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Volumn 587, Issue 6, 2013, Pages 607-613

ECHS1 interacts with STAT3 and negatively regulates STAT3 signaling

Author keywords

Enoyl CoA hydratase short chain 1; Phosphorylation regulation; Protein interaction; Signal transducer and activator of transcription 3

Indexed keywords

CELL PROTEIN; CYCLIN D1; ENOYL COENZYME A HYDRATASE; ENOYL COENZYME A HYDRATASE SHORT CHAIN 1; GELATINASE A; PROTEIN BCL 2; PROTEIN BCL 2 L1; STAT3 PROTEIN; UNCLASSIFIED DRUG;

EID: 84875212441     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.02.005     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0028349735 scopus 로고
    • STAT3: A STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
    • Z. Zhong, Z. Wen, and J.E. Darnell Jr. STAT3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6 Science 264 1994 95 98
    • (1994) Science , vol.264 , pp. 95-98
    • Zhong, Z.1    Wen, Z.2    Darnell Jr., J.E.3
  • 3
    • 0036731485 scopus 로고    scopus 로고
    • STATs: Transcriptional control and biological impact
    • D.E. Levy, and J.E. Darnell Jr. STATs: transcriptional control and biological impact Nat. Rev. Mol. Cell Biol. 3 2002 651 662
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 651-662
    • Levy, D.E.1    Darnell Jr., J.E.2
  • 4
    • 0036251154 scopus 로고    scopus 로고
    • STAT proteins and oncogenesis
    • J. Bromberg STAT proteins and oncogenesis J. Clin. Invest. 109 2002 1139 1142
    • (2002) J. Clin. Invest. , vol.109 , pp. 1139-1142
    • Bromberg, J.1
  • 5
    • 1042302005 scopus 로고    scopus 로고
    • The STATs of cancer-new molecular targets come of age
    • H. Yu, and R. Jove The STATs of cancer-new molecular targets come of age Nat. Rev. Cancer 4 2004 97 105
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 97-105
    • Yu, H.1    Jove, R.2
  • 6
    • 11144357779 scopus 로고    scopus 로고
    • Regulation of the innate and adaptive immune responses by STAT-3 signaling in tumor cells
    • T. Wang, G. Niu, M. Kortylewski, L. Burdelya, and K. Shain Regulation of the innate and adaptive immune responses by STAT-3 signaling in tumor cells Nat. Med. 10 2004 48 54
    • (2004) Nat. Med. , vol.10 , pp. 48-54
    • Wang, T.1    Niu, G.2    Kortylewski, M.3    Burdelya, L.4    Shain, K.5
  • 7
    • 0036233585 scopus 로고    scopus 로고
    • Cytokine signaling in 2002: New surprises in the JAK/STAT pathway
    • J.J. O'Shea, M. Gadina, and R.D. Schreiber Cytokine signaling in 2002: new surprises in the JAK/STAT pathway Cell 109 2002 S121 S131
    • (2002) Cell , vol.109
    • O'Shea, J.J.1    Gadina, M.2    Schreiber, R.D.3
  • 8
    • 0036256644 scopus 로고    scopus 로고
    • What does STAT3 do?
    • D.E. Levy, and C.K. Lee What does STAT3 do? J. Clin. Invest. 109 2002 1143 1148
    • (2002) J. Clin. Invest. , vol.109 , pp. 1143-1148
    • Levy, D.E.1    Lee, C.K.2
  • 9
    • 0034658153 scopus 로고    scopus 로고
    • STAT signaling in the pathogenesis and treatment of leukemias
    • T.S. Lin, S. Mahajan, and D.A. Frank STAT signaling in the pathogenesis and treatment of leukemias Oncogene 19 2000 2496 2504
    • (2000) Oncogene , vol.19 , pp. 2496-2504
    • Lin, T.S.1    Mahajan, S.2    Frank, D.A.3
  • 10
    • 80053300050 scopus 로고    scopus 로고
    • Multiplex ligation-dependent probe amplification of conjunctival melanoma reveals common BRAF V600E gene mutation and gene copy number changes
    • S.L. Lake, F. Jmor, J. Dopierala, A.F. Taktak, and S.E. Coupland Multiplex ligation-dependent probe amplification of conjunctival melanoma reveals common BRAF V600E gene mutation and gene copy number changes Invest. Ophthalmol. Vis. Sci. 52 2011 5598 5604
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 5598-5604
    • Lake, S.L.1    Jmor, F.2    Dopierala, J.3    Taktak, A.F.4    Coupland, S.E.5
  • 11
    • 21344456396 scopus 로고    scopus 로고
    • Identification of proteins differentially expressed in the conventional renal cell carcinoma by proteomic analysis
    • J.S. Hwa, H.J. Park, J.H. Jung, S.C. Kam, and H.C. Park Identification of proteins differentially expressed in the conventional renal cell carcinoma by proteomic analysis J. Korean Med. Sci. 20 2005 450 455
    • (2005) J. Korean Med. Sci. , vol.20 , pp. 450-455
    • Hwa, J.S.1    Park, H.J.2    Jung, J.H.3    Kam, S.C.4    Park, H.C.5
  • 12
    • 3042732887 scopus 로고    scopus 로고
    • Proteomic profiling of proteins decreased in hepatocellular carcinoma from patients infected with hepatitis C virus
    • Y. Yokoyama, Y. Kuramitsu, M. Takashima, N. Iizuka, and T. Toda Proteomic profiling of proteins decreased in hepatocellular carcinoma from patients infected with hepatitis C virus Proteomics 4 2004 2111 2116
    • (2004) Proteomics , vol.4 , pp. 2111-2116
    • Yokoyama, Y.1    Kuramitsu, Y.2    Takashima, M.3    Iizuka, N.4    Toda, T.5
  • 13
    • 33750968212 scopus 로고    scopus 로고
    • PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus
    • J.H. Man, H.Y. Li, P.J. Zhang, T. Zhou, and K. He PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus Nucleic Acids Res. 34 2006 5552 5566
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5552-5566
    • Man, J.H.1    Li, H.Y.2    Zhang, P.J.3    Zhou, T.4    He, K.5
  • 14
    • 62649134663 scopus 로고    scopus 로고
    • Induction of SOX4 by DNA damage is critical for p53 stabilization and function
    • X. Pan, J. Zhao, W.N. Zhang, H.Y. Li, and R. Mu Induction of SOX4 by DNA damage is critical for p53 stabilization and function Proc. Natl. Acad. Sci. USA 106 2009 3788 3793
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3788-3793
    • Pan, X.1    Zhao, J.2    Zhang, W.N.3    Li, H.Y.4    Mu, R.5
  • 15
    • 0035905767 scopus 로고    scopus 로고
    • CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling
    • J. Irie-Sasaki, T. Sasaki, W. Matsumoto, A. Opavsky, and M. Cheng CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling Nature 409 2001 349 354
    • (2001) Nature , vol.409 , pp. 349-354
    • Irie-Sasaki, J.1    Sasaki, T.2    Matsumoto, W.3    Opavsky, A.4    Cheng, M.5
  • 17
    • 0030839112 scopus 로고    scopus 로고
    • A new protein containing an SH2 domain that inhibits JAK kinases
    • T.A. Endo, M. Masuhara, M. Yokouchi, R. Suzuki, and H. Sakamoto A new protein containing an SH2 domain that inhibits JAK kinases Nature 387 1997 921 924
    • (1997) Nature , vol.387 , pp. 921-924
    • Endo, T.A.1    Masuhara, M.2    Yokouchi, M.3    Suzuki, R.4    Sakamoto, H.5
  • 18
    • 0030755934 scopus 로고    scopus 로고
    • Structure and function of a new STAT-induced STAT inhibitor
    • T. Naka, M. Narazaki, M. Hirata, T. Matsumoto, and S. Minamoto Structure and function of a new STAT-induced STAT inhibitor Nature 387 1997 924 929
    • (1997) Nature , vol.387 , pp. 924-929
    • Naka, T.1    Narazaki, M.2    Hirata, M.3    Matsumoto, T.4    Minamoto, S.5
  • 19
    • 84855287537 scopus 로고    scopus 로고
    • CUEDC2 (CUE domain-containing 2) and SOCS3 (suppressors of cytokine signaling 3) cooperate to negatively regulate Janus kinase 1/signal transducers and activators of transcription 3 signaling
    • W.N. Zhang, L. Wang, Q. Wang, X. Luo, and D.F. Fang CUEDC2 (CUE domain-containing 2) and SOCS3 (suppressors of cytokine signaling 3) cooperate to negatively regulate Janus kinase 1/signal transducers and activators of transcription 3 signaling J. Biol. Chem. 287 2012 382 392
    • (2012) J. Biol. Chem. , vol.287 , pp. 382-392
    • Zhang, W.N.1    Wang, L.2    Wang, Q.3    Luo, X.4    Fang, D.F.5
  • 20
    • 0030725378 scopus 로고    scopus 로고
    • Specific inhibition of STAT3 signal transduction by PIAS3
    • C.D. Chung, J. Liao, B. Liu, X. Rao, and P. Jay Specific inhibition of STAT3 signal transduction by PIAS3 Science 278 1997 1803 1805
    • (1997) Science , vol.278 , pp. 1803-1805
    • Chung, C.D.1    Liao, J.2    Liu, B.3    Rao, X.4    Jay, P.5
  • 21
    • 0037451235 scopus 로고    scopus 로고
    • GRIM-19, a death-regulatory gene product, suppresses STAT3 activity via functional interaction
    • C. Lufei, J. Ma, G. Huang, T. Zhang, and V. Novotny-Diermayr GRIM-19, a death-regulatory gene product, suppresses STAT3 activity via functional interaction EMBO J. 22 2003 1325 1335
    • (2003) EMBO J. , vol.22 , pp. 1325-1335
    • Lufei, C.1    Ma, J.2    Huang, G.3    Zhang, T.4    Novotny-Diermayr, V.5
  • 22
    • 33645530423 scopus 로고    scopus 로고
    • Physical and functional interactions between Daxx and STAT3
    • R. Muromoto, K. Nakao, T. Watanabe, N. Sato, and Y. Sekine Physical and functional interactions between Daxx and STAT3 Oncogene 25 2006 2131 2136
    • (2006) Oncogene , vol.25 , pp. 2131-2136
    • Muromoto, R.1    Nakao, K.2    Watanabe, T.3    Sato, N.4    Sekine, Y.5
  • 23
    • 33748943974 scopus 로고    scopus 로고
    • Regulation of STAT3-mediated signaling by LMW-DSP2
    • Y. Sekine, S. Tsuji, O. Ikeda, N. Sato, and N. Aoki Regulation of STAT3-mediated signaling by LMW-DSP2 Oncogene 25 2006 5801 5806
    • (2006) Oncogene , vol.25 , pp. 5801-5806
    • Sekine, Y.1    Tsuji, S.2    Ikeda, O.3    Sato, N.4    Aoki, N.5
  • 24
    • 0029146749 scopus 로고
    • Characterisation of a novel enzyme of human fatty acid beta-oxidation: A matrix-associated, mitochondrial 2-enoyl-CoA hydratase
    • S. Jackson, J. Schaefer, B. Middleton, and D.M. Turnbull Characterisation of a novel enzyme of human fatty acid beta-oxidation: a matrix-associated, mitochondrial 2-enoyl-CoA hydratase Biochem. Biophys. Res. Commun. 214 1995 247 253
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 247-253
    • Jackson, S.1    Schaefer, J.2    Middleton, B.3    Turnbull, D.M.4
  • 25
    • 0037413353 scopus 로고    scopus 로고
    • Enoyl-CoA hydratase. Reaction, mechanism, and inhibition
    • G. Agnihotri, and H.W. Liu Enoyl-CoA hydratase. Reaction, mechanism, and inhibition Bioorg. Med. Chem. 11 2003 9 20
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 9-20
    • Agnihotri, G.1    Liu, H.W.2
  • 26
    • 77950625001 scopus 로고    scopus 로고
    • Functional proteomic analysis of non-alcoholic fatty liver disease in rat models: Enoyl-coenzyme a hydratase down-regulation exacerbates hepatic steatosis
    • X. Zhang, J. Yang, Y. Guo, H. Ye, and C. Yu Functional proteomic analysis of non-alcoholic fatty liver disease in rat models: enoyl-coenzyme a hydratase down-regulation exacerbates hepatic steatosis Hepatology 51 2010 1190 1199
    • (2010) Hepatology , vol.51 , pp. 1190-1199
    • Zhang, X.1    Yang, J.2    Guo, Y.3    Ye, H.4    Yu, C.5
  • 27
    • 79551545889 scopus 로고    scopus 로고
    • Bioinformatics-driven identification and examination of candidate genes for non-alcoholic fatty liver disease
    • K. Banasik, J.M. Justesen, M. Hornbak, N.T. Krarup, and A.P. Gjesing Bioinformatics-driven identification and examination of candidate genes for non-alcoholic fatty liver disease PLoS One 6 2011 e16542
    • (2011) PLoS One , vol.6 , pp. 16542
    • Banasik, K.1    Justesen, J.M.2    Hornbak, M.3    Krarup, N.T.4    Gjesing, A.P.5
  • 28
    • 79960321110 scopus 로고    scopus 로고
    • Ovine corpus luteum proteins, with functions including oxidative stress and lipid metabolism, show complex alterations during implantation
    • M. Arianmanesh, R.H. McIntosh, R.G. Lea, P.A. Fowler, and K.H. Al-Gubory Ovine corpus luteum proteins, with functions including oxidative stress and lipid metabolism, show complex alterations during implantation J. Endocrinol. 210 2011 47 58
    • (2011) J. Endocrinol. , vol.210 , pp. 47-58
    • Arianmanesh, M.1    McIntosh, R.H.2    Lea, R.G.3    Fowler, P.A.4    Al-Gubory, K.H.5
  • 29
    • 80255136274 scopus 로고    scopus 로고
    • Valproic acid utilizes the isoleucine breakdown pathway for its complete beta-oxidation
    • P.B. Luis, J.P. Ruiter, R. Ofman, L. Ijlst, and M. Moedas Valproic acid utilizes the isoleucine breakdown pathway for its complete beta-oxidation Biochem. Pharmacol. 82 2011 1740 1746
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1740-1746
    • Luis, P.B.1    Ruiter, J.P.2    Ofman, R.3    Ijlst, L.4    Moedas, M.5
  • 30
    • 77954176099 scopus 로고    scopus 로고
    • The role of enoyl-CoA hydratase short chain 1 and peroxiredoxin 3 in PP2-induced apoptosis in human breast cancer MCF-7 cells
    • X. Liu, R. Feng, and L. Du The role of enoyl-CoA hydratase short chain 1 and peroxiredoxin 3 in PP2-induced apoptosis in human breast cancer MCF-7 cells FEBS Lett. 584 2010 3185 3192
    • (2010) FEBS Lett. , vol.584 , pp. 3185-3192
    • Liu, X.1    Feng, R.2    Du, L.3


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