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Volumn 11, Issue 6, 2012, Pages 3175-3185

Comprehensive identification of substrates for f-box proteins by differential proteomics analysis

Author keywords

differential proteomics; F box protein; substrate identification; ubiquitin ligase

Indexed keywords

BETA ACTIN; F BOX PROTEIN; FBXL5 PROTEIN; FBXW7ALPHA PROTEIN; HEAT SHOCK PROTEIN 90; KRUPPEL LIKE FACTOR 5; MYC PROTEIN; NOTCH RECEPTOR; PROTEIN C JUN; PROTEIN P27; S PHASE KINASE ASSOCIATED PROTEIN 2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; PROTEIN BINDING; UBIQUITINATED PROTEIN;

EID: 84861833034     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr201216u     Document Type: Article
Times cited : (28)

References (42)
  • 1
    • 0005791934 scopus 로고
    • Memoire sur la Diastase, les Principaux Produits de ses Reactions, et leurs Applications aux arts Industriels
    • Payen, A.; Persoz, J. F. Memoire sur la Diastase, les Principaux Produits de ses Reactions, et leurs Applications aux arts Industriels Ann. Chim. (Phys.) 1833, 53, 73-92
    • (1833) Ann. Chim. (Phys.) , vol.53 , pp. 73-92
    • Payen, A.1    Persoz, J.F.2
  • 2
    • 0009502136 scopus 로고
    • Über die enzymatische Aufspaltung der Kreatinphosphorsäure; Zugleich ein Beitrag zum Chemismus der Muskelkontraktion
    • Lohmann, K. Über die enzymatische Aufspaltung der Kreatinphosphorsäure; zugleich ein Beitrag zum Chemismus der Muskelkontraktion Biochem. Z 1934, 271, 264-277
    • (1934) Biochem. Z , vol.271 , pp. 264-277
    • Lohmann, K.1
  • 3
    • 0029033504 scopus 로고
    • Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast
    • Irniger, S.; Piatti, S.; Michaelis, C.; Nasmyth, K. Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast Cell 1995, 81 (2) 269-278
    • (1995) Cell , vol.81 , Issue.2 , pp. 269-278
    • Irniger, S.1    Piatti, S.2    Michaelis, C.3    Nasmyth, K.4
  • 4
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B
    • King, R. W.; Peters, J. M.; Tugendreich, S.; Rolfe, M.; Hieter, P.; Kirschner, M. W. A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B Cell 1995, 81 (2) 279-288
    • (1995) Cell , vol.81 , Issue.2 , pp. 279-288
    • King, R.W.1    Peters, J.M.2    Tugendreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.W.6
  • 5
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis
    • Sudakin, V.; Ganoth, D.; Dahan, A.; Heller, H.; Hershko, J.; Luca, F. C.; Ruderman, J. V.; Hershko, A. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis Mol. Biol. Cell 1995, 6 (2) 185-197
    • (1995) Mol. Biol. Cell , vol.6 , Issue.2 , pp. 185-197
    • Sudakin, V.1    Ganoth, D.2    Dahan, A.3    Heller, H.4    Hershko, J.5    Luca, F.C.6    Ruderman, J.V.7    Hershko, A.8
  • 6
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning, G.; Whyte, D. B.; Martinez, R.; Hunter, T.; Sudarsanam, S. The protein kinase complement of the human genome Science 2002, 298 (5600) 1912-1934
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 7
    • 0037673562 scopus 로고    scopus 로고
    • The comparative proteomics of ubiquitination in mouse
    • Semple, C. A. The comparative proteomics of ubiquitination in mouse Genome Res. 2003, 13 (6B) 1389-1394
    • (2003) Genome Res. , vol.13 , Issue.6 , pp. 1389-1394
    • Semple, C.A.1
  • 9
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cell-cycle control and cancer
    • Nakayama, K. I.; Nakayama, K. Ubiquitin ligases: Cell-cycle control and cancer Nat. Rev. Cancer 2006, 6 (5) 369-381
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.5 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 10
    • 38549086019 scopus 로고    scopus 로고
    • FBW7 ubiquitin ligase: A tumour suppressor at the crossroads of cell division, growth and differentiation
    • Welcker, M.; Clurman, B. E. FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation Nat. Rev. Cancer 2008, 8 (2) 83-93
    • (2008) Nat. Rev. Cancer , vol.8 , Issue.2 , pp. 83-93
    • Welcker, M.1    Clurman, B.E.2
  • 11
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: Tipping the scales of cancer
    • Frescas, D.; Pagano, M. Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: Tipping the scales of cancer Nat. Rev. Cancer 2008, 8 (6) 438-449
    • (2008) Nat. Rev. Cancer , vol.8 , Issue.6 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 12
  • 13
    • 3142708002 scopus 로고    scopus 로고
    • An SCF-like ubiquitin ligase complex that controls presynaptic differentiation
    • Liao, E. H.; Hung, W.; Abrams, B.; Zhen, M. An SCF-like ubiquitin ligase complex that controls presynaptic differentiation Nature 2004, 430 (6997) 345-350
    • (2004) Nature , vol.430 , Issue.6997 , pp. 345-350
    • Liao, E.H.1    Hung, W.2    Abrams, B.3    Zhen, M.4
  • 14
    • 67650088235 scopus 로고    scopus 로고
    • Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal development
    • Saiga, T.; Fukuda, T.; Matsumoto, M.; Tada, H.; Okano, H. J.; Okano, H.; Nakayama, K. I. Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal development Mol. Cell. Biol. 2009, 29 (13) 3529-3543
    • (2009) Mol. Cell. Biol. , vol.29 , Issue.13 , pp. 3529-3543
    • Saiga, T.1    Fukuda, T.2    Matsumoto, M.3    Tada, H.4    Okano, H.J.5    Okano, H.6    Nakayama, K.I.7
  • 15
    • 67349209553 scopus 로고    scopus 로고
    • Survival of the flexible: Hormonal growth control and adaptation in plant development
    • Wolters, H.; Jurgens, G. Survival of the flexible: hormonal growth control and adaptation in plant development Nat. Rev. Genet. 2009, 10 (5) 305-317
    • (2009) Nat. Rev. Genet. , vol.10 , Issue.5 , pp. 305-317
    • Wolters, H.1    Jurgens, G.2
  • 17
    • 34249097203 scopus 로고    scopus 로고
    • Circadian mutant Overtime reveals F-box protein FBXL3 regulation of cryptochrome and period gene expression
    • Siepka, S. M.; Yoo, S. H.; Park, J.; Song, W.; Kumar, V.; Hu, Y.; Lee, C.; Takahashi, J. S. Circadian mutant Overtime reveals F-box protein FBXL3 regulation of cryptochrome and period gene expression Cell 2007, 129 (5) 1011-1023
    • (2007) Cell , vol.129 , Issue.5 , pp. 1011-1023
    • Siepka, S.M.1    Yoo, S.H.2    Park, J.3    Song, W.4    Kumar, V.5    Hu, Y.6    Lee, C.7    Takahashi, J.S.8
  • 19
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
    • Albritton, L. M.; Tseng, L.; Scadden, D.; Cunningham, J. M. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection Cell 1989, 57 (4) 659-666
    • (1989) Cell , vol.57 , Issue.4 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3    Cunningham, J.M.4
  • 25
    • 10644276385 scopus 로고    scopus 로고
    • VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
    • Kamura, T.; Maenaka, K.; Kotoshiba, S.; Matsumoto, M.; Kohda, D.; Conaway, R. C.; Conaway, J. W.; Nakayama, K. I. VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases Genes Dev. 2004, 18 (24) 3055-3065
    • (2004) Genes Dev. , vol.18 , Issue.24 , pp. 3055-3065
    • Kamura, T.1    Maenaka, K.2    Kotoshiba, S.3    Matsumoto, M.4    Kohda, D.5    Conaway, R.C.6    Conaway, J.W.7    Nakayama, K.I.8
  • 26
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E.; Blagoev, B.; Kratchmarova, I.; Kristensen, D. B.; Steen, H.; Pandey, A.; Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 2002, 1 (5) 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 27
    • 70350576223 scopus 로고    scopus 로고
    • An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
    • Salahudeen, A. A.; Thompson, J. W.; Ruiz, J. C.; Ma, H. W.; Kinch, L. N.; Li, Q.; Grishin, N. V.; Bruick, R. K. An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis Science 2009, 326 (5953) 722-726
    • (2009) Science , vol.326 , Issue.5953 , pp. 722-726
    • Salahudeen, A.A.1    Thompson, J.W.2    Ruiz, J.C.3    Ma, H.W.4    Kinch, L.N.5    Li, Q.6    Grishin, N.V.7    Bruick, R.K.8
  • 29
    • 36549071481 scopus 로고    scopus 로고
    • Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis
    • Onoyama, I.; Tsunematsu, R.; Matsumoto, A.; Kimura, T.; de Alboran, I. M.; Nakayama, K.; Nakayama, K. I. Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis J. Exp. Med. 2007, 204 (12) 2875-2888
    • (2007) J. Exp. Med. , vol.204 , Issue.12 , pp. 2875-2888
    • Onoyama, I.1    Tsunematsu, R.2    Matsumoto, A.3    Kimura, T.4    De Alboran, I.M.5    Nakayama, K.6    Nakayama, K.I.7
  • 30
    • 77953310667 scopus 로고    scopus 로고
    • The Fbw7/human CDC4 tumor suppressor targets proproliferative factor KLF5 for ubiquitination and degradation through multiple phosphodegron motifs
    • Liu, N.; Li, H.; Li, S.; Shen, M.; Xiao, N.; Chen, Y.; Wang, Y.; Wang, W.; Wang, R.; Wang, Q.; Sun, J.; Wang, P. The Fbw7/human CDC4 tumor suppressor targets proproliferative factor KLF5 for ubiquitination and degradation through multiple phosphodegron motifs J. Biol. Chem. 2010, 285 (24) 18858-18867
    • (2010) J. Biol. Chem. , vol.285 , Issue.24 , pp. 18858-18867
    • Liu, N.1    Li, H.2    Li, S.3    Shen, M.4    Xiao, N.5    Chen, Y.6    Wang, Y.7    Wang, W.8    Wang, R.9    Wang, Q.10    Sun, J.11    Wang, P.12
  • 31
    • 77953158826 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor targets KLF5 for ubiquitin-mediated degradation and suppresses breast cell proliferation
    • Zhao, D.; Zheng, H. Q.; Zhou, Z.; Chen, C. The Fbw7 tumor suppressor targets KLF5 for ubiquitin-mediated degradation and suppresses breast cell proliferation Cancer Res. 2010, 70 (11) 4728-4738
    • (2010) Cancer Res. , vol.70 , Issue.11 , pp. 4728-4738
    • Zhao, D.1    Zheng, H.Q.2    Zhou, Z.3    Chen, C.4
  • 34
    • 80052698326 scopus 로고    scopus 로고
    • The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo
    • Moroishi, T.; Nishiyama, M.; Takeda, Y.; Iwai, K.; Nakayama, K. I. The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo Cell Metab. 2011, 14 (3) 339-351
    • (2011) Cell Metab. , vol.14 , Issue.3 , pp. 339-351
    • Moroishi, T.1    Nishiyama, M.2    Takeda, Y.3    Iwai, K.4    Nakayama, K.I.5
  • 35
    • 55849133733 scopus 로고    scopus 로고
    • Identification of SCF ubiquitin ligase substrates by global protein stability profiling
    • Yen, H. C.; Elledge, S. J. Identification of SCF ubiquitin ligase substrates by global protein stability profiling Science 2008, 322 (5903) 923-929
    • (2008) Science , vol.322 , Issue.5903 , pp. 923-929
    • Yen, H.C.1    Elledge, S.J.2
  • 36
    • 62449196769 scopus 로고    scopus 로고
    • Large-scale detection of ubiquitination substrates using cell extracts and protein microarrays
    • Merbl, Y.; Kirschner, M. W. Large-scale detection of ubiquitination substrates using cell extracts and protein microarrays Proc. Natl. Acad. Sci. U.S.A. 2009, 106 (8) 2543-2548
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.8 , pp. 2543-2548
    • Merbl, Y.1    Kirschner, M.W.2
  • 37
    • 70649083505 scopus 로고    scopus 로고
    • A label-free quantitative proteomics strategy to identify E3 ubiquitin ligase substrates targeted to proteasome degradation
    • Burande, C. F.; Heuze, M. L.; Lamsoul, I.; Monsarrat, B.; Uttenweiler-Joseph, S.; Lutz, P. G. A label-free quantitative proteomics strategy to identify E3 ubiquitin ligase substrates targeted to proteasome degradation Mol. Cell Proteomics 2009, 8 (7) 1719-1727
    • (2009) Mol. Cell Proteomics , vol.8 , Issue.7 , pp. 1719-1727
    • Burande, C.F.1    Heuze, M.L.2    Lamsoul, I.3    Monsarrat, B.4    Uttenweiler-Joseph, S.5    Lutz, P.G.6
  • 42
    • 79953899846 scopus 로고    scopus 로고
    • Fbxw7-dependent degradation of Notch is required for control of 'stemness' and neuronal-glial differentiation in neural stem cells
    • Matsumoto, A.; Onoyama, I.; Sunabori, T.; Kageyama, R.; Okano, H.; Nakayama, K. I. Fbxw7-dependent degradation of Notch is required for control of â€stemness' and neuronal-glial differentiation in neural stem cells J. Biol. Chem. 2011, 286 (15) 13754-13764
    • (2011) J. Biol. Chem. , vol.286 , Issue.15 , pp. 13754-13764
    • Matsumoto, A.1    Onoyama, I.2    Sunabori, T.3    Kageyama, R.4    Okano, H.5    Nakayama, K.I.6


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