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Volumn 40, Issue 2, 2012, Pages 404-408

Structural insights into specificity and diversity in mechanisms of ubiquitin recognition by ubiquitin-binding domains

Author keywords

Atrogene; NMR spectroscopy; p62; Paget's disease of bone (PDB); Sequestosome 1 (SQSTM1); Ubiquitin associated domain (UBA domain)

Indexed keywords

PROTEIN P62; UBIQUITIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; ZINC FINGER PROTEIN 216;

EID: 84859318544     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20110729     Document Type: Review
Times cited : (17)

References (34)
  • 1
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander, D. (2009) The emerging complexity of protein ubiquitination. Biochem. Soc. Trans. 37, 937-953
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 3
    • 76649123968 scopus 로고    scopus 로고
    • Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding
    • Hagai, T. and Levy, Y. (2010) Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding. Proc. Natl. Acad. Sci. U.S.A. 107, 2001-2006
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2001-2006
    • Hagai, T.1    Levy, Y.2
  • 4
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains: From structures to functions
    • Dikic, I., Wakatsuki, S. and Walters, K.J. (2009) Ubiquitin-binding domains: from structures to functions. Nat. Rev. Mol. Cell Biol. 10, 659-671
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 5
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper, J.W. and Schulman, B.A. (2006) Structural complexity in ubiquitin recognition. Cell 124, 1133-1136
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, J.W.1    Schulman, B.A.2
  • 6
    • 75949107942 scopus 로고    scopus 로고
    • Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases ι and Rev1
    • Bomar, M.G., D'Souza, S., Bienko, M., Dikic, I., Walker, G.C. and Zhou, P. (2010) Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases ι and Rev1. Mol. Cell 37, 408-417
    • (2010) Mol. Cell , vol.37 , pp. 408-417
    • Bomar, M.G.1    D'Souza, S.2    Bienko, M.3    Dikic, I.4    Walker, G.C.5    Zhou, P.6
  • 7
    • 77953108542 scopus 로고    scopus 로고
    • The diversity of ubiquitin recognition: Hot spots and varied specificity
    • Winget, J.M. and Mayor, T. (2010) The diversity of ubiquitin recognition: hot spots and varied specificity. Mol. Cell 38, 627-635
    • (2010) Mol. Cell , vol.38 , pp. 627-635
    • Winget, J.M.1    Mayor, T.2
  • 8
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen, Z.J. and Sun, L.J. (2009) Nonproteolytic functions of ubiquitin in cell signaling. Mol. Cell 33, 275-286
    • (2009) Mol. Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 12
    • 32544444479 scopus 로고    scopus 로고
    • A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophy
    • DOI 10.1038/sj.emboj.7600945, PII 7600945
    • Hishiya, A., Iemura, S., Natsume, T., Takayama, S., Ikeda, K. and Watanabe, K. (2006) A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophy. EMBO J. 25, 554-564 (Pubitemid 43237662)
    • (2006) EMBO Journal , vol.25 , Issue.3 , pp. 554-564
    • Hishiya, A.1    Iemura, S.-I.2    Natsume, T.3    Takayama, S.4    Ikeda, K.5    Watanabe, K.6
  • 13
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker, S.H., Solomon, V., Mitch, W.E. and Goldberg, A.L. (1999) Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. 129, 227S-237S
    • (1999) J. Nutr. , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 14
    • 56449095862 scopus 로고    scopus 로고
    • The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy
    • Murton, A.J., Constantin, D. and Greenhaff, P.L. (2008) The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy. Biochim. Biophys. Acta 1782, 730-743
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 730-743
    • Murton, A.J.1    Constantin, D.2    Greenhaff, P.L.3
  • 16
    • 1942425971 scopus 로고    scopus 로고
    • ZNF216 Is an A20-like and IκB kinase γ-interacting inhibitor of NF-κB activation
    • Huang, J., Teng, L., Li, L., Liu, T., Li, L., Chen, D., Xu, L.G., Zhai, Z. and Shu, H.B. (2004) ZNF216 Is an A20-like and IκB kinase γ-interacting inhibitor of NF-κB activation. J. Biol. Chem. 279, 16847-16853
    • (2004) J. Biol. Chem. , vol.279 , pp. 16847-16853
    • Huang, J.1    Teng, L.2    Li, L.3    Liu, T.4    Li, L.5    Chen, D.6    Xu, L.G.7    Zhai, Z.8    Shu, H.B.9
  • 17
    • 33846240526 scopus 로고    scopus 로고
    • Sequestosome 1/p62 - More than just a scaffold
    • DOI 10.1016/j.febslet.2006.12.027, PII S0014579306014815
    • Seibenhener, M.L., Geetha, T. and Wooten, M.W. (2007) Sequestosome 1/p62: more than just a scaffold. FEBS Lett. 581, 175-179 (Pubitemid 46096472)
    • (2007) FEBS Letters , vol.581 , Issue.2 , pp. 175-179
    • Seibenhener, M.L.1    Geetha, T.2    Wooten, M.W.3
  • 19
    • 0034599476 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 channels NF-κB activation by the IL-1-TRAF6 pathway
    • Sanz, L., Diaz-Meco, M.T., Nakano, H. and Moscat, J. (2000) The atypical PKC-interacting protein p62 channels NF-κB activation by the IL-1-TRAF6 pathway. EMBO J. 19, 1576-1586 (Pubitemid 30182165)
    • (2000) EMBO Journal , vol.19 , Issue.7 , pp. 1576-1586
    • Sanz, L.1    Diaz-Meco, M.T.2    Nakano, H.3    Moscat, J.4
  • 20
    • 0033153320 scopus 로고    scopus 로고
    • The interaction of p62 with RIP links the atypical PKCs to NF-κB activation
    • DOI 10.1093/emboj/18.11.3044
    • Sanz, L., Sanchez, P., Lallena, M.J., Diaz-Meco, M.T. and Moscat, J. (1999) The interaction of p62 with RIP links the atypical PKCs to NF-κB activation. EMBO J. 18, 3044-3053 (Pubitemid 29255613)
    • (1999) EMBO Journal , vol.18 , Issue.11 , pp. 3044-3053
    • Sanz, L.1    Sanchez, P.2    Lallena, M.-J.3    Diaz-Meco, M.T.4    Moscat, J.5
  • 22
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez, C., Boelens, R. and Bonvin, A.M. (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125, 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 23
    • 33645472931 scopus 로고    scopus 로고
    • Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy
    • Liang, B., Bushweller, J.H. and Tamm, L.K. (2006) Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy. J. Am. Chem. Soc. 128, 4389-4397
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4389-4397
    • Liang, B.1    Bushweller, J.H.2    Tamm, L.K.3
  • 24
    • 39649120317 scopus 로고    scopus 로고
    • Affinity makes the difference: Nonselective interaction of the UBA domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains
    • Zhang, D., Raasi, S. and Fushman, D. (2008) Affinity makes the difference: nonselective interaction of the UBA domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. J. Mol. Biol. 377, 162-180
    • (2008) J. Mol. Biol. , vol.377 , pp. 162-180
    • Zhang, D.1    Raasi, S.2    Fushman, D.3
  • 25
    • 41949134141 scopus 로고    scopus 로고
    • Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch
    • Long, J., Gallagher, T.R., Cavey, J.R., Sheppard, P.W., Ralston, S.H., Layfield, R. and Searle, M.S. (2008) Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch. J. Biol. Chem. 283, 5427-5440
    • (2008) J. Biol. Chem. , vol.283 , pp. 5427-5440
    • Long, J.1    Gallagher, T.R.2    Cavey, J.R.3    Sheppard, P.W.4    Ralston, S.H.5    Layfield, R.6    Searle, M.S.7
  • 28
    • 79958086002 scopus 로고    scopus 로고
    • Impact of p62/SQSTM1 UBA domain mutations linked to Paget's disease of bone on ubiquitin recognition
    • Garner, T.P., Long, J., Layfield, R. and Searle, M.S. (2011) Impact of p62/SQSTM1 UBA domain mutations linked to Paget's disease of bone on ubiquitin recognition. Biochemistry 50, 4665-4674
    • (2011) Biochemistry , vol.50 , pp. 4665-4674
    • Garner, T.P.1    Long, J.2    Layfield, R.3    Searle, M.S.4
  • 29
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C. and Stenmark, H. (2009) The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 31
    • 3142581995 scopus 로고    scopus 로고
    • Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitin proteins
    • Teo, H., Veprintsev, D.B. and Williams, R.L. (2004) Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitin proteins. J. Biol. Chem. 279, 28689-28696
    • (2004) J. Biol. Chem. , vol.279 , pp. 28689-28696
    • Teo, H.1    Veprintsev, D.B.2    Williams, R.L.3
  • 32
    • 4544255838 scopus 로고    scopus 로고
    • Structure of the ESCRT-II endosomal trafficking complex
    • DOI 10.1038/nature02914
    • Hierro, A., Sun, J., Rusnak, A.S., Kim, J., Prag, G., Emr, S.D. and Hurley, J.H. (2004) Structure of the ESCRT-II endosomal trafficking complex. Nature 431, 221-225 (Pubitemid 39243478)
    • (2004) Nature , vol.431 , Issue.7005 , pp. 221-225
    • Hierro, A.1    Sun, J.I.2    Rusnak, A.S.3    Kim, J.4    Prag, G.5    Emr, S.O.6    Hurley, J.H.7


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