메뉴 건너뛰기




Volumn 287, Issue 50, 2012, Pages 42344-42351

The ubiquitin-associated (UBA) 1 domain of Schizosaccharomyces pombe Rhp23 is essential for the recognition of ubiquitin-proteasome system substrates both in vitro and in vivo

Author keywords

[No Author keywords available]

Indexed keywords

26 S PROTEASOME; BINDING ASSAYS; BINDING PROPERTIES; CHIMERIC PROTEINS; CONTEXT DEPENDENT; DOMAIN ARCHITECTURES; FOLDED PROTEINS; FULL-LENGTH PROTEINS; FUNCTIONAL CELLS; IN-VITRO; IN-VIVO; N-TERMINALS; PROTEASOMES; PROTEIN LEVEL; SCHIZOSACCHAROMYCES POMBE; SPATIAL AND TEMPORAL DISTRIBUTION; UBIQUITIN; UBIQUITIN-LIKE; UBIQUITIN-PROTEASOME SYSTEM;

EID: 84871303226     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.419838     Document Type: Article
Times cited : (5)

References (41)
  • 1
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S., and Ciechanover, A. (1983) Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258, 8206-8214
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 2
    • 0022975275 scopus 로고
    • The protein substrate binding site of the ubiquitin-protein ligase system
    • Hershko, A., Heller, H., Eytan, E., and Reiss, Y. (1986) The protein substrate binding site of the ubiquitin-protein ligase system. J. Biol. Chem. 261, 11992-11999 (Pubitemid 17202754)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.26 , pp. 11992-11999
    • Hershko, A.1    Heller, H.2    Eytan, E.3    Reiss, Y.4
  • 5
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, J. S., Hoffman, L., Rechsteiner, M., and Pickart, C. M. (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94-102 (Pubitemid 30009229)
    • (2000) EMBO Journal , vol.19 , Issue.1 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 6
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • DOI 10.1016/j.cbpa.2004.09.009, PII S1367593104001413
    • Pickart, C. M., and Fushman, D. (2004) Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol. 8, 610-616 (Pubitemid 39535722)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.6 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 7
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583 (Pubitemid 19090506)
    • (1989) Science , vol.243 , Issue.4898 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 8
    • 76549089605 scopus 로고    scopus 로고
    • UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex
    • Wu, T., Merbl, Y., Huo, Y., Gallop, J. L., Tzur, A., and Kirschner, M. W. (2010) UBE2S drives elongation of K11-linked ubiquitin chains by the anaphase-promoting complex. Proc. Natl. Acad. Sci. U.S.A. 107, 1355-1360
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1355-1360
    • Wu, T.1    Merbl, Y.2    Huo, Y.3    Gallop, J.L.4    Tzur, A.5    Kirschner, M.W.6
  • 10
    • 0034685806 scopus 로고    scopus 로고
    • Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised
    • DOI 10.1074/jbc.275.20.15182
    • Wilkinson, C. R., Ferrell, K., Penney, M., Wallace, M., Dubiel, W., and Gordon, C. (2000) Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised. J. Biol. Chem. 275, 15182-15192 (Pubitemid 30337242)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.20 , pp. 15182-15192
    • Wilkinson, C.R.M.1    Ferrell, K.2    Penney, M.3    Wallace, M.4    Dubiel, W.5    Gordon, C.6
  • 12
    • 0038268188 scopus 로고    scopus 로고
    • Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins
    • DOI 10.1074/jbc.M208281200
    • Seeger, M., Hartmann-Petersen, R., Wilkinson, C. R., Wallace, M., Samejima, I., Taylor, M. S., and Gordon, C. (2003) Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins. J. Biol. Chem. 278, 16791-16796 (Pubitemid 36799547)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16791-16796
    • Seeger, M.1    Hartmann-Petersen, R.2    Wilkinson, C.R.M.3    Wallace, M.4    Samejima, I.5    Taylor, M.S.6    Gordon, C.7
  • 15
    • 0031890210 scopus 로고    scopus 로고
    • Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1
    • DOI 10.1074/jbc.273.4.1970
    • Fu, H., Sadis, S., Rubin, D. M., Glickman, M., van Nocker, S., Finley, D., and Vierstra, R. D. (1998) Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. J. Biol. Chem. 273, 1970-1981 (Pubitemid 28069242)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 1970-1981
    • Fu, H.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Van Nocker, S.5    Finley, D.6    Vierstra, R.D.7
  • 16
    • 0141625301 scopus 로고    scopus 로고
    • Structural determinants for the binding of ubiquitin-like domains to the proteasome
    • DOI 10.1093/emboj/cdg467
    • Mueller, T. D., and Feigon, J. (2003) Structural determinants for the binding of ubiquitin-like domains to the proteasome. EMBO J. 22, 4634-4645 (Pubitemid 37162900)
    • (2003) EMBO Journal , vol.22 , Issue.18 , pp. 4634-4645
    • Mueller, T.D.1    Feigon, J.2
  • 17
    • 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
  • 21
    • 0036300780 scopus 로고    scopus 로고
    • Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions
    • DOI 10.1016/S0022-2836(02)00302-9
    • 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 (Pubitemid 34729432)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1243-1255
    • Mueller, T.D.1    Feigon, J.2
  • 22
    • 26944465404 scopus 로고    scopus 로고
    • Diverse polyubiquitin interaction properties of ubiquitin-associated domains
    • DOI 10.1038/nsmb962, PII NSMB962
    • 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 (Pubitemid 43086277)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.8 , pp. 708-714
    • Raasi, S.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4
  • 23
    • 20444391345 scopus 로고    scopus 로고
    • Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain
    • DOI 10.1016/j.molcel.2005.05.013, PII S1097276505013195
    • 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 (Pubitemid 40804804)
    • (2005) Molecular Cell , vol.18 , Issue.6 , pp. 687-698
    • Varadan, R.1    Assfalg, M.2    Raasi, S.3    Pickart, C.4    Fushman, D.5
  • 24
    • 17044368771 scopus 로고    scopus 로고
    • The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation
    • Heessen, S., Masucci, M. G., and Dantuma, N. P. (2005) The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. Mol. Cell 18, 225-235
    • (2005) Mol. Cell , vol.18 , pp. 225-235
    • Heessen, S.1    Masucci, M.G.2    Dantuma, N.P.3
  • 25
    • 84867582157 scopus 로고    scopus 로고
    • C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation
    • Heinen, C., Acs, K., Hoogstraten, D., and Dantuma, N. P. (2011) C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation. Nat. Commun. 2, 191
    • (2011) Nat. Commun. , vol.2 , pp. 191
    • Heinen, C.1    Acs, K.2    Hoogstraten, D.3    Dantuma, N.P.4
  • 26
    • 0029885890 scopus 로고    scopus 로고
    • XPC and human homologs of RAD23: Intracellular localization and relationship to other nucleotide excision repair complexes
    • DOI 10.1093/nar/24.13.2551
    • van der Spek, P. J., Eker, A., Rademakers, S., Visser, C., Sugasawa, K., Masutani, C., Hanaoka, F., Bootsma, D., and Hoeijmakers, J. H. (1996) XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes. Nucleic Acids Res. 24, 2551-2559 (Pubitemid 26237154)
    • (1996) Nucleic Acids Research , vol.24 , Issue.13 , pp. 2551-2559
    • Van Der, S.P.J.1    Eker, A.2    Rademakers, S.3    Visser, C.4    Sugasawa, K.5    Masutani, C.6    Hanaoka, F.7    Bootsma, D.8    Hoeijmakers, J.H.J.9
  • 27
    • 63049109748 scopus 로고    scopus 로고
    • The ubiquitin receptor Rad23: At the crossroads of nucleotide excision repair and proteasomal degradation
    • Dantuma, N. P., Heinen, C., and Hoogstraten, D. (2009) The ubiquitin receptor Rad23: at the crossroads of nucleotide excision repair and proteasomal degradation. DNA Repair 8, 449-460
    • (2009) DNA Repair , vol.8 , pp. 449-460
    • Dantuma, N.P.1    Heinen, C.2    Hoogstraten, D.3
  • 29
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., Klar, A., and Nurse, P. (1991) Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194, 795-823
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 30
    • 28844462033 scopus 로고    scopus 로고
    • Controlled synthesis of polyubiquitin chains
    • DOI 10.1016/S0076-6879(05)99002-2, PII S0076687905990022, 2, Ubiquitin and Protein Degradation, Part B
    • Pickart, C. M., and Raasi, S. (2005) Controlled synthesis of polyubiquitin chains. Methods Enzymol. 399, 21-36 (Pubitemid 41772719)
    • (2005) Methods in Enzymology , vol.399 , pp. 21-36
    • Pickart, C.M.1    Raasi, S.2
  • 31
    • 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
    • DOI 10.1016/j.molcel.2007.12.018, PII S1097276508000154
    • Komander, D., Lord, C. J., Scheel, H., Swift, S., Hofmann, K., Ashworth, A., and Barford, D. (2008) The structure of the CYLDUSP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol. Cell 29, 451-464 (Pubitemid 351282537)
    • (2008) Molecular Cell , vol.29 , Issue.4 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3    Swift, S.4    Hofmann, K.5    Ashworth, A.6    Barford, D.7
  • 32
    • 0020479850 scopus 로고
    • Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins
    • Hershko, A., Eytan, E., Ciechanover, A., and Haas, A. L. (1982) Immunochemical analysis of the turnover of ubiquitin-protein conjugates in intact cells. Relationship to the breakdown of abnormal proteins. J. Biol. Chem. 257, 13964-13970
    • (1982) J. Biol. Chem. , vol.257 , pp. 13964-13970
    • Hershko, A.1    Eytan, E.2    Ciechanover, A.3    Haas, A.L.4
  • 33
    • 0020961333 scopus 로고
    • Cyclin: A protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division
    • Evans, T., Rosenthal, E. T., Youngblom, J., Distel, D., and Hunt, T. (1983) Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell 33, 389-396 (Pubitemid 13062490)
    • (1983) Cell , vol.33 , Issue.2 , pp. 389-396
    • Evans, T.1    Rosenthal, E.T.2    Youngblom, J.3
  • 34
    • 38949099707 scopus 로고    scopus 로고
    • Cdh1 is required to maintain genome integrity in primary human cells
    • DOI 10.1038/sj.onc.1210703, PII 1210703
    • Engelbert, D., Schnerch, D., Baumgarten, A., and Wäsch, R. (2008) The ubiquitin ligase APC(Cdh1) is required to maintain genome integrity in primary human cells. Oncogene 27, 907-917 (Pubitemid 351225382)
    • (2008) Oncogene , vol.27 , Issue.7 , pp. 907-917
    • Engelbert, D.1    Schnerch, D.2    Baumgarten, A.3    Wasch, R.4
  • 36
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • DOI 10.1126/science.292.5521.1552
    • Bence, N. F., Sampat, R. M., and Kopito, R. R. (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (Pubitemid 32493425)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 37
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • DOI 10.1016/j.tcb.2004.10.006, PII S0962892404002855
    • Ross, C. A., and Pickart, C. M. (2004) The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol. 14, 703-711 (Pubitemid 39572556)
    • (2004) Trends in Cell Biology , vol.14 , Issue.12 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 38
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • DOI 10.1128/MCB.22.13.4902-4913.2002
    • Chen, L., and Madura, K. (2002) Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol. Cell. Biol. 22, 4902-4913 (Pubitemid 34620423)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.13 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 39
    • 44349094727 scopus 로고    scopus 로고
    • Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
    • DOI 10.1038/nature06924, PII NATURE06924
    • Schreiner, P., Chen, X., Husnjak, K., Randles, L., Zhang, N., Elsasser, S., Finley, D., Dikic, I., Walters, K. J., and Groll, M. (2008) Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction. Nature 453, 548-552 (Pubitemid 351733316)
    • (2008) Nature , vol.453 , Issue.7194 , pp. 548-552
    • Schreiner, P.1    Chen, X.2    Husnjak, K.3    Randles, L.4    Zhang, N.5    Elsasser, S.6    Finley, D.7    Dikic, I.8    Walters, K.J.9    Groll, M.10
  • 40
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • DOI 10.1042/BJ20061138
    • Hurley, J. H., Lee, S., and Prag, G. (2006) Ubiquitin-binding domains. Biochem. J. 399, 361-372 (Pubitemid 44672627)
    • (2006) Biochemical Journal , vol.399 , Issue.3 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 41
    • 0037023716 scopus 로고    scopus 로고
    • Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23
    • DOI 10.1074/jbc.M200245200
    • Rao, H., and Sastry, A. (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23. J. Biol. Chem. 277, 11691-11695 (Pubitemid 34952721)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 11691-11695
    • Rao, H.1    Sastry, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.