopus 로고
    • REDD1, an inhibitor of mTOR signalling, is regulated by the CUL4A-DDB1 ubiquitin ligase
    • Katiyar S, Liu E, Knutzen CA, et al. REDD1, an inhibitor of mTOR signalling, is regulated by the CUL4A-DDB1 ubiquitin ligase. EMBO Rep. 2009;10(8):866-872.
    • (2009) EMBO Rep , vol.10 , Issue.8 , pp. 866-872
    • Katiyar, S.1    Liu, E.2    Knutzen, C.A.3
  • 25
    • 0037179847 scopus 로고    scopus 로고
    • Role of the phosphatidylinositol 3-kinase/Akt and mTOR/P70S6-kinase pathways in the proliferation and apoptosis in multiple myeloma
    • DOI 10.1038/sj.onc.1205923
    • Pene F, Claessens YE, Muller O, et al. Role of the phosphatidylinositol 3-kinase/Akt and mTOR/P70S6-kinase pathways in the proliferation and apoptosis in multiple myeloma. Oncogene. 2002;21(43):6587-6597. (Pubitemid 35177037)
    • (2002) Oncogene , vol.21 , Issue.43 , pp. 6587-6597
    • Pene, F.1    Claessens, Y.-E.2    Muller, O.3    Viguie, F.4    Mayeux, P.5    Dreyfus, F.6    Lacombe, C.7    Bouscary, D.8
  • 26
    • 84866885402 scopus 로고    scopus 로고
    • The PI3K/Akt/mTOR signaling pathway mediates insulin-like growth factor 1-induced E-cadherin down-regulation and cell proliferation in ovarian cancer cells
    • Lau MT, Leung PC. The PI3K/Akt/mTOR signaling pathway mediates insulin-like growth factor 1-induced E-cadherin down-regulation and cell proliferation in ovarian cancer cells. Cancer Lett. 2012;326(2):191-198.
    • (2012) Cancer Lett , vol.326 , Issue.2 , pp. 191-198
    • Lau, M.T.1    Leung, P.C.2
  • 27
    • 78049434915 scopus 로고    scopus 로고
    • Mammalian target of rapamycin activation underlies HSC defects in autoimmune disease and inflammation in mice
    • Chen C, Liu Y, Liu Y, Zheng P. Mammalian target of rapamycin activation underlies HSC defects in autoimmune disease and inflammation in mice. J Clin Invest. 2010;120(11):4091-4101.
    • (2010) J Clin Invest , vol.120 , Issue.11 , pp. 4091-4101
    • Chen, C.1    Liu, Y.2    Liu, Y.3    Zheng, P.4
  • 28
    • 78650943298 scopus 로고    scopus 로고
    • ERK1/2 phosphorylate Raptor to promote Ras-dependent activation of mTOR complex 1 (mTORC1)
    • Carriere A, Romeo Y, Acosta-Jaquez HA, et al. ERK1/2 phosphorylate Raptor to promote Ras-dependent activation of mTOR complex 1 (mTORC1). J Biol Chem. 2011;286(1):567-577.
    • (2011) J Biol Chem , vol.286 , Issue.1 , pp. 567-577
    • Carriere, A.1    Romeo, Y.2    Acosta-Jaquez, H.A.3
  • 29
    • 84862637714 scopus 로고    scopus 로고
    • Molecular and cellular effects of NEDD8-activating enzyme inhibition in myeloma
    • McMillin DW, Jacobs HM, Delmore JE, et al. Molecular and cellular effects of NEDD8-activating enzyme inhibition in myeloma. Mol Cancer Ther. 2012;11(4):942-951.
    • (2012) Mol Cancer Ther , vol.11 , Issue.4 , pp. 942-951
    • McMillin, D.W.1    Jacobs, H.M.2    Delmore, J.E.3
  • 30
    • 58149395816 scopus 로고    scopus 로고
    • RTP801 is induced in Parkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation
    • Malagelada C, Jin ZH, Greene LA. RTP801 is induced in Parkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation. J Neurosci. 2008;28(53):14363-14371.
    • (2008) J Neurosci , vol.28 , Issue.53 , pp. 14363-14371
    • Malagelada, C.1    Jin, Z.H.2    Greene, L.A.3
  • 31
    • 77952724361 scopus 로고    scopus 로고
    • Downregulation of Akt/mammalian target of rapamycin pathway in skeletal muscle is associated with increased REDD1 expression in response to chronic hypoxia
    • Favier FB, Costes F, Defour A, et al. Downregulation of Akt/mammalian target of rapamycin pathway in skeletal muscle is associated with increased REDD1 expression in response to chronic hypoxia. Am J Physiol Regul Integr Comp Physiol. 2010;298(6):R1659-R1666.
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.298 , Issue.6
    • Favier, F.B.1    Costes, F.2    Defour, A.3
  • 32
    • 65649154116 scopus 로고    scopus 로고
    • Myeloma cells exhibit an increase in proteasome activity and an enhanced response to proteasome inhibition in the bone marrow microenvironment in vivo
    • Edwards CM, Lwin ST, Fowler JA, et al. Myeloma cells exhibit an increase in proteasome activity and an enhanced response to proteasome inhibition in the bone marrow microenvironment in vivo. Am J Hematol. 2009;84(5):268-272.
    • (2009) Am J Hematol , vol.84 , Issue.5 , pp. 268-272
    • Edwards, C.M.1    Lwin, S.T.2    Fowler, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.