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Volumn 8, Issue 7, 2013, Pages 1449-1458

Selective monitoring of ubiquitin signals with genetically encoded ubiquitin chain-specific sensors

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; GREEN FLUORESCENT PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TUMOR NECROSIS FACTOR; UBIQUITIN;

EID: 84904686159     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2013.089     Document Type: Article
Times cited : (10)

References (46)
  • 2
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • Ikeda, F. & Dikic, I. Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series. EMBO Rep. 9, 536-542 (2008).
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 3
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: A new regulator of NF-B activation
    • Iwai, K. & Tokunaga, F. Linear polyubiquitination: a new regulator of NF-B activation. EMBO Rep. 10, 706-713 (2009).
    • (2009) EMBO Rep , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 4
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513 (2009).
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 5
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich, H.D. & Walden, H. Ubiquitin signalling in DNA replication and repair. Nat. Rev. Mol. Cell Biol. 11, 479-489 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 6
    • 80755132190 scopus 로고    scopus 로고
    • Endosomal transport via ubiquitination
    • Piper, R.C. & Lehner, P.J. Endosomal transport via ubiquitination. Trends Cell Biol. 21, 647-655 (2011).
    • (2011) Trends Cell Biol , vol.21 , pp. 647-655
    • Piper, R.C.1    Lehner, P.J.2
  • 7
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions
    • Husnjak, K. & Dikic, I. Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu. Rev. Biochem. 81, 291-322 (2012).
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 8
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains - From structures to functions
    • Dikic, I., Wakatsuki, S. & Walters, K.J. Ubiquitin-binding domains - from structures to functions. Nat. Rev. Mol. Cell Biol. 10, 659-671 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 9
    • 84860427832 scopus 로고    scopus 로고
    • Ubiquitin and its binding domains
    • Randles, L. & Walters, K.J. Ubiquitin and its binding domains. Front. Biosci. 17, 2140-2157 (2012).
    • (2012) Front. Biosci , vol.17 , pp. 2140-2157
    • Randles, L.1    Walters, K.J.2
  • 10
    • 71449095149 scopus 로고    scopus 로고
    • Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain
    • Kulathu, Y., Akutsu, M., Bremm, A., Hofmann, K. & Komander, D. Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain. Nat. Struct. Mol. Biol. 16, 1328-1330 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 1328-1330
    • Kulathu, Y.1    Akutsu, M.2    Bremm, A.3    Hofmann, K.4    Komander, D.5
  • 11
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-B activation
    • Rahighi, S. et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-B activation. Cell 136, 1098-1109 (2009).
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1
  • 12
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu, Y. & Komander, D. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat. Rev. Mol. Cell Biol. 13, 508-523 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 13
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P. et al. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137, 133-145 (2009).
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1
  • 14
    • 79955763306 scopus 로고    scopus 로고
    • Improved quantitative mass spectrometry methods for characterizing complex ubiquitin signals
    • M110 003756
    • Phu, L. et al. Improved quantitative mass spectrometry methods for characterizing complex ubiquitin signals. Mol. Cell Proteomics 10, M110 003756 (2011).
    • (2011) Mol. Cell Proteomics , vol.10
    • Phu, L.1
  • 15
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach, B. et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 471, 591-596 (2011).
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1
  • 16
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas, T.L. et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 36, 831-844 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1
  • 17
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-B activity and apoptosis
    • Ikeda, F. et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-B activity and apoptosis. Nature 471, 637-641 (2011).
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1
  • 18
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-B-activating linear ubiquitin chain assembly complex
    • Tokunaga, F. et al. SHARPIN is a component of the NF-B-activating linear ubiquitin chain assembly complex. Nature 471, 633-636 (2011).
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1
  • 20
    • 78751496279 scopus 로고    scopus 로고
    • Proteomic snapshot of the EGF-induced ubiquitin network
    • Argenzio, E. et al. Proteomic snapshot of the EGF-induced ubiquitin network. Mol. Syst. Biol. 7, 462 (2011).
    • (2011) Mol. Syst. Biol , vol.7 , pp. 462
    • Argenzio, E.1
  • 22
    • 23144452492 scopus 로고    scopus 로고
    • Weighing in on ubiquitin: The expanding role of mass-spectrometry-based proteomics
    • Kirkpatrick, D.S., Denison, C. & Gygi, S.P. Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics. Nat. Cell Biol. 7, 750-757 (2005).
    • (2005) Nat. Cell Biol , vol.7 , pp. 750-757
    • Kirkpatrick, D.S.1    Denison, C.2    Gygi, S.P.3
  • 23
    • 84867101049 scopus 로고    scopus 로고
    • Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass
    • Povlsen, L.K. et al. Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Nat. Cell Biol. 14, 1089-1098 (2012).
    • (2012) Nat. Cell Biol , vol.14 , pp. 1089-1098
    • Povlsen, L.K.1
  • 24
    • 84867103151 scopus 로고    scopus 로고
    • Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues
    • Wagner, S.A. et al. Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Mol. Cell Proteomics 11, 1578-1585 (2012).
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 1578-1585
    • Wagner, S.A.1
  • 25
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G., Paige, J.S. & Jaffrey, S.R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling. Nat. Biotechnol. 28, 868-873 (2010).
    • (2010) Nat. Biotechnol , vol.28 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 26
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • M111 013284
    • Wagner, S.A. et al. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol. Cell Proteomics 10, M111 013284 (2011).
    • (2011) Mol. Cell Proteomics , vol.10
    • Wagner, S.A.1
  • 27
    • 80054694510 scopus 로고    scopus 로고
    • Global identification of modular cullin-RING ligase substrates
    • Emanuele, M.J. et al. Global identification of modular cullin-RING ligase substrates. Cell 147, 459-474 (2011).
    • (2011) Cell , vol.147 , pp. 459-474
    • Emanuele, M.J.1
  • 28
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick, D.S., Gerber, S.A. & Gygi, S.P. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 35, 265-273 (2005).
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 29
    • 28844499047 scopus 로고    scopus 로고
    • Production of antipolyubiquitin monoclonal antibodies and their use for characterization and isolation of polyubiquitinated proteins
    • Fujimuro, M. & Yokosawa, H. Production of antipolyubiquitin monoclonal antibodies and their use for characterization and isolation of polyubiquitinated proteins. Methods Enzymol. 399, 75-86 (2005).
    • (2005) Methods Enzymol , vol.399 , pp. 75-86
    • Fujimuro, M.1    Yokosawa, H.2
  • 30
    • 77955516435 scopus 로고    scopus 로고
    • K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody
    • Matsumoto, M.L. et al. K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody. Mol. Cell 39, 477-484 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 477-484
    • Matsumoto, M.L.1
  • 31
    • 85080842087 scopus 로고    scopus 로고
    • Engineering and structural characterization of a linear-polyubiquitin- specific antibody
    • Matsumoto, M.L. et al. Engineering and structural characterization of a linear-polyubiquitin-specific antibody. J. Mol. Biol. 418, 144 (2011).
    • (2011) J. Mol. Biol , vol.418 , pp. 144
    • Matsumoto, M.L.1
  • 32
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • Newton, K. et al. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies. Cell 134, 668-678 (2008).
    • (2008) Cell , vol.134 , pp. 668-678
    • Newton, K.1
  • 33
    • 84861706639 scopus 로고    scopus 로고
    • A dual role for K63-linked ubiquitin chains in multivesicular body biogenesis and cargo sorting
    • Erpapazoglou, Z. et al. A dual role for K63-linked ubiquitin chains in multivesicular body biogenesis and cargo sorting. Mol. Biol. Cell 23, 2170-2183 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2170-2183
    • Erpapazoglou, Z.1
  • 34
    • 84866300942 scopus 로고    scopus 로고
    • Fluorescence-based sensors to monitor localization and functions of linear and K63-linked ubiquitin chains in cells
    • van Wijk, S.J. et al. Fluorescence-based sensors to monitor localization and functions of linear and K63-linked ubiquitin chains in cells. Mol. Cell 47, 797-809 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 797-809
    • Van Wijk, S.J.1
  • 35
    • 84857782898 scopus 로고    scopus 로고
    • Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling
    • Sims, J.J. et al. Polyubiquitin-sensor proteins reveal localization and linkage-type dependence of cellular ubiquitin signaling. Nat. Methods 9, 303-309 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 303-309
    • Sims, J.J.1
  • 36
    • 84875236362 scopus 로고    scopus 로고
    • Regulation of NF-B by ubiquitination
    • Chen, J. & Chen, Z.J. Regulation of NF-B by ubiquitination. Curr. Opin. Immunol. 25, 4-12 (2013).
    • (2013) Curr. Opin. Immunol , vol.25 , pp. 4-12
    • Chen, J.1    Chen, Z.J.2
  • 37
    • 79955484976 scopus 로고    scopus 로고
    • The spatial and temporal organization of ubiquitin networks
    • Grabbe, C., Husnjak, K. & Dikic, I. The spatial and temporal organization of ubiquitin networks. Nat. Rev. Mol. Cell Biol. 12, 295-307 (2011).
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 295-307
    • Grabbe, C.1    Husnjak, K.2    Dikic, I.3
  • 38
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild, P. et al. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science 333, 228-233 (2011).
    • (2011) Science , vol.333 , pp. 228-233
    • Wild, P.1
  • 39
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston, T.L., Ryzhakov, G., Bloor, S., von Muhlinen, N. & Randow, F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat. Immunol. 10, 1215-1221 (2009).
    • (2009) Nat. Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    Von Muhlinen, N.4    Randow, F.5
  • 40
    • 84871006349 scopus 로고    scopus 로고
    • The LRR and RING domain protein LRSAM1 is an E3 ligase crucial for ubiquitin-dependent autophagy of intracellular Salmonella Typhimurium
    • Huett, A. et al. The LRR and RING domain protein LRSAM1 is an E3 ligase crucial for ubiquitin-dependent autophagy of intracellular Salmonella Typhimurium. Cell Host Microbe 12, 778-790 (2012).
    • (2012) Cell Host Microbe , vol.12 , pp. 778-790
    • Huett, A.1
  • 41
    • 34248529801 scopus 로고    scopus 로고
    • Identification of host-induced pathogen genes by differential fluorescence induction reporter systems
    • Bumann, D. & Valdivia, R.H. Identification of host-induced pathogen genes by differential fluorescence induction reporter systems. Nat. Protoc. 2, 770-777 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 770-777
    • Bumann, D.1    Valdivia, R.H.2
  • 42
    • 80052476537 scopus 로고    scopus 로고
    • Shared and unique properties of ubiquitin and SUMO interaction networks in DNA repair
    • van Wijk, S.J., Muller, S. & Dikic, I. Shared and unique properties of ubiquitin and SUMO interaction networks in DNA repair. Genes Dev. 25, 1763-1769 (2011).
    • (2011) Genes Dev , vol.25 , pp. 1763-1769
    • Van Wijk, S.J.1    Muller, S.2    Dikic, I.3
  • 43
    • 79953163464 scopus 로고    scopus 로고
    • The Three Musketeers of autophagy: Phosphorylation, ubiquitylation and acetylation
    • McEwan, D.G. & Dikic, I. The Three Musketeers of autophagy: phosphorylation, ubiquitylation and acetylation. Trends Cell Biol. 21, 195-201 (2011).
    • (2011) Trends Cell Biol , vol.21 , pp. 195-201
    • McEwan, D.G.1    Dikic, I.2
  • 44
    • 77449102676 scopus 로고    scopus 로고
    • Modulation of protein properties in living cells using nanobodies
    • Kirchhofer, A. et al. Modulation of protein properties in living cells using nanobodies. Nat. Struct. Mol. Biol. 17, 133-138 (2010).
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 133-138
    • Kirchhofer, A.1
  • 45
    • 84859920287 scopus 로고    scopus 로고
    • Live-cell super-resolution imaging with synthetic fluorophores
    • van de Linde, S., Heilemann, M. & Sauer, M. Live-cell super-resolution imaging with synthetic fluorophores. Annu. Rev. Phys. Chem. 63, 519-540 (2012).
    • (2012) Annu. Rev. Phys. Chem , vol.63 , pp. 519-540
    • Van De Linde, S.1    Heilemann, M.2    Sauer, M.3
  • 46
    • 7444254365 scopus 로고    scopus 로고
    • Oscillations in NF-B signaling control the dynamics of gene expression
    • Nelson, D.E. et al. Oscillations in NF-B signaling control the dynamics of gene expression. Science 306, 704-708 (2004).
    • (2004) Science , vol.306 , pp. 704-708
    • Nelson, D.E.1


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