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Volumn 10, Issue 15, 2010, Pages 2746-2757

Identification of FBXO25-interacting proteins using an integrated proteomics approach

Author keywords

Actin; Cell biology; FANDs; Global protein analysis; Molecular interaction; Proteolysis

Indexed keywords

BETA ACTIN; F BOX PROTEIN; PROTEIN ANTIBODY; PROTEIN FBX025; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 77955108101     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900419     Document Type: Article
Times cited : (9)

References (39)
  • 1
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: Tipping the scales of cancer
    • DOI 10.1038/nrc2396, PII NRC2396
    • Frescas, D., Pagano, M., Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer. Nat. Rev. Cancer 2008, 8, 438-449. (Pubitemid 351744963)
    • (2008) Nature Reviews Cancer , vol.8 , Issue.6 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 3
    • 27644546219 scopus 로고    scopus 로고
    • In vitro reconstitution of SCF substrate ubiquitination with purified proteins
    • Petroski, M. D., Deshaies, R. J., In vitro reconstitution of SCF substrate ubiquitination with purified proteins. Methods Enzymol. 2005, 398, 143-158.
    • (2005) Methods Enzymol. , vol.398 , pp. 143-158
    • Petroski, M.D.1    Deshaies, R.J.2
  • 4
    • 4444318673 scopus 로고    scopus 로고
    • The SCF ubiquitin ligase: Insights into a molecular machine
    • DOI 10.1038/nrm1471
    • Cardozo, T., Pagano, M., The SCF ubiquitin ligase: insights into a molecular machine. Nat. Rev. Mol. Cell Biol. 2004, 5, 739-751. (Pubitemid 39208183)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 739-751
    • Cardozo, T.1    Pagano, M.2
  • 5
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W. et al., Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 2008, 134, 995-1006.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4
  • 6
    • 0036929129 scopus 로고    scopus 로고
    • CAND1, an inhibitor of CUL1-SKP1 binding and SCF ligases
    • DOI 10.1016/S1097-2765(02)00783-9
    • Liu, J., Furukawa, M., Matsumoto, T., Xiong, Y., NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol. Cell 2002, 10, 1511-1518. (Pubitemid 36050891)
    • (2002) Molecular Cell , vol.10 , Issue.6 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 7
    • 0036924046 scopus 로고    scopus 로고
    • CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
    • Zheng, J., Yang, X., Harrell, J. M., Ryzhikov, S. et al., CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol. Cell 2002, 10, 1519-1526.
    • (2002) Mol. Cell , vol.10 , pp. 1519-1526
    • Zheng, J.1    Yang, X.2    Harrell, J.M.3    Ryzhikov, S.4
  • 8
    • 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., Gomes, M. D., FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle. Biochim. Biophys. Acta 2006, 1760, 966-972.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 966-972
    • Maragno, A.L.1    Baqui, M.M.2    Gomes, M.D.3
  • 9
    • 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., Goldberg, A. L., Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA 2001, 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
  • 10
    • 44849099042 scopus 로고    scopus 로고
    • FBXO25-associated Nuclear Domains: A Novel Subnuclear Structure
    • Manfiolli, A. O., Maragno, A. L., Baqui, M. M., Yokoo, S. et al., FBXO25-associated Nuclear Domains: A Novel Subnuclear Structure. Mol. Biol. Cell 2008, 19, 1848-1861.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1848-1861
    • Manfiolli, A.O.1    Maragno, A.L.2    Baqui, M.M.3    Yokoo, S.4
  • 13
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • DOI 10.1038/340245a0
    • Fields, S., Song, O. K., A novel genetic system to detect protein protein interactions. Nature 1989, 340, 245-246. (Pubitemid 19171591)
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 14
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J. H. et al., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25, 3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.H.4
  • 16
    • 33750325090 scopus 로고    scopus 로고
    • Actin-based modeling of a transcriptionally competent nuclear substructure induced by transcription inhibition
    • Wang, I. F., Chang, H. Y., Shen, C. K., Actin-based modeling of a transcriptionally competent nuclear substructure induced by transcription inhibition. Exp. Cell. Res. 2006, 312, 3796-3807.
    • (2006) Exp. Cell. Res. , vol.312 , pp. 3796-3807
    • Wang, I.F.1    Chang, H.Y.2    Shen, C.K.3
  • 17
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., Gygi, S. P., Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 2007, 4, 207-214.
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 18
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database
    • Eng, J. K., Mccormack, A. L., Yates, J. R., An approach to correlate tandem mass-spectral data of peptides with amino-acid-sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    Mccormack, A.L.2    Yates, J.R.3
  • 21
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 22
    • 7944239067 scopus 로고    scopus 로고
    • Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II
    • Hofmann, W. A., Stojiljkovic, L., Fuchsova, B., Vargas, G. M. et al., Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat. Cell Biol. 2004, 6, 1094-1101.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1094-1101
    • Hofmann, W.A.1    Stojiljkovic, L.2    Fuchsova, B.3    Vargas, G.M.4
  • 23
    • 49449090299 scopus 로고    scopus 로고
    • Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes
    • Sonnberg, S., Seet, B. T., Pawson, T., Fleming, S. B., Mercer, A. A., Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes. Proc. Natl. Acad. Sci. USA 2008, 105, 10955-10960.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10955-10960
    • Sonnberg, S.1    Seet, B.T.2    Pawson, T.3    Fleming, S.B.4    Mercer, A.A.5
  • 24
    • 32644449429 scopus 로고    scopus 로고
    • Nuclear act to polymerize or not to polymerize
    • Hofmann, W. A., de Lanerolle, P., Nuclear actin: to polymerize or not to polymerize. J. Cell Biol. 2006, 172, 495-496.
    • (2006) J. Cell Biol. , vol.172 , pp. 495-496
    • Hofmann, W.A.1    De Lanerolle, P.2
  • 25
    • 58049173935 scopus 로고    scopus 로고
    • Transcriptional control of gene expression by actin and myosin
    • Louvet, E., Percipalle, P., Transcriptional control of gene expression by actin and myosin. Int. Rev. Cell Mol. Biol. 2009, 272, 107-147.
    • (2009) Int. Rev. Cell Mol. Biol. , vol.272 , pp. 107-147
    • Louvet, E.1    Percipalle, P.2
  • 26
    • 12344299676 scopus 로고    scopus 로고
    • Nuclear actin is partially associated with Cajal bodies in human cells in culture and relocates to the nuclear periphery after infection of cells by adenovirus 5
    • Gedge, L. J., Morrison, E. E., Blair, G. E., Walker, J. H., Nuclear actin is partially associated with Cajal bodies in human cells in culture and relocates to the nuclear periphery after infection of cells by adenovirus 5. Exp. Cell Res. 2005, 303, 229-239.
    • (2005) Exp. Cell Res. , vol.303 , pp. 229-239
    • Gedge, L.J.1    Morrison, E.E.2    Blair, G.E.3    Walker, J.H.4
  • 27
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J. A., Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 1987, 105, 1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 28
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue, M., Brenner, S. L., Spector, I., Korn, E. D., Inhibition of actin polymerization by latrunculin A. FEBS Lett. 1987, 213, 316-318.
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 29
    • 33750590972 scopus 로고    scopus 로고
    • Genetic and expression aberrations of E3 ubiquitin ligases in human breast cancer
    • DOI 10.1158/1541-7786.MCR-06-0182
    • Chen, C., Seth, A. K., Aplin, A. E., Genetic and expression aberrations of E3 ubiquitin ligases in human breast cancer. Mol. Cancer Res. 2006, 4, 695-707. (Pubitemid 44683310)
    • (2006) Molecular Cancer Research , vol.4 , Issue.10 , pp. 695-707
    • Chen, C.1    Seth, A.K.2    Aplin, A.E.3
  • 30
    • 33645285000 scopus 로고    scopus 로고
    • Molecular functions of nuclear actin in transcription
    • Percipalle, P., Visa, N., Molecular functions of nuclear actin in transcription. J. Cell Biol. 2006, 172, 967-971.
    • (2006) J. Cell Biol. , vol.172 , pp. 967-971
    • Percipalle, P.1    Visa, N.2
  • 32
    • 27644506209 scopus 로고    scopus 로고
    • Nuclear actin extends, with no contraction in sight
    • DOI 10.1091/mbc.E05-07-0656
    • Pederson, T., Aebi, U., Nuclear actin extends, with no contraction in sight. Mol. Biol. Cell 2005, 16, 5055-5060. (Pubitemid 41566818)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5055-5060
    • Pederson, T.1    Aebi, U.2
  • 33
    • 0032957520 scopus 로고    scopus 로고
    • Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody
    • Gonsior, S. M., Platz, S., Buchmeier, S., Scheer, U. et al., Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J. Cell Sci. 1999, 112, 797-809. (Pubitemid 29179313)
    • (1999) Journal of Cell Science , vol.112 , Issue.6 , pp. 797-809
    • Gonsior, S.M.1    Platz, S.2    Buchmeier, S.3    Scheer, U.4    Jockusch, B.M.5    Hinssen, H.6
  • 34
    • 17844390892 scopus 로고    scopus 로고
    • Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators
    • DOI 10.1002/bies.20200
    • Archer, S. K., Claudianos, C., Campbell, H. D., Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators. Bioessays 2005, 27, 388-396. (Pubitemid 40592595)
    • (2005) BioEssays , vol.27 , Issue.4 , pp. 388-396
    • Archer, S.K.1    Claudianos, C.2    Campbell, H.D.3
  • 36
    • 47549089279 scopus 로고    scopus 로고
    • Myosin-10 and actin filaments are essential for mitotic spindle function
    • DOI 10.1083/jcb.200804062
    • Woolner, S., O'Brien, L. L., Wiese, C., Bement, W. M., Myosin-10 and actin filaments are essential for mitotic spindle function. J. Cell Biol. 2008, 182, 77-88. (Pubitemid 352008623)
    • (2008) Journal of Cell Biology , vol.182 , Issue.1 , pp. 77-88
    • Woolner, S.1    O'Brien, L.L.2    Wiese, C.3    Bement, W.M.4
  • 37
    • 3342951462 scopus 로고    scopus 로고
    • Isolation and characterisation of GTF21RD2, a novel fusion gene and member of the TFII-I family of transcription factors, deleted in Williams-Beuren syndrome
    • DOI 10.1038/sj.ejhg.5201174
    • Tipney, H. J., Hinsley, T. A., Brass, A., Metcalfe, K. et al., Isolation and characterisation of GTF2IRD2, a novel fusion gene and member of the TFII-I family of transcription factors, deleted in Williams-Beuren syndrome. Eur. J. Hum. Genet. 2004, 12, 551-560. (Pubitemid 39077163)
    • (2004) European Journal of Human Genetics , vol.12 , Issue.7 , pp. 551-560
    • Tipney, H.J.1    Hinsley, T.A.2    Brass, A.3    Metcalfe, K.4    Donai, D.5    Tassabehji, M.6
  • 38
    • 0034749352 scopus 로고    scopus 로고
    • Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein
    • Hino, S., Kishida, S., Michiue, T., Fukui, A. et al., Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein. Mol. Cell. Biol. 2001, 21, 330-342.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 330-342
    • Hino, S.1    Kishida, S.2    Michiue, T.3    Fukui, A.4
  • 39
    • 33744524659 scopus 로고    scopus 로고
    • FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region
    • Assmann, E. M., Alborghetti, M. R., Camargo, M. E., Kobarg, J., FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region. J. Biol. Chem. 2006, 281, 9869-9881.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9869-9881
    • Assmann, E.M.1    Alborghetti, M.R.2    Camargo, M.E.3    Kobarg, J.4


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