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Volumn 6, Issue , 2015, Pages

Ubiquitination of the Dishevelled DIX domain blocks its head-to-tail polymerization

Author keywords

[No Author keywords available]

Indexed keywords

DISHEVELLED 2; LYSINE; DISHEVELLED PROTEIN; DVL2 PROTEIN, HUMAN; PHOSPHOPROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TUMOR SUPPRESSOR PROTEIN;

EID: 84928604958     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7718     Document Type: Article
Times cited : (52)

References (48)
  • 1
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling and disease
    • Clevers, H. & Nusse, R. Wnt/beta-catenin signaling and disease. Cell 149, 1192-1205 (2012
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 2
    • 84861699364 scopus 로고    scopus 로고
    • The adenomatous polyposis coli tumour suppressor is essential for axin complex assembly and function and opposes axin's interaction with dishevelled
    • Mendoza-Topaz, C., Mieszczanek, J. & Bienz, M. The Adenomatous polyposis coli tumour suppressor is essential for Axin complex assembly and function and opposes Axin's interaction with Dishevelled. Open Biol. 1, 110013 (2011
    • (2011) Open Biol , vol.1 , pp. 110013
    • Mendoza-Topaz, C.1    Mieszczanek, J.2    Bienz, M.3
  • 3
    • 67650230896 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling: Components, mechanisms, and diseases
    • MacDonald, B. T., Tamai, K. & He, X. Wnt/beta-catenin signaling: components, mechanisms, and diseases. Dev. Cell 17, 9-26 (2009
    • (2009) Dev. Cell , vol.17 , pp. 9-26
    • Macdonald, B.T.1    Tamai, K.2    He, X.3
  • 4
    • 34250827150 scopus 로고    scopus 로고
    • Wnt induces lrp6 signalosomes and promotes dishevelleddependent lrp6 phosphorylation
    • Bilic, J. et al. Wnt induces LRP6 signalosomes and promotes dishevelleddependent LRP6 phosphorylation. Science 316, 1619-1622 (2007
    • (2007) Science , vol.316 , pp. 1619-1622
    • Bilic, J.1
  • 5
    • 34249890531 scopus 로고    scopus 로고
    • The dix domain of dishevelled confers wnt signaling by dynamic polymerization
    • Schwarz-Romond, T. et al. The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization. Nature Struct. Mol. Biol. 14, 484-492 (2007
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 484-492
    • Schwarz-Romond, T.1
  • 6
    • 84918528755 scopus 로고    scopus 로고
    • Signalosome assembly by domains undergoing dynamic head-to-tail polymerization
    • Bienz, M. Signalosome assembly by domains undergoing dynamic head-to-tail polymerization. Trends Biochem. Sci. 39, 487-495 (2014
    • (2014) Trends Biochem. Sci , vol.39 , pp. 487-495
    • Bienz, M.1
  • 7
    • 79952148045 scopus 로고    scopus 로고
    • Dishevelled interacts with the dix domain polymerization interface of axin to interfere with its function in down-regulating b-catenin
    • Fiedler, M., Mendoza-Topaz, C., Rutherford, T. J., Mieszczanek, J. & Bienz, M. Dishevelled interacts with the DIX domain polymerization interface of Axin to interfere with its function in down-regulating b-catenin. Proc. Natl Acad. Sci. USA 108, 1937-1942 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 1937-1942
    • Fiedler, M.1    Mendoza-Topaz, C.2    Rutherford, T.J.3    Mieszczanek, J.4    Bienz, M.5
  • 8
    • 0037513408 scopus 로고    scopus 로고
    • A role of dishevelled in relocating axin to the plasma membrane during wingless signaling
    • Cliffe, A., Hamada, F. & Bienz, M. A role of Dishevelled in relocating Axin to the plasma membrane during wingless signaling. Curr. Biol. 13, 960-966 (2003
    • (2003) Curr. Biol , vol.13 , pp. 960-966
    • Cliffe, A.1    Hamada, F.2    Bienz, M.3
  • 9
    • 84898749421 scopus 로고    scopus 로고
    • Structural basis of gsk-3 inhibition by n-terminal phosphorylation and by the wnt receptor lrp6
    • Stamos, J. L., Chu, M. L., Enos, M. D., Shah, N. &Weis, W. I. Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6. eLife 3, e01998 (2014
    • (2014) ELife , vol.3 , pp. e01998
    • Stamos, J.L.1    Chu, M.L.2    Enos, M.D.3    Shah, N.4    Weis, W.I.5
  • 10
    • 33845355511 scopus 로고    scopus 로고
    • Diversity of lef/tcf action in development and disease
    • Arce, L., Yokoyama, N. N. & Waterman, M. L. Diversity of LEF/TCF action in development and disease. Oncogene 25, 7492-7504 (2006
    • (2006) Oncogene , vol.25 , pp. 7492-7504
    • Arce, L.1    Yokoyama, N.N.2    Waterman, M.L.3
  • 11
    • 79953155959 scopus 로고    scopus 로고
    • Molecular basis of wnt activation via the dix domain protein ccd1
    • Liu, Y. T. et al. Molecular basis of Wnt activation via the DIX domain protein Ccd1. J. Biol. Chem. 286, 8597-8608 (2011
    • (2011) J. Biol. Chem , vol.286 , pp. 8597-8608
    • Liu, Y.T.1
  • 12
    • 29244462476 scopus 로고    scopus 로고
    • The wnt signalling effector dishevelled forms dynamic protein assemblies rather than stable associations with cytoplasmic vesicles
    • Schwarz-Romond, T., Merrifield, C., Nichols, B. J. & Bienz, M. The Wnt signalling effector Dishevelled forms dynamic protein assemblies rather than stable associations with cytoplasmic vesicles. J. Cell Sci. 118, 5269-5277 (2005
    • (2005) J. Cell Sci , vol.118 , pp. 5269-5277
    • Schwarz-Romond, T.1    Merrifield, C.2    Nichols, B.J.3    Bienz, M.4
  • 14
    • 84897128080 scopus 로고    scopus 로고
    • Huwe1-mediated ubiquitylation of dishevelled defines a negative feedback loop in the wnt signaling pathway
    • de Groot, R. E. et al. Huwe1-mediated ubiquitylation of dishevelled defines a negative feedback loop in the Wnt signaling pathway. Sci. Signal. 7, ra26 (2014
    • (2014) Sci. Signal , vol.7 , pp. ra26
    • De Groot, R.E.1
  • 15
    • 77649259009 scopus 로고    scopus 로고
    • Loss of the tumor suppressor cyld enhances wnt/bcatenin signaling through k63-linked ubiquitination of dvl
    • Tauriello, D. V. et al. Loss of the tumor suppressor CYLD enhances Wnt/bcatenin signaling through K63-linked ubiquitination of Dvl. Mol. Cell 37, 607-619 (2010
    • (2010) Mol. Cell , vol.37 , pp. 607-619
    • Tauriello, D.V.1
  • 16
    • 84883185607 scopus 로고    scopus 로고
    • Deubiquitination of dishevelled by usp14 is required for wnt signaling
    • Jung, H. et al. Deubiquitination of Dishevelled by Usp14 is required for Wnt signaling. Oncogenesis 2, e64 (2013
    • (2013) Oncogenesis , vol.2 , pp. e64
    • Jung, H.1
  • 17
    • 84555218153 scopus 로고    scopus 로고
    • The differential modulation of usp activity by internal regulatory domains, interactors and eight ubiquitin chain types
    • Faesen, A. C. et al. The differential modulation of USP activity by internal regulatory domains, interactors and eight ubiquitin chain types. Chem. Biol. 18, 1550-1561 (2011
    • (2011) Chem. Biol , vol.18 , pp. 1550-1561
    • Faesen, A.C.1
  • 18
    • 39549106692 scopus 로고    scopus 로고
    • The structure of the cyld usp domain explains its specificity for lys63-linked polyubiquitin and reveals a b box module
    • Komander, D. et al. The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol. Cell 29, 451-464 (2008
    • (2008) Mol. Cell , vol.29 , pp. 451-464
    • Komander, D.1
  • 19
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals lys29-isopeptide specificity of an otu deubiquitinase
    • Virdee, S., Ye, Y., Nguyen, D. P., Komander, D. & Chin, J. W. Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase. Nat. Chem. Biol. 6, 750-757 (2010
    • (2010) Nat. Chem. Biol , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 20
    • 80455123843 scopus 로고    scopus 로고
    • Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme
    • Castaneda, C. et al. Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme. J. Am. Chem. Soc. 133, 17855-17868 (2011
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 17855-17868
    • Castaneda, C.1
  • 21
    • 84902207255 scopus 로고    scopus 로고
    • Nonenzymatic rubylation and ubiquitination of proteins for structural and functional studies
    • Singh, R. K., Sundar, A. & Fushman, D. Nonenzymatic rubylation and ubiquitination of proteins for structural and functional studies. Angew. Chem. Int. Ed. Engl. 53, 6120-6125 (2014
    • (2014) Angew. Chem. Int. Ed. Engl , vol.53 , pp. 6120-6125
    • Singh, R.K.1    Sundar, A.2    Fushman, D.3
  • 22
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase cezanne
    • Bremm, A., Freund, S. M. & Komander, D. Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nature Struct. Mol. Biol. 17, 939-947 (2010
    • (2010) Nature Struct. Mol. Biol , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.2    Komander, D.3
  • 23
    • 0033397158 scopus 로고    scopus 로고
    • Polypeptide synthesis by the thioester method
    • Aimoto, S. Polypeptide synthesis by the thioester method. Biopolymers 51, 247-265 (1999
    • (1999) Biopolymers , vol.51 , pp. 247-265
    • Aimoto, S.1
  • 25
    • 33748620928 scopus 로고    scopus 로고
    • Ruthenium-induced allylcarbamate cleavage in living cells
    • Streu, C. & Meggers, E. Ruthenium-induced allylcarbamate cleavage in living cells. Angew. Chem. Int. Ed. Engl. 45, 5645-5648 (2006
    • (2006) Angew. Chem. Int. Ed. Engl , vol.45 , pp. 5645-5648
    • Streu, C.1    Meggers, E.2
  • 26
    • 77954903507 scopus 로고    scopus 로고
    • Balanced ubiquitylation and deubiquitylation of frizzled regulate cellular responsiveness to wg/wnt
    • Mukai, A. et al. Balanced ubiquitylation and deubiquitylation of Frizzled regulate cellular responsiveness to Wg/Wnt. EMBO J. 29, 2114-2125 (2010
    • (2010) EMBO J , vol.29 , pp. 2114-2125
    • Mukai, A.1
  • 27
    • 39449084931 scopus 로고    scopus 로고
    • Trabid a new positive regulator of wnt-induced transcription with preference for binding and cleaving k63-linked ubiquitin chains
    • Tran, H., Hamada, F., Schwarz-Romond, T. & Bienz, M. Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains. Genes Dev. 22, 528-542 (2008
    • (2008) Genes Dev , vol.22 , pp. 528-542
    • Tran, H.1    Hamada, F.2    Schwarz-Romond, T.3    Bienz, M.4
  • 28
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent lys 63-linked and linear polyubiquitin chains
    • Komander, D. et al. Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep. 10, 466-473 (2009
    • (2009) EMBO Rep , vol.10 , pp. 466-473
    • Komander, D.1
  • 29
    • 84878832998 scopus 로고    scopus 로고
    • Otu deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis
    • Mevissen, T. E. et al. OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis. Cell 154, 169-184 (2013
    • (2013) Cell , vol.154 , pp. 169-184
    • Mevissen, T.E.1
  • 30
    • 50349102579 scopus 로고    scopus 로고
    • Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase t
    • Reyes-Turcu, F. E., Shanks, J. R., Komander, D. &Wilkinson, K. D. Recognition of polyubiquitin isoforms by the multiple ubiquitin binding modules of isopeptidase T. J. Biol. Chem. 283, 19581-19592 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 19581-19592
    • Reyes-Turcu, F.E.1    Shanks, J.R.2    Komander, D.3    Wilkinson, K.D.4
  • 31
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of usp14
    • Lee, B. H. et al. Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184 (2010
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1
  • 32
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • Lee, M. J., Lee, B. H., Hanna, J., King, R. W. & Finley, D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell. Proteomics 10, R110.003871 (2011
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. R110003871
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 33
    • 84859142134 scopus 로고    scopus 로고
    • Semisynthetic, site-specific ubiquitin modification of a-synuclein reveals differential effects on aggregation
    • Meier, F. et al. Semisynthetic, site-specific ubiquitin modification of a-synuclein reveals differential effects on aggregation. J. Am. Chem. Soc. 134, 5468-5471 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 5468-5471
    • Meier, F.1
  • 34
    • 78650866766 scopus 로고    scopus 로고
    • Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated a-synuclein
    • Hejjaoui, M., Haj-Yahya, M., Kumar, K. S., Brik, A. & Lashuel, H. A. Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated a-synuclein. Angew. Chem. Int. Ed. Engl. 50, 405-409 (2011
    • (2011) Angew. Chem. Int. Ed. Engl , vol.50 , pp. 405-409
    • Hejjaoui, M.1    Haj-Yahya, M.2    Kumar, K.S.3    Brik, A.4    Lashuel, H.A.5
  • 35
    • 84887102319 scopus 로고    scopus 로고
    • Synthetic polyubiquitinated a-synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology
    • Haj-Yahya, M. et al. Synthetic polyubiquitinated a-synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology. Proc. Natl Acad. Sci. USA 110, 17726-17731 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 17726-17731
    • Haj-Yahya, M.1
  • 36
    • 84893848639 scopus 로고    scopus 로고
    • Cyld regulates spindle orientation by stabilizing astral microtubules and promoting dishevelled-numa-dynein/dynactin complex formation
    • Yang, Y. et al. CYLD regulates spindle orientation by stabilizing astral microtubules and promoting dishevelled-NuMA-dynein/dynactin complex formation. Proc. Natl Acad. Sci. USA 111, 2158-2163 (2014
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 2158-2163
    • Yang, Y.1
  • 37
    • 84883740585 scopus 로고    scopus 로고
    • E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of otub1
    • Wiener, R. et al. E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of OTUB1. Nature Struct. Mol. Biol. 20, 1033-1039 (2013
    • (2013) Nature Struct. Mol. Biol , vol.20 , pp. 1033-1039
    • Wiener, R.1
  • 38
    • 52149103164 scopus 로고    scopus 로고
    • Structural basis for specific cleavage of lys 63-linked polyubiquitin chains
    • Sato, Y. et al. Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains. Nature 455, 358-362 (2008
    • (2008) Nature , vol.455 , pp. 358-362
    • Sato, Y.1
  • 39
    • 84878862687 scopus 로고    scopus 로고
    • Otulin antagonizes lubac signaling by specifically hydrolyzing met1-linked polyubiquitin
    • Keusekotten, K. et al. OTULIN antagonizes LUBAC signaling by specifically hydrolyzing Met1-linked polyubiquitin. Cell 153, 1312-1326 (2013
    • (2013) Cell , vol.153 , pp. 1312-1326
    • Keusekotten, K.1
  • 40
    • 84879834151 scopus 로고    scopus 로고
    • Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains
    • Castaneda, C. A., Kashyap, T. R., Nakasone, M. A., Krueger, S. & Fushman, D. Unique structural, dynamical, and functional properties of K11-linked polyubiquitin chains. Structure 21, 1168-1181 (2013
    • (2013) Structure , vol.21 , pp. 1168-1181
    • Castaneda, C.A.1    Kashyap, T.R.2    Nakasone, M.A.3    Krueger, S.4    Fushman, D.5
  • 41
    • 23044484731 scopus 로고    scopus 로고
    • Various strategies of using residual dipolar couplings in nmr-driven protein docking: Application to lys48-linked di-ubiquitin and validation against 15n-relaxation data
    • van Dijk, A. D., Fushman, D. & Bonvin, A. M. Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data. Proteins 60, 367-381 (2005
    • (2005) Proteins , vol.60 , pp. 367-381
    • Van Dijk, A.D.1    Fushman, D.2    Bonvin, A.M.3
  • 42
    • 44849100496 scopus 로고    scopus 로고
    • Chemically ubiquitylated histone h2b stimulates hdot1l-mediated intranucleosomal methylation
    • McGinty, R. K., Kim, J., Chatterjee, C., Roeder, R. G. & Muir, T. W. Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 453, 812-816 (2008
    • (2008) Nature , vol.453 , pp. 812-816
    • McGinty, R.K.1    Kim, J.2    Chatterjee, C.3    Roeder, R.G.4    Muir, T.W.5
  • 43
    • 77951241293 scopus 로고    scopus 로고
    • Chemical approaches for studying histone modifications
    • Chatterjee, C. & Muir, T. W. Chemical approaches for studying histone modifications. J. Biol. Chem. 285, 11045-11050 (2010
    • (2010) J. Biol. Chem , vol.285 , pp. 11045-11050
    • Chatterjee, C.1    Muir, T.W.2
  • 44
    • 78751515133 scopus 로고    scopus 로고
    • Histone h2b ubiquitylation disrupts local and higher-order chromatin compaction
    • Fierz, B. et al. Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction. Nat. Chem. Biol. 7, 113-119 (2011
    • (2011) Nat. Chem. Biol , vol.7 , pp. 113-119
    • Fierz, B.1
  • 45
    • 77949875253 scopus 로고    scopus 로고
    • Chemically ubiquitylated pcna as a probe for eukaryotic translesion dna synthesis
    • Chen, J., Ai, Y., Wang, J., Haracska, L. & Zhuang, Z. Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis. Nat. Chem. Biol. 6, 270-272 (2010
    • (2010) Nat. Chem. Biol , vol.6 , pp. 270-272
    • Chen, J.1    Ai, Y.2    Wang, J.3    Haracska, L.4    Zhuang, Z.5
  • 46
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding ne-acetyllysine in recombinant proteins
    • Neumann, H., Peak-Chew, S. Y. & Chin, J. W. Genetically encoding Ne-acetyllysine in recombinant proteins. Nat. Chem. Biol. 4, 232-234 (2008
    • (2008) Nat. Chem. Biol , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 47
    • 43449132666 scopus 로고    scopus 로고
    • Decoding of methylated histone h3 tail by the pygo-bcl9 wnt signaling complex
    • Fiedler, M. et al. Decoding of methylated histone H3 tail by the Pygo-BCL9 Wnt signaling complex. Mol. Cell 30, 507-518 (2008
    • (2008) Mol. Cell , vol.30 , pp. 507-518
    • Fiedler, M.1
  • 48
    • 84907358982 scopus 로고    scopus 로고
    • Screening of dub activity and specificity by maldi-tof mass spectrometry
    • Ritorto, M. S. et al. Screening of DUB activity and specificity by MALDI-TOF mass spectrometry. Nat. Commun. 5, 4763 (2014).
    • (2014) Nat. Commun , vol.5 , pp. 4763
    • Ritorto, M.S.1


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