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Volumn 137, Issue 2, 2005, Pages 133-139

A novel UbcH10-binding protein facilitates the ubiquitinylation of cyclin B in vitro

Author keywords

Cyclin B; HECT domain; UbcH10; Ubiquitin conjugating enzyme; Ubiquitin ligase

Indexed keywords

ANAPHASE PROMOTING COMPLEX; CYCLIN B; PROTEIN UBCH10; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 17044401854     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi026     Document Type: Article
Times cited : (13)

References (34)
  • 1
    • 0012810697 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway of intracellular proteolysis
    • Doherty, J.F., Dawson, S., and Mayer, J.R. (2002) The ubiquitin-proteasome pathway of intracellular proteolysis. Essays Biochem. 38, 51-63
    • (2002) Essays Biochem. , vol.38 , pp. 51-63
    • Doherty, J.F.1    Dawson, S.2    Mayer, J.R.3
  • 2
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/ multicatalytic-multifunctional proteinase: Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • Heinemeyer, W., Kleinschmidt, A.J., Saidowsky, J., Escher, C., and Wolf, H.D. (1991) Proteinase yscE, the yeast proteasome/ multicatalytic- multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10, 555-562
    • (1991) EMBO J. , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, A.J.2    Saidowsky, J.3    Escher, C.4    Wolf, H.D.5
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz J., Zuhl, F., and Seemuller, E. (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 4
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, S.J. Huffman, L. Rechsteiner, M., and Pickart, C. (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94-102
    • (2000) EMBO J. , vol.19 , pp. 94-102
    • Thrower, S.J.1    Huffman, L.2    Rechsteiner, M.3    Pickart, C.4
  • 5
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A., and Varshavsky A. (1984) Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell 37, 43-55
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 6
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T. and Jentsch, S. (1993) A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365, 176-179
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 7
    • 0030297097 scopus 로고    scopus 로고
    • Lessons from the discovery of the ubiquitin system
    • Hershko, A. (1996) Lessons from the discovery of the ubiquitin system. Trends Biochem. Sci. 21, 445-449
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 445-449
    • Hershko, A.1
  • 8
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, L.A. and Siepmann, J.T. (1997) Pathways of ubiquitin conjugation. FASEB J. 11, 1257-1268
    • (1997) FASEB J. , vol.11 , pp. 1257-1268
    • Haas, L.A.1    Siepmann, J.T.2
  • 9
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on Ubiquitinylation
    • Weissman, A.M. (2001) Themes and variations on Ubiquitinylation. Nat. Rev. Mol. Cell. Biol. 2, 169-178
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 10
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, A.C. and Weissman, M.A. (2000) RING finger proteins: mediators of ubiquitin ligase activity. Cell 102, 549-552
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, A.C.1    Weissman, M.A.2
  • 13
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination
    • Aravind, L. and Koonin, V.E. (2000) The U box is a modified RING finger - a common domain in ubiquitination. Curr. Biol. 10, R132-R134
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, V.E.2
  • 14
    • 0035375052 scopus 로고    scopus 로고
    • Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes
    • Pringa, E., Martinez-Noel, G., Muller, U., and Harbers, K. (2001) Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. J. Biol. Chem. 276, 19617-19623
    • (2001) J. Biol. Chem. , vol.276 , pp. 19617-19623
    • Pringa, E.1    Martinez-Noel, G.2    Muller, U.3    Harbers, K.4
  • 15
    • 0033567387 scopus 로고    scopus 로고
    • Whose end is destruction: Cell division and the anaphase-promoting complex
    • Zachariae, W and Nasmyth, K. (1999) Whose end is destruction: cell division and the anaphase-promoting complex. Genes Dev. 13, 2039-2058
    • (1999) Genes Dev. , vol.13 , pp. 2039-2058
    • Zachariae, W.1    Nasmyth, K.2
  • 16
    • 0034255264 scopus 로고    scopus 로고
    • The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex
    • Gmachl, M., Gieffers, C., Podtelejnikov, V.A., Mann, M., and Peters, M.J. (2000) The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proc. Natl Acad. Sci. USA 97, 8973-8978
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8973-8978
    • Gmachl, M.1    Gieffers, C.2    Podtelejnikov, V.A.3    Mann, M.4    Peters, M.J.5
  • 18
    • 0035661566 scopus 로고    scopus 로고
    • APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex
    • Tang, Z., Bharadwaj, R., Zhu, H., Ozkan, E., Hakala, K., Deisenhofer, J., and Yu, H. (2001) APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol. Biol. Cell 12, 3839-3851
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3839-3851
    • Tang, Z.1    Bharadwaj, R.2    Zhu, H.3    Ozkan, E.4    Hakala, K.5    Deisenhofer, J.6    Yu, H.7
  • 19
    • 0035878126 scopus 로고    scopus 로고
    • Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: A novel mechanism for regulating Cdh1
    • Pfleger, M.C., Salic, A., Lee, E., and Kirschner, W.M. (2001) Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1. Genes Dev. 15, 1759-1764
    • (2001) Genes Dev. , vol.15 , pp. 1759-1764
    • Pfleger, M.C.1    Salic, A.2    Lee, E.3    Kirschner, W.M.4
  • 20
    • 0036713310 scopus 로고    scopus 로고
    • The anaphase-promoting complex: It's not just for mitosis any more
    • Harper, W.J., Burton, L.J., and Solomon, J.M. (2002) The anaphase-promoting complex: it's not just for mitosis any more. Genes Dev. 16, 2179-2206
    • (2002) Genes Dev. , vol.16 , pp. 2179-2206
    • Harper, W.J.1    Burton, L.J.2    Solomon, J.M.3
  • 21
    • 0035883946 scopus 로고    scopus 로고
    • Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex
    • Pfleger, C.M., Lee, E., and Kirschner, W.M. (2001) Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex. Genes Dev. 15, 2396-2407
    • (2001) Genes Dev. , vol.15 , pp. 2396-2407
    • Pfleger, C.M.1    Lee, E.2    Kirschner, W.M.3
  • 22
    • 0030113930 scopus 로고    scopus 로고
    • Identification of a novel ubiquitin-conjugating enzyme involved in mitotic cyclin degradation
    • Yu, H., King, W.R., Peters, M.J., and Kirschner, W.M. (1996) Identification of a novel ubiquitin-conjugating enzyme involved in mitotic cyclin degradation. Curr. Biol. 6, 455-466
    • (1996) Curr. Biol. , vol.6 , pp. 455-466
    • Yu, H.1    King, W.R.2    Peters, M.J.3    Kirschner, W.M.4
  • 23
    • 0030909599 scopus 로고    scopus 로고
    • Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase
    • Townsley, M.F., Aristarkhov, A., Beck, S., Hershko, A., and Ruderman, V.J. (1997) Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10 blocks cells in metaphase. Proc. Natl Acad. Sci. USA 94, 2362-2367
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 2362-2367
    • Townsley, M.F.1    Aristarkhov, A.2    Beck, S.3    Hershko, A.4    Ruderman, V.J.5
  • 24
    • 0030924351 scopus 로고    scopus 로고
    • A ubiquitin-conjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis
    • Osaka, R, Seino, H., Seno, T., and Yamao, F. (1997) A ubiquitin-conjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis. Mol. Cell. Biol. 17, 3388-3397
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3388-3397
    • Osaka, R.1    Seino, H.2    Seno, T.3    Yamao, F.4
  • 25
    • 0035498980 scopus 로고    scopus 로고
    • Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN
    • Stroschein, L.S., Bonni, S., Wrana, L.J., and Luo, K. (2001) Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN. Genes Dev. 15, 2822-2836
    • (2001) Genes Dev. , vol.15 , pp. 2822-2836
    • Stroschein, L.S.1    Bonni, S.2    Wrana, L.J.3    Luo, K.4
  • 26
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • Honda, R. and Yasuda, H. (2000) Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19, 1473-1476
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 27
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffher, M., Huibregtse, M.J., Vierstra, D.R., and Howley, M.P. (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffher, M.1    Huibregtse, M.J.2    Vierstra, D.R.3    Howley, M.P.4
  • 28
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cb1-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, D.P., and Pavletich, P.N. (2000) Structure of a c-Cb1-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533-539
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, D.P.3    Pavletich, P.N.4
  • 29
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang, L., Kinnucan, E., Wang, G., Beaudenon, S., Howley, M.P., Huibregtse, M.J., and Pavletich, P.N. (1999) Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286, 1321-1326
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1    Kinnucan, E.2    Wang, G.3    Beaudenon, S.4    Howley, M.P.5    Huibregtse, M.J.6    Pavletich, P.N.7
  • 30
    • 0029036701 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, M.J., Scheffher, M., Beaudenon, S., and Howley, M.P. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA 92, 2563-2567
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, M.J.1    Scheffher, M.2    Beaudenon, S.3    Howley, M.P.4
  • 32
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • Hershko, A. (1997) Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 9, 788-799
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 788-799
    • Hershko, A.1
  • 33
    • 0033134014 scopus 로고    scopus 로고
    • Subunits and substrates of the anaphase-promoting complex
    • Peters, M.J. (1999) Subunits and substrates of the anaphase-promoting complex. Exp. Cell Res. 248, 339-349
    • (1999) Exp. Cell Res. , vol.248 , pp. 339-349
    • Peters, M.J.1
  • 34
    • 0032189040 scopus 로고    scopus 로고
    • The role of the destruction box and its neighbouring lysine residues in cyclin B for anaphase ubiquitin-dependent proteolysis in fission yeast: Defining the D-box receptor
    • Yamano, H., Tsurumi, C., Gannon, J., and Hunt, T. (1998) The role of the destruction box and its neighbouring lysine residues in cyclin B for anaphase ubiquitin-dependent proteolysis in fission yeast: defining the D-box receptor. EMBO J. 17, 5670-5678
    • (1998) EMBO J. , vol.17 , pp. 5670-5678
    • Yamano, H.1    Tsurumi, C.2    Gannon, J.3    Hunt, T.4


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