메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

High expression of nuclear factor 90 (NF90) leads to mitochondrial degradation in skeletal and cardiac muscles

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN ENHANCER BINDING FACTOR 3; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF 1; TRANSCRIPTION FACTOR PGC 1; UNCLASSIFIED DRUG;

EID: 84865097384     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043340     Document Type: Article
Times cited : (6)

References (35)
  • 1
    • 0037711199 scopus 로고    scopus 로고
    • The dsRNA binding protein family: critical roles, diverse cellular functions
    • Saunders LR, Barber GN, (2003) The dsRNA binding protein family: critical roles, diverse cellular functions. FASEB J. 17: 961-983.
    • (2003) FASEB J , vol.17 , pp. 961-983
    • Saunders, L.R.1    Barber, G.N.2
  • 2
    • 77955902024 scopus 로고    scopus 로고
    • The widespread regulation of microRNA biogenesis, function and decay
    • Krol J, Loedige I, Filipowicz W, (2010) The widespread regulation of microRNA biogenesis, function and decay. Nat Rev Genet. 11: 597-610.
    • (2010) Nat Rev Genet , vol.11 , pp. 597-610
    • Krol, J.1    Loedige, I.2    Filipowicz, W.3
  • 4
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter JM, Schultz SC, (1998) Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA. EMBO J 17: 7505-7513.
    • (1998) EMBO J , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 5
    • 0028088479 scopus 로고
    • Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90
    • Kao PN, Chen L, Brock G, Ng J, Kenny J, et al. (1994) Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90. J Biol Chem 269: 20691-20699.
    • (1994) J Biol Chem , vol.269 , pp. 20691-20699
    • Kao, P.N.1    Chen, L.2    Brock, G.3    Ng, J.4    Kenny, J.5
  • 6
    • 0033574260 scopus 로고    scopus 로고
    • A binding protein to the DNase I hypersensitive site II in HLA-DR alpha gene was identified as NF90
    • Sakamoto S, Morisawa K, Ota K, Nie J, Taniguchi T, (1999) A binding protein to the DNase I hypersensitive site II in HLA-DR alpha gene was identified as NF90. Biochemistry 38: 3355-3361.
    • (1999) Biochemistry , vol.38 , pp. 3355-3361
    • Sakamoto, S.1    Morisawa, K.2    Ota, K.3    Nie, J.4    Taniguchi, T.5
  • 7
    • 77950875317 scopus 로고    scopus 로고
    • NF45 and NF90 regulate HS4-dependent interleukin-13 transcription in T cells
    • Kiesler P, Haynes PA, Shi L, Kao PN, Wysocki VH, et al. (2010) NF45 and NF90 regulate HS4-dependent interleukin-13 transcription in T cells. J Biol Chem. 285: 8256-8267.
    • (2010) J Biol Chem , vol.285 , pp. 8256-8267
    • Kiesler, P.1    Haynes, P.A.2    Shi, L.3    Kao, P.N.4    Wysocki, V.H.5
  • 8
    • 0347093422 scopus 로고    scopus 로고
    • Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3
    • Gwizdek C, Ossareh-Nazari B, Brownawell AM, Evers S, Macara IG, et al. (2004) Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3. J Biol Chem 279: 884-891.
    • (2004) J Biol Chem , vol.279 , pp. 884-891
    • Gwizdek, C.1    Ossareh-Nazari, B.2    Brownawell, A.M.3    Evers, S.4    Macara, I.G.5
  • 9
    • 67650080812 scopus 로고    scopus 로고
    • The NF90-NF45 complex functions as a negative regulator in the microRNA processing pathway
    • Sakamoto S, Aoki K, Higuchi T, Todaka H, Morisawa K, et al. (2009) The NF90-NF45 complex functions as a negative regulator in the microRNA processing pathway. Mol Cell Biol. 29: 3754-3769.
    • (2009) Mol Cell Biol , vol.29 , pp. 3754-3769
    • Sakamoto, S.1    Aoki, K.2    Higuchi, T.3    Todaka, H.4    Morisawa, K.5
  • 10
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou Z, Licklider LJ, Gygi SP, Reed R, (2002) Comprehensive proteomic analysis of the human spliceosome. Nature. 419: 182-185.
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 11
    • 78149483844 scopus 로고    scopus 로고
    • IL-2 mRNA stabilization upon PMA stimulation is dependent on NF90-Ser647 phosphorylation by protein kinase CbetaI
    • United States
    • Zhu P, Jiang W, Cao L, Yu W, Pei Y, et al. (2010) IL-2 mRNA stabilization upon PMA stimulation is dependent on NF90-Ser647 phosphorylation by protein kinase CbetaI. J Immunol. United States. 5140-5149.
    • (2010) J Immunol. , pp. 5140-5149
    • Zhu, P.1    Jiang, W.2    Cao, L.3    Yu, W.4    Pei, Y.5
  • 12
    • 0036924040 scopus 로고    scopus 로고
    • Nuclear export of NF90 is required for interleukin-2 mRNA stabilization
    • J R.Y
    • Shim J, Lim H, J RY, Karin M, (2002) Nuclear export of NF90 is required for interleukin-2 mRNA stabilization. Mol Cell. 10: 1331-1344.
    • (2002) Mol Cell , vol.10 , pp. 1331-1344
    • Shim, J.1    Lim, H.2    Karin, M.3
  • 13
    • 47049116117 scopus 로고    scopus 로고
    • MKP-1 mRNA stabilization and translational control by RNA-binding proteins HuR and NF90
    • Kuwano Y, Kim HH, Abdelmohsen K, Pullmann R Jr, Martindale JL, et al. (2008) MKP-1 mRNA stabilization and translational control by RNA-binding proteins HuR and NF90. Mol Cell Biol. 28: 4562-4575.
    • (2008) Mol Cell Biol , vol.28 , pp. 4562-4575
    • Kuwano, Y.1    Kim, H.H.2    Abdelmohsen, K.3    Pullmann Jr., R.4    Martindale, J.L.5
  • 14
    • 75649105362 scopus 로고    scopus 로고
    • NF90 selectively represses the translation of target mRNAs bearing an AU-rich signature motif
    • Kuwano Y, Pullmann R Jr, Marasa BS, Abdelmohsen K, Lee EK, et al. (2010) NF90 selectively represses the translation of target mRNAs bearing an AU-rich signature motif. Nucleic Acids Res. 38: 225-238.
    • (2010) Nucleic Acids Res , vol.38 , pp. 225-238
    • Kuwano, Y.1    Pullmann Jr., R.2    Marasa, B.S.3    Abdelmohsen, K.4    Lee, E.K.5
  • 15
    • 67749127718 scopus 로고    scopus 로고
    • Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein
    • Wang P, Song W, Mok BW, Zhao P, Qin K, et al. (2009) Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein. J Virol. 83: 7850-7861.
    • (2009) J Virol , vol.83 , pp. 7850-7861
    • Wang, P.1    Song, W.2    Mok, B.W.3    Zhao, P.4    Qin, K.5
  • 16
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa H, Yamamura K, Miyazaki J, (1991) Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108: 193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 17
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y, (2004) In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 15: 1101-1111.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 18
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, et al. (2000) LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19: 5720-5728.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5
  • 19
    • 0042206454 scopus 로고    scopus 로고
    • Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B
    • He H, Dang Y, Dai F, Guo Z, Wu J, et al. (2003) Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B. J Biol Chem 278: 29278-29287.
    • (2003) J Biol Chem , vol.278 , pp. 29278-29287
    • He, H.1    Dang, Y.2    Dai, F.3    Guo, Z.4    Wu, J.5
  • 20
    • 28144431882 scopus 로고    scopus 로고
    • Molecular cloning and characterization of rat LC3A and LC3B-two novel markers of autophagosome
    • Wu J, Dang Y, Su W, Liu C, Ma H, et al. (2006) Molecular cloning and characterization of rat LC3A and LC3B-two novel markers of autophagosome. Biochem Biophys Res Commun 339: 437-442.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 437-442
    • Wu, J.1    Dang, Y.2    Su, W.3    Liu, C.4    Ma, H.5
  • 21
    • 0032549811 scopus 로고    scopus 로고
    • A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis
    • Puigserver P, Wu Z, Park CW, Graves R, Wright M, et al. (1998) A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 92: 829-839.
    • (1998) Cell , vol.92 , pp. 829-839
    • Puigserver, P.1    Wu, Z.2    Park, C.W.3    Graves, R.4    Wright, M.5
  • 22
    • 0033538473 scopus 로고    scopus 로고
    • Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1
    • Wu Z, Puigserver P, Andersson U, Zhang C, Adelmant G, et al. (1999) Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 98: 115-124.
    • (1999) Cell , vol.98 , pp. 115-124
    • Wu, Z.1    Puigserver, P.2    Andersson, U.3    Zhang, C.4    Adelmant, G.5
  • 23
    • 0035971150 scopus 로고    scopus 로고
    • Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR
    • Tian B, Mathews MB, (2001) Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR. J Biol Chem. 276: 9936-9944.
    • (2001) J Biol Chem , vol.276 , pp. 9936-9944
    • Tian, B.1    Mathews, M.B.2
  • 24
    • 0033575228 scopus 로고    scopus 로고
    • DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR
    • Patel RC, Vestal DJ, Xu Z, Bandyopadhyay S, Guo W, et al. (1999) DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR. J Biol Chem 274: 20432-20437.
    • (1999) J Biol Chem , vol.274 , pp. 20432-20437
    • Patel, R.C.1    Vestal, D.J.2    Xu, Z.3    Bandyopadhyay, S.4    Guo, W.5
  • 25
    • 0031914976 scopus 로고    scopus 로고
    • DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45
    • Ting NS, Kao PN, Chan DW, Lintott LG, Lees-Miller SP, (1998) DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. J Biol Chem 273: 2136-2145.
    • (1998) J Biol Chem , vol.273 , pp. 2136-2145
    • Ting, N.S.1    Kao, P.N.2    Chan, D.W.3    Lintott, L.G.4    Lees-Miller, S.P.5
  • 26
    • 34249853312 scopus 로고    scopus 로고
    • Dynamic binding of Ku80, Ku70 and NF90 to the IL-2 promoter in vivo in activated T-cells
    • Shi L, Qiu D, Zhao G, Corthesy B, Lees-Miller S, et al. (2007) Dynamic binding of Ku80, Ku70 and NF90 to the IL-2 promoter in vivo in activated T-cells. Nucleic Acids Res. 35: 2302-2310.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2302-2310
    • Shi, L.1    Qiu, D.2    Zhao, G.3    Corthesy, B.4    Lees-Miller, S.5
  • 27
    • 0034733748 scopus 로고    scopus 로고
    • Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3
    • Tang J, Kao PN, Herschman HR, (2000) Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. J Biol Chem. 275: 19866-19876.
    • (2000) J Biol Chem , vol.275 , pp. 19866-19876
    • Tang, J.1    Kao, P.N.2    Herschman, H.R.3
  • 29
    • 0036132874 scopus 로고    scopus 로고
    • The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells
    • Reichman TW, Muniz LC, Mathews MB, (2002) The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells. Mol Cell Biol 22: 343-356.
    • (2002) Mol Cell Biol , vol.22 , pp. 343-356
    • Reichman, T.W.1    Muniz, L.C.2    Mathews, M.B.3
  • 30
    • 2342592545 scopus 로고    scopus 로고
    • The estrogen-related receptor alpha (ERRalpha) functions in PPARgamma coactivator 1alpha (PGC-1alpha)-induced mitochondrial biogenesis
    • Schreiber SN, Emter R, Hock MB, Knutti D, Cardenas J, et al. (2004) The estrogen-related receptor alpha (ERRalpha) functions in PPARgamma coactivator 1alpha (PGC-1alpha)-induced mitochondrial biogenesis. Proc Natl Acad Sci U S A 101: 6472-6477.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 6472-6477
    • Schreiber, S.N.1    Emter, R.2    Hock, M.B.3    Knutti, D.4    Cardenas, J.5
  • 31
    • 21444448612 scopus 로고    scopus 로고
    • NF90 regulates cell cycle exit and terminal myogenic differentiation by direct binding to the 3'-untranslated region of MyoD and p21WAF1/CIP1 mRNAs
    • Shi L, Zhao G, Qiu D, Godfrey WR, Vogel H, et al. (2005) NF90 regulates cell cycle exit and terminal myogenic differentiation by direct binding to the 3'-untranslated region of MyoD and p21WAF1/CIP1 mRNAs. J Biol Chem 280: 18981-18989.
    • (2005) J Biol Chem , vol.280 , pp. 18981-18989
    • Shi, L.1    Zhao, G.2    Qiu, D.3    Godfrey, W.R.4    Vogel, H.5
  • 32
    • 17144399857 scopus 로고    scopus 로고
    • High-efficiency protein extraction from polyacrylamide gels for molecular mass measurement by matrix-assisted laser desorption/ionization-time of flight-mass spectrometry
    • Jin Y, Manabe T, (2005) High-efficiency protein extraction from polyacrylamide gels for molecular mass measurement by matrix-assisted laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 26: 1019-1028.
    • (2005) Electrophoresis , vol.26 , pp. 1019-1028
    • Jin, Y.1    Manabe, T.2
  • 33
    • 0028264320 scopus 로고
    • Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy
    • Rando TA, Blau HM, (1994) Primary mouse myoblast purification, characterization, and transplantation for cell-mediated gene therapy. J Cell Biol 125: 1275-1287.
    • (1994) J Cell Biol , vol.125 , pp. 1275-1287
    • Rando, T.A.1    Blau, H.M.2
  • 34
    • 0000360265 scopus 로고
    • The fluorometric measurement of deoxyribonucleic acid in animal tissues with special reference to the central nervous system
    • Kissane JM, Robins E, (1958) The fluorometric measurement of deoxyribonucleic acid in animal tissues with special reference to the central nervous system. J Biol Chem 233: 184-188.
    • (1958) J Biol Chem , vol.233 , pp. 184-188
    • Kissane, J.M.1    Robins, E.2
  • 35
    • 0035813123 scopus 로고    scopus 로고
    • Identification of a phorbol ester-responsive element in the interferon-gamma receptor 1 chain gene
    • Sakamoto S, Taniguchi T, (2001) Identification of a phorbol ester-responsive element in the interferon-gamma receptor 1 chain gene. J Biol Chem 276: 37237-37241.
    • (2001) J Biol Chem , vol.276 , pp. 37237-37241
    • Sakamoto, S.1    Taniguchi, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.