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Volumn 399, Issue 3, 2006, Pages 361-372

Ubiquitin-binding domains

Author keywords

Endocytosis; Proteasome; Protein structure; Ubiquitin binding domain; Ubiquitination; Vesicle trafficking

Indexed keywords

CELL CULTURE; CHEMICAL MODIFICATION; COMPLEXATION; DEGRADATION; MOLECULAR STRUCTURE; POLYMERIZATION; QUALITY CONTROL;

EID: 33750555919     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061138     Document Type: Review
Times cited : (525)

References (110)
  • 2
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001) Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 3
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman, A. M. (2001) Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell Biol. 2, 169-178
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 4
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser, M. (2000) Evolution and function of ubiquitin-like protein-conjugation systems. Nat. Cell Biol. 2, E153-E157
    • (2000) Nat. Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 5
    • 20444399163 scopus 로고    scopus 로고
    • The regulation of proteasome degradation by multi-ubiquitin chain binding proteins
    • Miller, J. and Gordon, C. (2005) The regulation of proteasome degradation by multi-ubiquitin chain binding proteins. FEBS Lett. 579, 3224-3230
    • (2005) FEBS Lett. , vol.579 , pp. 3224-3230
    • Miller, J.1    Gordon, C.2
  • 6
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding macbines
    • Elsasser, S. and Finley, D. (2005) Delivery of ubiquitinated substrates to protein-unfolding macbines. Nat. Cell Biol. 7, 742-710
    • (2005) Nat. Cell Biol. , vol.7 , pp. 742-1710
    • Elsasser, S.1    Finley, D.2
  • 7
    • 0035823032 scopus 로고    scopus 로고
    • A new ticket for entry into budding vesicles - Ubiquitin
    • Hicke, L. (2001) A new ticket for entry into budding vesicles - ubiquitin. Cell 106, 527-530
    • (2001) Cell , vol.106 , pp. 527-530
    • Hicke, L.1
  • 9
    • 33645854348 scopus 로고    scopus 로고
    • Roie of ubiquitylation in cellular membrane transport
    • Staub, O. and Rotin, D. (2006) Roie of ubiquitylation in cellular membrane transport. Physiol. Rev. 86, 669-707
    • (2006) Physiol. Rev. , vol.86 , pp. 669-707
    • Staub, O.1    Rotin, D.2
  • 10
    • 33646196532 scopus 로고    scopus 로고
    • Regulation of DNA repair by ubiquitylation
    • Huang, T. T. and D'Andrea, A. D. (2006) Regulation of DNA repair by ubiquitylation. Nat. Rev. Mol. Cell Biol. 7, 323-334
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 323-334
    • Huang, T.T.1    D'Andrea, A.D.2
  • 11
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signalling connection
    • Di Fiore, P. P., Polo, S. and Hofmann, K. (2003) When ubiquitin meets ubiquitin receptors: a signalling connection. Nat. Rev. Mol. Cell Biol. 4, 491-497
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 12
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund, K. and Dikic, I. (2005) Ubiquitylation and cell signaling. EMBO J. 24, 3353-3359
    • (2005) EMBO J. , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 14
    • 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
  • 15
    • 0141744750 scopus 로고    scopus 로고
    • STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif
    • Mizuno, E., Kawahata, K., Kato, M., Kitamura, N. and Komada, M. (2003) STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif. Mol. Biol. Cell 14, 3675-3689
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3675-3689
    • Mizuno, E.1    Kawahata, K.2    Kato, M.3    Kitamura, N.4    Komada, M.5
  • 16
    • 0035369556 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems
    • Hofmann, K. and Falquet, L. (2001) A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26, 347-350
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 347-350
    • Hofmann, K.1    Falquet, L.2
  • 18
    • 0036094688 scopus 로고    scopus 로고
    • Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis
    • Shih, S. C., Katzmann, D. J., Schnell, J. D., Sutanto, M., Emr, S. D. and Hicke, L. (2002) Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nat. Cell Biol. 4, 389-393
    • (2002) Nat. Cell Biol. , vol.4 , pp. 389-393
    • Shih, S.C.1    Katzmann, D.J.2    Schnell, J.D.3    Sutanto, M.4    Emr, S.D.5    Hicke, L.6
  • 19
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C. and Piper, R. C. (2002) The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat. Cell Biol. 4, 534-539
    • (2002) Nat. Cell Biol. , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 22
    • 0037046805 scopus 로고    scopus 로고
    • The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination
    • Oldham, C. E., Mohney, R. P., Miller, S. L. H., Hanes, R. N. and O'Bryan, J. P. (2002) The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination. Curr. Biol. 12, 1112-1116
    • (2002) Curr. Biol. , vol.12 , pp. 1112-1116
    • Oldham, C.E.1    Mohney, R.P.2    Miller, S.L.H.3    Hanes, R.N.4    O'Bryan, J.P.5
  • 23
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • Katz, M., Shtiegman, K., Tal-Or, P., Yakir, L., Mosesson, Y., Harari, D., Machluf, Y., Asao, H., Jovin, T., Sugamura, K. and Yarden, Y. (2002) Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 3, 740-751
    • (2002) Traffic , vol.3 , pp. 740-751
    • Katz, M.1    Shtiegman, K.2    Tal-Or, P.3    Yakir, L.4    Mosesson, Y.5    Harari, D.6    Machluf, Y.7    Asao, H.8    Jovin, T.9    Sugamura, K.10    Yarden, Y.11
  • 24
    • 3242878438 scopus 로고    scopus 로고
    • Analysis of the role of ubiquitin-interacting motifs in ubiquitin binding and ubiquitylation
    • Miller, S. L. H., Malotky, E. and O'Bryan, J. P. (2004) Analysis of the role of ubiquitin-interacting motifs in ubiquitin binding and ubiquitylation. J. Biol. Chem. 279, 33528-33537
    • (2004) J. Biol. Chem. , vol.279 , pp. 33528-33537
    • Miller, S.L.H.1    Malotky, E.2    O'Bryan, J.P.3
  • 25
    • 0036392305 scopus 로고    scopus 로고
    • A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins
    • Shekhtman, A. and Cowburn, D. (2002) A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins. Biochem. Biophys. Res. Commun. 296, 1222-1227
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 1222-1227
    • Shekhtman, A.1    Cowburn, D.2
  • 27
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • Swanson, K. A., Kang, R. S., Stamenova, S. D., Hicke, L. and Radhakrishnan, I. (2003) Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J. 22, 4597-4606
    • (2003) EMBO J. , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5
  • 28
    • 0141480905 scopus 로고    scopus 로고
    • Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a
    • Ryu, K. S., Lee, K. J., Bae, S. H., Kim, B. K., Kim, K. A. and Choi, B. S. (2003) Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a. J. Biol. Chem. 278, 36621-36627
    • (2003) J. Biol. Chem. , vol.278 , pp. 36621-36627
    • Ryu, K.S.1    Lee, K.J.2    Bae, S.H.3    Kim, B.K.4    Kim, K.A.5    Choi, B.S.6
  • 29
    • 17144417404 scopus 로고    scopus 로고
    • Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
    • Wang, Q. H., Young, P. and Walters, K. J. (2005) Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. J. Mol. Biol. 348, 727-739
    • (2005) J. Mol. Biol. , vol.348 , pp. 727-739
    • Wang, Q.H.1    Young, P.2    Walters, K.J.3
  • 33
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann, K. and Bucher, P. (1996) The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21, 172-173
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 35
    • 0034700249 scopus 로고    scopus 로고
    • Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr
    • Withers-Ward, E. S., Mueller, T. D., Chen, I. S. Y. and Feigon, J. (2000) Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr. Biochemistry 39, 14103-14112
    • (2000) Biochemistry , vol.39 , pp. 14103-14112
    • Withers-Ward, E.S.1    Mueller, T.D.2    Chen, I.S.Y.3    Feigon, J.4
  • 36
    • 0036300780 scopus 로고    scopus 로고
    • Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions
    • Mueller, T. D. and Feigon, J. (2002) Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J. Mol. Biol. 319, 1243-1255
    • (2002) J. Mol. Biol. , vol.319 , pp. 1243-1255
    • Mueller, T.D.1    Feigon, J.2
  • 38
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi, M., Sasaki, T., Nishimoto, T. and Kobayashi, H. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. U.S.A. 99, 745-750
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 39
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • Raasi, S. and Pickart, C. M. (2003) Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J. Biol. Chem. 278, 8951-8959
    • (2003) J. Biol. Chem. , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 40
    • 0029809134 scopus 로고    scopus 로고
    • p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding protiens
    • Vadlamudi, R. K., Joung, I., Strominger, J. L. and Shin, J. (1996) p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding protiens. J. Biol. Chem. 271, 20235-20237
    • (1996) J. Biol. Chem. , vol.271 , pp. 20235-20237
    • Vadlamudi, R.K.1    Joung, I.2    Strominger, J.L.3    Shin, J.4
  • 42
    • 0034762028 scopus 로고    scopus 로고
    • Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
    • Chen, L., Shinde, U., Ortolan, T. G. and Madura, K. (2001) Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly. EMBO Rep. 2, 933-938
    • (2001) EMBO Rep. , vol.2 , pp. 933-938
    • Chen, L.1    Shinde, U.2    Ortolan, T.G.3    Madura, K.4
  • 43
    • 0035834467 scopus 로고    scopus 로고
    • UBA domains mediate protein-protein interactions between two DNA damage-inducible proteins
    • Bertolaet, B. L., Clarke, D. J., Wolff, M., Watson, M. H., Henze, M., Divita, G. and Reed, S. I. (2001) UBA domains mediate protein-protein interactions between two DNA damage-inducible proteins. J. Mol. Biol. 313, 955-963
    • (2001) J. Mol. Biol. , vol.313 , pp. 955-963
    • Bertolaet, B.L.1    Clarke, D.J.2    Wolff, M.3    Watson, M.H.4    Henze, M.5    Divita, G.6    Reed, S.I.7
  • 44
    • 0345686439 scopus 로고    scopus 로고
    • Ubiquitin recognition by the DNA repair protein hHR23a
    • Wang, Q. H., Goh, A. M., Howley, P. M. and Walters, K. J. (2003) Ubiquitin recognition by the DNA repair protein hHR23a. Biochemistry 42, 13529-13535
    • (2003) Biochemistry , vol.42 , pp. 13529-13535
    • Wang, Q.H.1    Goh, A.M.2    Howley, P.M.3    Walters, K.J.4
  • 45
    • 1642482834 scopus 로고    scopus 로고
    • Specificity of the interaction between ubiquitin-associated domains and ubiquitin
    • Mueller, T. D., Kamionka, M. and Feigon, J. (2004) Specificity of the interaction between ubiquitin-associated domains and ubiquitin. J. Biol. Chem. 279, 11926-11936
    • (2004) J. Biol. Chem. , vol.279 , pp. 11926-11936
    • Mueller, T.D.1    Kamionka, M.2    Feigon, J.3
  • 47
    • 17044420416 scopus 로고    scopus 로고
    • Structure of the UBA domain of Dsk2p in complex with ubiquitin: Molecular determinants for ubiquitin recognition
    • Ohno, A., Jee, J., Fujiwara, K., Tenno, T., Goda, N., Tochio, H., Kobayashi, H., Hiroaki, H. and Shirakawa, M. (2005) Structure of the UBA domain of Dsk2p in complex with ubiquitin: molecular determinants for ubiquitin recognition. Structure 13, 521-532
    • (2005) Structure , vol.13 , pp. 521-532
    • Ohno, A.1    Jee, J.2    Fujiwara, K.3    Tenno, T.4    Goda, N.5    Tochio, H.6    Kobayashi, H.7    Hiroaki, H.8    Shirakawa, M.9
  • 48
    • 20444391345 scopus 로고    scopus 로고
    • Structural determinants for selective recognition of a lys48-linked polyubiquitin chain by a UBA domain
    • Varadan, R., Assfalg, M., Raasi, S., Pickart, C. and Fushman, D. (2005) Structural determinants for selective recognition of a lys48-linked polyubiquitin chain by a UBA domain. Mol. Cell 18, 687-698
    • (2005) Mol. Cell , vol.18 , pp. 687-698
    • Varadan, R.1    Assfalg, M.2    Raasi, S.3    Pickart, C.4    Fushman, D.5
  • 49
    • 33646041593 scopus 로고    scopus 로고
    • Structural basis for monoubiquitin recognition by the Ede1 UBA domain
    • Swanson, K. A., Hicke, L. and Radhakrishnan, I. (2006) Structural basis for monoubiquitin recognition by the Ede1 UBA domain. J. Mol. Biol. 358, 713-724
    • (2006) J. Mol. Biol. , vol.358 , pp. 713-724
    • Swanson, K.A.1    Hicke, L.2    Radhakrishnan, I.3
  • 50
    • 33744461058 scopus 로고    scopus 로고
    • Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin
    • Chang, Y. G., Song, A. X., Gao, Y. G., Shi, Y. H., Lin, X. J., Cao, X. T., Lin, D. H. and Hu, H. Y. (2006) Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin. Prot. Sci. 15, 1248-1259
    • (2006) Prot. Sci. , vol.15 , pp. 1248-1259
    • Chang, Y.G.1    Song, A.X.2    Gao, Y.G.3    Shi, Y.H.4    Lin, X.J.5    Cao, X.T.6    Lin, D.H.7    Hu, H.Y.8
  • 53
    • 0038820381 scopus 로고    scopus 로고
    • Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding
    • Kang, R. S., Daniels, C. M., Francis, S. A., Shih, S. C., Salerno, W. J., Hicke, L. and Radhakrishnan, I. (2003) Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell 113, 621-630
    • (2003) Cell , vol.113 , pp. 621-630
    • Kang, R.S.1    Daniels, C.M.2    Francis, S.A.3    Shih, S.C.4    Salerno, W.J.5    Hicke, L.6    Radhakrishnan, I.7
  • 54
    • 26944465404 scopus 로고    scopus 로고
    • Diverse polyubiquitin interaction properties of ubiquitin-associated domains
    • Raasi, S., Varadan, R., Fushman, D. and Pickart, C. M. (2005) Diverse polyubiquitin interaction properties of ubiquitin-associated domains. Nat. Struct. Mol. Biol. 12, 708-714
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 708-714
    • Raasi, S.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4
  • 56
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan, R., Walker, O., Pickart, C. and Fushman, D. (2002) Structural properties of polyubiquitin chains in solution. J. Mol. Biol. 324, 637-647
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 58
    • 0034667598 scopus 로고    scopus 로고
    • Proteins of the endoplasmic-reticulum-associated degradation pathway: Domain detection and function prediction
    • Ponting, C. P. (2000) Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction. Biochem. J. 351, 527-535
    • (2000) Biochem. J. , vol.351 , pp. 527-535
    • Ponting, C.P.1
  • 59
    • 0037316409 scopus 로고    scopus 로고
    • Ubiquitin signals protein trafficking via interaction with a novel ubiquitin binding domain in the membrane fusion regulator, Vps9p
    • Donaldson, K. M., Yin, H. W., Gekakis, N., Supek, F. and Joazeiro, C. A. P. (2003) Ubiquitin signals protein trafficking via interaction with a novel ubiquitin binding domain in the membrane fusion regulator, Vps9p. Curr. Biol. 13, 258-262
    • (2003) Curr. Biol. , vol.13 , pp. 258-262
    • Donaldson, K.M.1    Yin, H.W.2    Gekakis, N.3    Supek, F.4    Joazeiro, C.A.P.5
  • 60
    • 0345616428 scopus 로고    scopus 로고
    • A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain
    • Shih, S. C., Prag, G., Francis, S. A., Sutanto, M. A., Hurley, J. H. and Hicke, L. (2003) A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain. EMBO J. 22, 1273-1281
    • (2003) EMBO J. , vol.22 , pp. 1273-1281
    • Shih, S.C.1    Prag, G.2    Francis, S.A.3    Sutanto, M.A.4    Hurley, J.H.5    Hicke, L.6
  • 62
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano, R. and Bonifacino, J. S. (2004) Interactions of GGA3 with the ubiquitin sorting machinery. Nat. Cell Biol. 6, 244-251
    • (2004) Nat. Cell Biol. , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 64
    • 0037343940 scopus 로고    scopus 로고
    • The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs
    • Collins, B. M., Watson, P. J. and Owen, D. J. (2003) The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs. Dev. Cell 4, 321-332
    • (2003) Dev. Cell , vol.4 , pp. 321-332
    • Collins, B.M.1    Watson, P.J.2    Owen, D.J.3
  • 65
    • 0037446843 scopus 로고    scopus 로고
    • Structure of the GAT domain of human GGA1: A syntaxin amino-terminal domain fold in an endosomal trafficking adaptor
    • Suer, S., Misra, S., Saidi, L. F. and Hurley, J. H. (2003) Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor. Proc. Natl. Acad. Sci. U.S.A. 100, 4451-4456
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4451-4456
    • Suer, S.1    Misra, S.2    Saidi, L.F.3    Hurley, J.H.4
  • 68
    • 33750555052 scopus 로고    scopus 로고
    • GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination
    • Shiba, Y., Katoh, Y., Shiba, T., Wakatsuki, S. and Nakayama, K. (2004) GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination. Mol. Biol. Cell 15, 314A-314A
    • (2004) Mol. Biol. Cell , vol.15
    • Shiba, Y.1    Katoh, Y.2    Shiba, T.3    Wakatsuki, S.4    Nakayama, K.5
  • 69
    • 3843118843 scopus 로고    scopus 로고
    • The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites
    • Mattera, R., Puertollano, R., Smith, W. J. and Bonifacino, J. S. (2004) The trihelical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites. J. Biol. Chem. 279, 31409-31418
    • (2004) J. Biol. Chem. , vol.279 , pp. 31409-31418
    • Mattera, R.1    Puertollano, R.2    Smith, W.J.3    Bonifacino, J.S.4
  • 71
    • 2642553077 scopus 로고    scopus 로고
    • Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes
    • Katoh, Y., Shiba, Y., Mitsuhashi, H., Yanagida, Y., Takatsu, H. and Nakayama, K. (2004) Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes. J. Biol. Chem. 279, 24435-24443
    • (2004) J. Biol. Chem. , vol.279 , pp. 24435-24443
    • Katoh, Y.1    Shiba, Y.2    Mitsuhashi, H.3    Yanagida, Y.4    Takatsu, H.5    Nakayama, K.6
  • 72
    • 14044278879 scopus 로고    scopus 로고
    • Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins
    • Prag, G., Lee, S. H., Mattera, R., Arighi, C. N., Beach, B. M., Bonifacino, J. S. and Hurley, J. H. (2005) Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 102, 2334-2339
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 2334-2339
    • Prag, G.1    Lee, S.H.2    Mattera, R.3    Arighi, C.N.4    Beach, B.M.5    Bonifacino, J.S.6    Hurley, J.H.7
  • 75
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • Meyer, H. H., Wang, Y. Z. and Warren, G. (2002) Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 21, 5645-5652
    • (2002) EMBO J. , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.Z.2    Warren, G.3
  • 77
    • 0037108963 scopus 로고    scopus 로고
    • Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes
    • Hook, S. S., Orian, A., Cowley, S. M. and Eisenman, R. N. (2002) Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc. Natl. Acad. Sci. U.S.A. 99, 13425-13430
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13425-13430
    • Hook, S.S.1    Orian, A.2    Cowley, S.M.3    Eisenman, R.N.4
  • 78
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S. and Khochbin, S. (2001) Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways. Mol. Cell. Biol. 21, 8035-8044
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6    Khochbin, S.7
  • 81
    • 33646070471 scopus 로고    scopus 로고
    • The Rab5 guanine nucleotide exchange factor Rabex-5 binds ubiquitin (Ub) and functions as a Ub ligase through an atypical Ub-interacting motif and a zinc finger domain
    • Mattera, R., Tsai, Y. C., Weissman, A. M. and Bonifacino, J. S. (2006) The Rab5 guanine nucleotide exchange factor Rabex-5 binds ubiquitin (Ub) and functions as a Ub ligase through an atypical Ub-interacting motif and a zinc finger domain. J. Biol. Chem. 281, 6874-6883
    • (2006) J. Biol. Chem. , vol.281 , pp. 6874-6883
    • Mattera, R.1    Tsai, Y.C.2    Weissman, A.M.3    Bonifacino, J.S.4
  • 82
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnFUBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu, F. E., Horton, J. R., Mullally, J. E., Heroux, A., Cheng, X. D. and Wilkinson, K. D. (2006) The ubiquitin binding domain ZnFUBP recognizes the C-terminal diglycine motif of unanchored ubiquitin. Cell 124, 1197-1208
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.D.5    Wilkinson, K.D.6
  • 84
    • 0038724478 scopus 로고    scopus 로고
    • Energetics and specificity of interactions within Ub · Uev · Ubc13 human ubiquitin conjugation complexes
    • McKenna, S., Hu, J., Moraes, T., Xiao, W., Ellison, M. J. and Spyracopoulos, L. (2003) Energetics and specificity of interactions within Ub · Uev · Ubc13 human ubiquitin conjugation complexes. Biochemistry 42, 7922-7930
    • (2003) Biochemistry , vol.42 , pp. 7922-7930
    • McKenna, S.1    Hu, J.2    Moraes, T.3    Xiao, W.4    Ellison, M.J.5    Spyracopoulos, L.6
  • 85
    • 0035955731 scopus 로고    scopus 로고
    • Noncovalent interaction between ubiquitin and the human DNA repair protein mms2 is required for ubc13-mediated polyubiquitination
    • McKenna, S., Spyracopoulos, L., Moraes, T., Pastushok, L., Ptak, C., Xiao, W. and Ellison, M. J. (2001) Noncovalent interaction between ubiquitin and the human DNA repair protein mms2 is required for ubc13-mediated polyubiquitination, J. Biol. Chem. 276, 40120-40126
    • (2001) J. Biol. Chem. , vol.276 , pp. 40120-40126
    • McKenna, S.1    Spyracopoulos, L.2    Moraes, T.3    Pastushok, L.4    Ptak, C.5    Xiao, W.6    Ellison, M.J.7
  • 86
    • 0038579251 scopus 로고    scopus 로고
    • An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13 - The structural basis for lysine 63 chain catalysis
    • McKenna, S., Moraes, T., Pastushok, L., Ptak, C., Xiao, W., Spyracopoulos, L. and Ellison, M. J. (2003) An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13 - the structural basis for lysine 63 chain catalysis. J. Biol. Chem. 278, 13151-13158
    • (2003) J. Biol. Chem. , vol.278 , pp. 13151-13158
    • McKenna, S.1    Moraes, T.2    Pastushok, L.3    Ptak, C.4    Xiao, W.5    Spyracopoulos, L.6    Ellison, M.J.7
  • 88
    • 3142581995 scopus 로고    scopus 로고
    • Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins
    • Teo, H., Veprintsev, D. B. and Williams, R. L. (2004) Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated 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
  • 90
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • Brzovic, P. S., Lissounov, A., Christensen, D. E., Hoyt, D. W. and Klevit, R. E. (2006) A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol. Cell 21, 873-880
    • (2006) Mol. Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 92
    • 33645981584 scopus 로고    scopus 로고
    • ESCRT-I core and ESCRT-II GLUE domain structure reveal role for GLUE in linking to ESCRT-I and membranes
    • Teo, H., Gill, D. J., Sun, J., Perisic, O., Veprintsev, D. B., Vallis, Y., Emr, S. D. and Williams, R. L. (2006) ESCRT-I core and ESCRT-II GLUE domain structure reveal role for GLUE in linking to ESCRT-I and membranes. Cell 125, 99-111
    • (2006) Cell , vol.125 , pp. 99-111
    • Teo, H.1    Gill, D.J.2    Sun, J.3    Perisic, O.4    Veprintsev, D.B.5    Vallis, Y.6    Emr, S.D.7    Williams, R.L.8
  • 94
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26 S proteasome
    • Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., Koonin, E. V. and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26 S proteasome, Science 298, 611-615
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 95
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T. T. and Cohen, R. E. (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.T.1    Cohen, R.E.2
  • 96
    • 31044444461 scopus 로고    scopus 로고
    • Ubiquitin binding by a variant Jab1/MPN domain in the essential pre-mRNA splicing factor Prp8p
    • Bellare, P., Kutach, A. K., Rines, A. K., Guthrie, C. and Sontheimer, E. J. (2006) Ubiquitin binding by a variant Jab1/MPN domain in the essential pre-mRNA splicing factor Prp8p. RNA 12, 292-302
    • (2006) RNA , vol.12 , pp. 292-302
    • Bellare, P.1    Kutach, A.K.2    Rines, A.K.3    Guthrie, C.4    Sontheimer, E.J.5
  • 97
    • 31344473702 scopus 로고    scopus 로고
    • Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain
    • Mullally, J. E., Chernova, T. and Wilkinson, K. D. (2006) Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain. Mol. Cell. Biol. 26, 822-830
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 822-830
    • Mullally, J.E.1    Chernova, T.2    Wilkinson, K.D.3
  • 98
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. (2001) Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2, 195-201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 99
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K., Sigismund, S., Polo, S., Szymkiewicz, I., Di Fiore, P. P. and Dikic, I. (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat. Cell Biol. 5, 461-466
    • (2003) Nat. Cell Biol. , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5    Dikic, I.6
  • 100
    • 0037677208 scopus 로고    scopus 로고
    • Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation
    • Mosesson, Y., Shtiegman, K., Katz, M., Zwang, Y., Vereb, G., Szollosi, J. and Yarden, Y. (2003) Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J. Biol. Chem. 278, 21323-21326
    • (2003) J. Biol. Chem. , vol.278 , pp. 21323-21326
    • Mosesson, Y.1    Shtiegman, K.2    Katz, M.3    Zwang, Y.4    Vereb, G.5    Szollosi, J.6    Yarden, Y.7
  • 101
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • Huang, F. T., Kirkpatrick, D., Jiang, X. J., Gygi, S. and Sorkin, A. (2006) Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol. Cell 21, 737-748
    • (2006) Mol. Cell , vol.21 , pp. 737-748
    • Huang, F.T.1    Kirkpatrick, D.2    Jiang, X.J.3    Gygi, S.4    Sorkin, A.5
  • 102
    • 33644529627 scopus 로고    scopus 로고
    • Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells
    • Barriere, H., Nemes, C., Lechardeur, D., Khan-Mohammad, M., Fruh, K. and Lukacs, G. L. (2006) Molecular basis of oligoubiquitin-dependent internalization of membrane proteins in mammalian cells. Traffic 7, 282-297
    • (2006) Traffic , vol.7 , pp. 282-297
    • Barriere, H.1    Nemes, C.2    Lechardeur, D.3    Khan-Mohammad, M.4    Fruh, K.5    Lukacs, G.L.6
  • 104
    • 33644799030 scopus 로고    scopus 로고
    • Two new structures of Ub-receptor complexes. U2
    • Alam, S. L. and Sundquist, W. I. (2006) Two new structures of Ub-receptor complexes. U2. Nat. Struct. Mol. Biol. 13, 186-188
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 186-188
    • Alam, S.L.1    Sundquist, W.I.2
  • 105
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley, J. H. and Emr, S. D. (2006) The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Ann. Rev. Biophys. Biomol. Struct. 35, 277-298
    • (2006) Ann. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 106
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S. and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 108
    • 32044443405 scopus 로고    scopus 로고
    • Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1
    • Panneerselvam, S., Marx, A., Mandelkow, E. M. and Mandelkow, E. (2006) Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1. Structure 14, 173-183
    • (2006) Structure , vol.14 , pp. 173-183
    • Panneerselvam, S.1    Marx, A.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 109
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter, D. and Lima, C. D. (2005) Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435, 687-692
    • (2005) Nature , vol.435 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 110
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund, K., Di Fiore, P. P. and Dikic, I. (2003) Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem. Sci. 28, 598-603
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3


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