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Volumn 19, Issue 5, 2008, Pages 1848-1861

FBXO25-associated nuclear domains: A novel subnuclear structure

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CULLIN; DACTINOMYCIN; HUNTINGTIN; NUCLEAR PROTEIN; POLYGLUTAMINE; PROTEASOME; PROTEIN FBXO25; PROTEIN SKP1; RING FINGER PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 44849099042     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E07-08-0815     Document Type: Article
Times cited : (18)

References (58)
  • 1
    • 18344386695 scopus 로고    scopus 로고
    • Interwoven ubiquitination oscillators and control of cell cycle transitions
    • Ang, X. L., and Harper, J. W. (2005). Interwoven ubiquitination oscillators and control of cell cycle transitions. Oncogene 17, 2860-2870.
    • (2005) Oncogene , vol.17 , pp. 2860-2870
    • Ang, X.L.1    Harper, J.W.2
  • 4
    • 0024114933 scopus 로고
    • Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells
    • Bond, U. (1988). Heat shock but not other stress inducers leads to the disruption of a sub-set of snRNPs and inhibition of in vitro splicing in HeLa cells. EMBO J. 7, 3509-3518.
    • (1988) EMBO J , vol.7 , pp. 3509-3518
    • Bond, U.1
  • 6
    • 12144283465 scopus 로고    scopus 로고
    • Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins
    • Chen, D., Dundr, M., Wang, C., Leung, A., Lamond, A., Misteli, T., and Huang, S. (2005). Condensed mitotic chromatin is accessible to transcription factors and chromatin structural proteins. J. Cell Biol. 168, 41-54.
    • (2005) J. Cell Biol , vol.168 , pp. 41-54
    • Chen, D.1    Dundr, M.2    Wang, C.3    Leung, A.4    Lamond, A.5    Misteli, T.6    Huang, S.7
  • 8
    • 28444456713 scopus 로고    scopus 로고
    • Cajal bodies: A long history of discovery
    • Cioce, M., and Lamond, A. I. (2005). Cajal bodies: a long history of discovery. Annu. Rev. Cell Dev. Biol. 21, 105-131.
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 105-131
    • Cioce, M.1    Lamond, A.I.2
  • 9
    • 36649036112 scopus 로고    scopus 로고
    • Intracellular calcium changes in mice Leydig cells are dependent on calcium entry through T-type calcium channels
    • Costa, R. R., and Varanda W. A. (2007). Intracellular calcium changes in mice Leydig cells are dependent on calcium entry through T-type calcium channels. J. Physiol. 585, 339-349.
    • (2007) J. Physiol , vol.585 , pp. 339-349
    • Costa, R.R.1    Varanda, W.A.2
  • 10
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
    • Dai, M. S., and Lu, H. (2004). Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5. J. Biol. Chem. 279, 44475-44482.
    • (2004) J. Biol. Chem , vol.279 , pp. 44475-44482
    • Dai, M.S.1    Lu, H.2
  • 11
    • 0033200397 scopus 로고    scopus 로고
    • Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle
    • Freed, E., Lacey, K. R., Huie, P., Lyapina, S. A., Deshaies, R. J., Stearns, T., and Jackson, P. K. (1999). Components of an SCF ubiquitin ligase localize to the centrosome and regulate the centrosome duplication cycle. Genes Dev. 13, 2242-2257.
    • (1999) Genes Dev , vol.13 , pp. 2242-2257
    • Freed, E.1    Lacey, K.R.2    Huie, P.3    Lyapina, S.A.4    Deshaies, R.J.5    Stearns, T.6    Jackson, P.K.7
  • 12
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • Fujimuro, M., Sawada, H., and Yokosawa, H. (1994). Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett. 349, 173-180.
    • (1994) FEBS Lett , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 13
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary, J. D., and Clarke, S. (1998). RNA and protein interactions modulated by protein arginine methylation. Prog. Nucleic Acid Res. Mol. Biol. 61, 65-131.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and Ciechanover, A. (2002). The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428.
    • (2002) Physiol. Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 15
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. (2003). Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 16
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., and Goldberg, A. L. (2001). Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA 98, 14440-14445.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 17
    • 0037339087 scopus 로고    scopus 로고
    • Reversible disassembly of somatic nucleoli by the germ cell proteins FRGY2a and FRGY2b
    • Gonda, K., Fowler, J., Katoku-Kikyo, N., Haroldson, J., Wudel, J., and Kikyo, N. (2003). Reversible disassembly of somatic nucleoli by the germ cell proteins FRGY2a and FRGY2b. Nat. Cell Biol. 5, 05-210.
    • (2003) Nat. Cell Biol , vol.5 , pp. 05-210
    • Gonda, K.1    Fowler, J.2    Katoku-Kikyo, N.3    Haroldson, J.4    Wudel, J.5    Kikyo, N.6
  • 18
    • 27744553732 scopus 로고    scopus 로고
    • Identification of thioredoxin reductase 1-regulated genes using small interference RNA and cDNA microarray
    • Gorreta, F., Runfola, T. P., VanMeter, A. J., Barzaghi, D., Chandhoke, V., and Del Giacco, L. (2005). Identification of thioredoxin reductase 1-regulated genes using small interference RNA and cDNA microarray. Cancer Biol. Ther. 4, 1079-1088.
    • (2005) Cancer Biol. Ther , vol.4 , pp. 1079-1088
    • Gorreta, F.1    Runfola, T.P.2    VanMeter, A.J.3    Barzaghi, D.4    Chandhoke, V.5    Del Giacco, L.6
  • 19
    • 0030980312 scopus 로고    scopus 로고
    • Mitotic repression of the transcriptional machinery. Trends Biochem
    • Gottesfeld, J. M., and Forbes, D. J. (1997). Mitotic repression of the transcriptional machinery. Trends Biochem. Trends Biochem. Sci. 22, 197-202.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 197-202
    • Gottesfeld, J.M.1    Forbes, D.J.2
  • 20
    • 0016813418 scopus 로고
    • Nucleolar necklaces in chick embryo fibroblast cells. I. Formation of necklaces by dichlororibobenzimidazole and other adenosine analogues that decrease RNA synthesis and degrade preribosomes
    • Granick, D. (1975). Nucleolar necklaces in chick embryo fibroblast cells. I. Formation of necklaces by dichlororibobenzimidazole and other adenosine analogues that decrease RNA synthesis and degrade preribosomes. J. Cell Biol. 65, 389-417.
    • (1975) J. Cell Biol , vol.65 , pp. 389-417
    • Granick, D.1
  • 22
    • 30444437477 scopus 로고    scopus 로고
    • Subnuclear organelles: New insights into form and function
    • Handwerger, K. E., and Gall, J. G. (2006). Subnuclear organelles: new insights into form and function. Trends Cell Biol. 16, 19-26.
    • (2006) Trends Cell Biol , vol.16 , pp. 19-26
    • Handwerger, K.E.1    Gall, J.G.2
  • 23
    • 0003448569 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 27
    • 4344660471 scopus 로고    scopus 로고
    • Inhibition of HDM2 and activation of p53 by ribosomal protein L23
    • Jin, A., Itahana, K., O'Keefe, K., and Zhang, Y. (2004a). Inhibition of HDM2 and activation of p53 by ribosomal protein L23. Mol. Cell. Biol. 24, 7669-7680.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 7669-7680
    • Jin, A.1    Itahana, K.2    O'Keefe, K.3    Zhang, Y.4
  • 29
    • 0034568688 scopus 로고    scopus 로고
    • The F-box protein family
    • Kipreos, E. T., and Pagano, M. (2000). The F-box protein family. Genome Biol. 1, 1-7.
    • (2000) Genome Biol , vol.1 , pp. 1-7
    • Kipreos, E.T.1    Pagano, M.2
  • 31
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: A model for nuclear organelles
    • Lamond, A. I., and Spector, D. L. (2003). Nuclear speckles: a model for nuclear organelles. Nat. Rev. Mol. Cell Biol. 4, 605-612.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 32
    • 0033590624 scopus 로고    scopus 로고
    • Inhibition of RNA polymerase II as a trigger for the p53 response
    • Ljungman, M., Zhang, F., Chen, F., Rainbow, A. J., and McKay, B. C. (1999). Inhibition of RNA polymerase II as a trigger for the p53 response. Oncogene 18, 583-592.
    • (1999) Oncogene , vol.18 , pp. 583-592
    • Ljungman, M.1    Zhang, F.2    Chen, F.3    Rainbow, A.J.4    McKay, B.C.5
  • 34
    • 0031561729 scopus 로고    scopus 로고
    • Inhibition of protein dephosphorylation results in the accumulation of splicing snRNPs and coiled bodies within the nucleolus
    • Lyon, C. E., Bohmann, K., Sleeman, J., and Lamond, A. I. (1997). Inhibition of protein dephosphorylation results in the accumulation of splicing snRNPs and coiled bodies within the nucleolus. Exp. Cell Res. 230, 84-93.
    • (1997) Exp. Cell Res , vol.230 , pp. 84-93
    • Lyon, C.E.1    Bohmann, K.2    Sleeman, J.3    Lamond, A.I.4
  • 37
    • 33744936267 scopus 로고    scopus 로고
    • FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle
    • Maragno, A. L., Baqui, M. M., and Gomes, M. D. (2006). FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle. Biochim. Biophys. Acta 1760, 966-972.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 966-972
    • Maragno, A.L.1    Baqui, M.M.2    Gomes, M.D.3
  • 38
    • 0037327059 scopus 로고    scopus 로고
    • Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 and 25 differently
    • Nefkens, I., Negorev, D. G., Ishov, A. M., Michaelson, J. S., Yeh, E. T., Tanguay, R. M., Muller, W. E., and Maul, G. G. (2003). Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 and 25 differently. J. Cell Sci. 116, 513-524.
    • (2003) J. Cell Sci , vol.116 , pp. 513-524
    • Nefkens, I.1    Negorev, D.G.2    Ishov, A.M.3    Michaelson, J.S.4    Yeh, E.T.5    Tanguay, R.M.6    Muller, W.E.7    Maul, G.G.8
  • 39
    • 0035943003 scopus 로고    scopus 로고
    • The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1
    • Pellizzoni, L., Baccon, J., Charroux, B., and Dreyfuss, G. (2001). The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr. Biol. 11, 1079-1088.
    • (2001) Curr. Biol , vol.11 , pp. 1079-1088
    • Pellizzoni, L.1    Baccon, J.2    Charroux, B.3    Dreyfuss, G.4
  • 40
    • 0014859062 scopus 로고
    • Persistent synthesis of 5S RNA when production of 28S and 18S ribosomal RNA is inhibited by low doses of actinomycin D
    • Perry, R. P., Kelley, D. E. (1970). Persistent synthesis of 5S RNA when production of 28S and 18S ribosomal RNA is inhibited by low doses of actinomycin D. J. Cell. Physiol. 76, 127-140.
    • (1970) J. Cell. Physiol , vol.76 , pp. 127-140
    • Perry, R.P.1    Kelley, D.E.2
  • 41
    • 0034739848 scopus 로고    scopus 로고
    • In vivo analysis of Cajal body movement, separation, and joining in live human cells
    • Platani, M., Goldberg, I., Swedlow, J. R., and Lamond, A. I. (2000). In vivo analysis of Cajal body movement, separation, and joining in live human cells. J. Cell Biol. 151, 1561-1574.
    • (2000) J. Cell Biol , vol.151 , pp. 1561-1574
    • Platani, M.1    Goldberg, I.2    Swedlow, J.R.3    Lamond, A.I.4
  • 43
    • 29244480602 scopus 로고    scopus 로고
    • Proteasomes degrade proteins in focal subdomains of the human cell nucleus
    • Rockel, T. D., Stuhlmann, D., and von Mikecz, A. (2005). Proteasomes degrade proteins in focal subdomains of the human cell nucleus. Cell Sci. 118, 5231-5242.
    • (2005) Cell Sci , vol.118 , pp. 5231-5242
    • Rockel, T.D.1    Stuhlmann, D.2    von Mikecz, A.3
  • 44
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D. C. (2006). The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 48
    • 0015293356 scopus 로고
    • The synthesis of acidic chromosomal proteins during the cell cycle of HeLa S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication
    • Stein, G. S., and Borun, T. W. (1972). The synthesis of acidic chromosomal proteins during the cell cycle of HeLa S-3 cells. I. The accelerated accumulation of acidic residual nuclear protein before the initiation of DNA replication. J. Cell Biol. 52, 292-307.
    • (1972) J. Cell Biol , vol.52 , pp. 292-307
    • Stein, G.S.1    Borun, T.W.2
  • 49
    • 0015307157 scopus 로고
    • Evolution of the nucleoli during oogenesis in Xenopus laevis studied by electron microscopy
    • Van Gansen, P., and Schram, A. (1972). Evolution of the nucleoli during oogenesis in Xenopus laevis studied by electron microscopy. J. Cell Sci. 10, 339-367.
    • (1972) J. Cell Sci , vol.10 , pp. 339-367
    • Van Gansen, P.1    Schram, A.2
  • 51
    • 0032879437 scopus 로고    scopus 로고
    • Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates
    • Wanker, E. E., Scherzinger, E., Heiser, V., Sittler, A., Eickhoff, H., and Lehrach, H. (1999). Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates. Methods Enzymol. 309, 375-386.
    • (1999) Methods Enzymol , vol.309 , pp. 375-386
    • Wanker, E.E.1    Scherzinger, E.2    Heiser, V.3    Sittler, A.4    Eickhoff, H.5    Lehrach, H.6
  • 52
    • 0016343080 scopus 로고
    • The transcriptional role of host DNA-dependent RNA polymerases in adenovirus-infected KB cells
    • Weinmann, R., Raskas, H. J., and Roeder, R. G. (1975). The transcriptional role of host DNA-dependent RNA polymerases in adenovirus-infected KB cells. Cold Spring Harb. Symp. Quant. Biol. 34, 495-500.
    • (1975) Cold Spring Harb. Symp. Quant. Biol , vol.34 , pp. 495-500
    • Weinmann, R.1    Raskas, H.J.2    Roeder, R.G.3
  • 53
    • 0033956753 scopus 로고    scopus 로고
    • The SCF(HOS/β-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation
    • Wu, K., Fuchs, S. Y., Chen, A., Tan, P., Gomez, C., Ronai, Z., and Pan, Z. Q. (2000). The SCF(HOS/β-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation. Mol. Cell. Biol. 20, 1382-1393.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 1382-1393
    • Wu, K.1    Fuchs, S.Y.2    Chen, A.3    Tan, P.4    Gomez, C.5    Ronai, Z.6    Pan, Z.Q.7
  • 54
    • 0022531458 scopus 로고
    • RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis
    • Yost, H. J., and Lindquist, S. (1986). RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis. Cell 25, 185-193.
    • (1986) Cell , vol.25 , pp. 185-193
    • Yost, H.J.1    Lindquist, S.2
  • 55
    • 0025114362 scopus 로고
    • Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells
    • Yung, B. Y., Bor, A. M., and Chan, P. K. (1990). Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells. Cancer Res. 50, 5987-5991.
    • (1990) Cancer Res , vol.50 , pp. 5987-5991
    • Yung, B.Y.1    Bor, A.M.2    Chan, P.K.3
  • 56
    • 0030909002 scopus 로고    scopus 로고
    • Dynamic relocation of transcription and splicing factors dependent upon transcriptional activity
    • Zeng, C., Kim, E., Warren, S. L., and Berget, S. M. (1997). Dynamic relocation of transcription and splicing factors dependent upon transcriptional activity. EMBO J. 16, 1401-1412.
    • (1997) EMBO J , vol.16 , pp. 1401-1412
    • Zeng, C.1    Kim, E.2    Warren, S.L.3    Berget, S.M.4
  • 57
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., Salomoni, P., and Pandolfi, P. P. (2000). The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2, E85-E90.
    • (2000) Nat. Cell Biol , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 58
    • 1842759541 scopus 로고    scopus 로고
    • Effect of alpha-pinene on nuclear translocation of NF-kappa B in THP-1 cells
    • Zhou, Y., Tang, F. D., Mao, G. G., and Bian, R. L. (2004). Effect of alpha-pinene on nuclear translocation of NF-kappa B in THP-1 cells. Acta Pharmacol. Sin. 25, 480-484.
    • (2004) Acta Pharmacol. Sin , vol.25 , pp. 480-484
    • Zhou, Y.1    Tang, F.D.2    Mao, G.G.3    Bian, R.L.4


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