메뉴 건너뛰기




Volumn 14, Issue 18, 2004, Pages

APC/C and SCF: Controlling each other and the cell cycle

Author keywords

[No Author keywords available]

Indexed keywords

ANAPHASE PROMOTING COMPLEX; ANAPHASE-PROMOTING COMPLEX; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 4544276433     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2004.09.020     Document Type: Review
Times cited : (244)

References (101)
  • 1
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle. Cyclins revisited
    • Murray A.W. Recycling the cell cycle. Cyclins revisited. Cell. 116:2004;221-234
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.W.1
  • 2
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 3
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters J.M. The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol. Cell. 9:2002;931-943
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 4
    • 0036713310 scopus 로고    scopus 로고
    • The anaphase-promoting complex: It's not just for mitosis any more
    • Harper J.W., Burton J.L., Solomon M.J. The anaphase-promoting complex: it's not just for mitosis any more. Genes Dev. 16:2002;2179-2206
    • (2002) Genes Dev. , vol.16 , pp. 2179-2206
    • Harper, J.W.1    Burton, J.L.2    Solomon, M.J.3
  • 5
    • 0033567387 scopus 로고    scopus 로고
    • Whose end is destruction: Cell division and the anaphase-promoting complex
    • Zachariae W., Nasmyth K. Whose end is destruction: cell division and the anaphase-promoting complex. Genes Dev. 13:1999;2039-2058
    • (1999) Genes Dev. , vol.13 , pp. 2039-2058
    • Zachariae, W.1    Nasmyth, K.2
  • 6
    • 0344668551 scopus 로고    scopus 로고
    • Securin and B-cyclin/CDK are the only essential targets of the APC
    • Thornton B.R., Toczyski D.P. Securin and B-cyclin/CDK are the only essential targets of the APC. Nat. Cell Biol. 5:2003;1090-1094
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1090-1094
    • Thornton, B.R.1    Toczyski, D.P.2
  • 7
    • 1642458099 scopus 로고    scopus 로고
    • Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells
    • Lindon C., Pines J. Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J. Cell Biol. 164:2004;233-241
    • (2004) J. Cell Biol. , vol.164 , pp. 233-241
    • Lindon, C.1    Pines, J.2
  • 8
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:1999;435-467
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 12
    • 0033120027 scopus 로고    scopus 로고
    • ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity
    • Ohta T., Michel J.J., Schottelius A.J., Xiong Y. ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol. Cell. 3:1999;535-541
    • (1999) Mol. Cell , vol.3 , pp. 535-541
    • Ohta, T.1    Michel, J.J.2    Schottelius, A.J.3    Xiong, Y.4
  • 14
    • 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 A.V., Mann M., Peters J.M. 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. 97:2000;8973-8978
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8973-8978
    • Gmachl, M.1    Gieffers, C.2    Podtelejnikov, A.V.3    Mann, M.4    Peters, J.M.5
  • 15
    • 0033120593 scopus 로고    scopus 로고
    • Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha
    • Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.Q. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha. Mol. Cell. 3:1999;527-533
    • (1999) Mol. Cell , vol.3 , pp. 527-533
    • Tan, P.1    Fuchs, S.Y.2    Chen, A.3    Wu, K.4    Gomez, C.5    Ronai, Z.6    Pan, Z.Q.7
  • 19
    • 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., Li B., Bharadwaj R., Zhu H., Ozkan E., Hakala K., Deisenhofer J., Yu H. APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex. Mol. Biol. Cell. 12:2001;3839-3851
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3839-3851
    • Tang, Z.1    Li, B.2    Bharadwaj, R.3    Zhu, H.4    Ozkan, E.5    Hakala, K.6    Deisenhofer, J.7    Yu, H.8
  • 21
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu L., Wei Y., Reboul J., Vaglio P., Shin T.H., Vidal M., Elledge S.J., Harper J.W. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature. 425:2003;316-321
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5    Vidal, M.6    Elledge, S.J.7    Harper, J.W.8
  • 22
    • 0026068805 scopus 로고
    • Naming a targeting signal
    • Varshavsky A. Naming a targeting signal. Cell. 64:1991;13-15
    • (1991) Cell , vol.64 , pp. 13-15
    • Varshavsky, A.1
  • 23
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumor suppressor function
    • Stebbins C.E., Kaelin W.G. Jr., Pavletich N.P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science. 284:1999;455-461
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 25
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer R., Wee S., Anderson S., Yates J., Wolf D.A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell. 12:2003;783-790
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 26
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • Furukawa M., He Y.J., Borchers C., Xiong Y. Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. Nat. Cell Biol. 5:2003;1001-1007
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 27
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell. 113:2003;357-367
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 28
    • 0037513423 scopus 로고    scopus 로고
    • Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans
    • Pintard L., Kurz T., Glaser S., Willis J.H., Peter M., Bowerman B. Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans. Curr. Biol. 13:2003;911-921
    • (2003) Curr. Biol. , vol.13 , pp. 911-921
    • Pintard, L.1    Kurz, T.2    Glaser, S.3    Willis, J.H.4    Peter, M.5    Bowerman, B.6
  • 29
    • 4444243577 scopus 로고    scopus 로고
    • CUL-2 and ZYG-11 promote meiotic anaphase II and the proper placement of the anterior-posterior axis in C. elegans
    • Liu J., Vasudevan S., Kipreos E.T. CUL-2 and ZYG-11 promote meiotic anaphase II and the proper placement of the anterior-posterior axis in C. elegans. Development. 131:2004;3513-3525
    • (2004) Development , vol.131 , pp. 3513-3525
    • Liu, J.1    Vasudevan, S.2    Kipreos, E.T.3
  • 30
    • 4444366942 scopus 로고    scopus 로고
    • Zyg-11 and cul-2 regulate progression through meiosis II and polarity establishment in C. elegans
    • Sonneville R., Gonczy P. zyg-11 and cul-2 regulate progression through meiosis II and polarity establishment in C. elegans. Development. 131:2004;3527-3543
    • (2004) Development , vol.131 , pp. 3527-3543
    • Sonneville, R.1    Gonczy, P.2
  • 31
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M., Murray A.W., Kirschner M.W. Cyclin is degraded by the ubiquitin pathway. Nature. 349:1991;132-138
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 32
    • 0034654399 scopus 로고    scopus 로고
    • The KEN box: An APC recognition signal distinct from the D box targeted by Cdh1
    • Pfleger C.M., Kirschner M.W. The KEN box: an APC recognition signal distinct from the D box targeted by Cdh1. Genes Dev. 14:2000;655-665
    • (2000) Genes Dev. , vol.14 , pp. 655-665
    • Pfleger, C.M.1    Kirschner, M.W.2
  • 33
    • 0037450770 scopus 로고    scopus 로고
    • Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition
    • Passmore L.A., McCormack E.A., Au S.W., Paul A., Willison K.R., Harper J.W., Barford D. Doc1 mediates the activity of the anaphase-promoting complex by contributing to substrate recognition. EMBO J. 22:2003;786-796
    • (2003) EMBO J. , vol.22 , pp. 786-796
    • Passmore, L.A.1    McCormack, E.A.2    Au, S.W.3    Paul, A.4    Willison, K.R.5    Harper, J.W.6    Barford, D.7
  • 34
    • 0042921286 scopus 로고    scopus 로고
    • TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1
    • Vodermaier H.C., Gieffers C., Maurer-Stroh S., Eisenhaber F., Peters J.M. TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1. Curr. Biol. 13:2003;1459-1468
    • (2003) Curr. Biol. , vol.13 , pp. 1459-1468
    • Vodermaier, H.C.1    Gieffers, C.2    Maurer-Stroh, S.3    Eisenhaber, F.4    Peters, J.M.5
  • 35
    • 0035903652 scopus 로고    scopus 로고
    • Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC
    • Schwab M., Neutzner M., Mocker D., Seufert W. Yeast Hct1 recognizes the mitotic cyclin Clb2 and other substrates of the ubiquitin ligase APC. EMBO J. 20:2001;5165-5175
    • (2001) EMBO J. , vol.20 , pp. 5165-5175
    • Schwab, M.1    Neutzner, M.2    Mocker, D.3    Seufert, W.4
  • 36
    • 0035884001 scopus 로고    scopus 로고
    • D box and KEN box motifs in budding yeast Hsl1p are required for APC-mediated degradation and direct binding to Cdc20p and Cdh1p
    • Burton J.L., Solomon M.J. D box and KEN box motifs in budding yeast Hsl1p are required for APC-mediated degradation and direct binding to Cdc20p and Cdh1p. Genes Dev. 15:2001;2381-2395
    • (2001) Genes Dev. , vol.15 , pp. 2381-2395
    • Burton, J.L.1    Solomon, M.J.2
  • 37
    • 0035883946 scopus 로고    scopus 로고
    • Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex
    • Pfleger C.M., Lee E., Kirschner M.W. Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex. Genes Dev. 15:2001;2396-2407
    • (2001) Genes Dev. , vol.15 , pp. 2396-2407
    • Pfleger, C.M.1    Lee, E.2    Kirschner, M.W.3
  • 38
    • 0035806974 scopus 로고    scopus 로고
    • The anaphase inhibitor Pds1 binds to the APC/C-associated protein Cdc20 in a destruction box-dependent manner
    • Hilioti Z., Chung Y.S., Mochizuki Y., Hardy C.F., Cohen-Fix O. The anaphase inhibitor Pds1 binds to the APC/C-associated protein Cdc20 in a destruction box-dependent manner. Curr. Biol. 11:2001;1347-1352
    • (2001) Curr. Biol. , vol.11 , pp. 1347-1352
    • Hilioti, Z.1    Chung, Y.S.2    Mochizuki, Y.3    Hardy, C.F.4    Cohen-Fix, O.5
  • 39
    • 0035899899 scopus 로고    scopus 로고
    • Cell cycle: Waiters serving the Destruction machinery
    • Vodermaier H.C. Cell cycle: Waiters serving the Destruction machinery. Curr. Biol. 11:2001;R834-R837
    • (2001) Curr. Biol. , vol.11
    • Vodermaier, H.C.1
  • 40
    • 0036850233 scopus 로고    scopus 로고
    • The Doc1 subunit is a processivity factor for the anaphase-promoting complex
    • Carroll C.W., Morgan D.O. The Doc1 subunit is a processivity factor for the anaphase-promoting complex. Nat. Cell Biol. 4:2002;880-887
    • (2002) Nat. Cell Biol. , vol.4 , pp. 880-887
    • Carroll, C.W.1    Morgan, D.O.2
  • 41
    • 1642523634 scopus 로고    scopus 로고
    • Cell cycle-regulated recognition of the destruction box of cyclin B by the APC/C in Xenopus egg extracts
    • Yamano H., Gannon J., Mahbubani H., Hunt T. Cell cycle-regulated recognition of the destruction box of cyclin B by the APC/C in Xenopus egg extracts. Mol. Cell. 13:2004;137-147
    • (2004) Mol. Cell , vol.13 , pp. 137-147
    • Yamano, H.1    Gannon, J.2    Mahbubani, H.3    Hunt, T.4
  • 42
    • 0242551536 scopus 로고    scopus 로고
    • Ratchets and clocks: The cell cycle, ubiquitylation and protein turnover
    • Reed S.I. Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover. Nat. Rev. Mol. Cell Biol. 4:2003;855-864
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 855-864
    • Reed, S.I.1
  • 46
    • 0034717570 scopus 로고    scopus 로고
    • Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex
    • Rudner A.D., Murray A.W. Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex. J. Cell Biol. 149:2000;1377-1390
    • (2000) J. Cell Biol. , vol.149 , pp. 1377-1390
    • Rudner, A.D.1    Murray, A.W.2
  • 47
    • 0037013326 scopus 로고    scopus 로고
    • The cyclin-ubiquitin ligase activity of cyclosome/APC is jointly activated by protein kinases Cdk1-cyclin B and Plk
    • Golan A., Yudkovsky Y., Hershko A. The cyclin-ubiquitin ligase activity of cyclosome/APC is jointly activated by protein kinases Cdk1-cyclin B and Plk. J. Biol. Chem. 277:2002;15552-15557
    • (2002) J. Biol. Chem. , vol.277 , pp. 15552-15557
    • Golan, A.1    Yudkovsky, Y.2    Hershko, A.3
  • 49
    • 0037166938 scopus 로고    scopus 로고
    • Human securin proteolysis is controlled by the spindle checkpoint and reveals when the APC/C switches from activation by Cdc20 to Cdh1
    • Hagting A., Den Elzen N., Vodermaier H.C., Waizenegger I.C., Peters J.M., Pines J. Human securin proteolysis is controlled by the spindle checkpoint and reveals when the APC/C switches from activation by Cdc20 to Cdh1. J. Cell Biol. 157:2002;1125-1137
    • (2002) J. Cell Biol. , vol.157 , pp. 1125-1137
    • Hagting, A.1    Den Elzen, N.2    Vodermaier, H.C.3    Waizenegger, I.C.4    Peters, J.M.5    Pines, J.6
  • 50
    • 0033163714 scopus 로고    scopus 로고
    • Four-dimensional control of the cell cycle
    • Pines J. Four-dimensional control of the cell cycle. Nat. Cell Biol. 1:1999;E73-E79
    • (1999) Nat. Cell Biol. , vol.1
    • Pines, J.1
  • 51
    • 0037099031 scopus 로고    scopus 로고
    • The dynamic localisation of the Drosophila APC/C: Evidence for the existence of multiple complexes that perform distinct functions and are differentially localised
    • Huang J.Y., Raff J.W. The dynamic localisation of the Drosophila APC/C: evidence for the existence of multiple complexes that perform distinct functions and are differentially localised. J. Cell Sci. 115:2002;2847-2856
    • (2002) J. Cell Sci. , vol.115 , pp. 2847-2856
    • Huang, J.Y.1    Raff, J.W.2
  • 52
    • 0037166933 scopus 로고    scopus 로고
    • The roles of Fzy/Cdc20 and Fzr/Cdh1 in regulating the destruction of cyclin B in space and time
    • Raff J.W., Jeffers K., Huang J.Y. The roles of Fzy/Cdc20 and Fzr/Cdh1 in regulating the destruction of cyclin B in space and time. J. Cell Biol. 157:2002;1139-1149
    • (2002) J. Cell Biol. , vol.157 , pp. 1139-1149
    • Raff, J.W.1    Jeffers, K.2    Huang, J.Y.3
  • 53
    • 0036789555 scopus 로고    scopus 로고
    • The spindle checkpoint: Structural insights into dynamic signalling
    • Musacchio A., Hardwick K.G. The spindle checkpoint: structural insights into dynamic signalling. Nat. Rev. Mol. Cell Biol. 3:2002;731-741
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 731-741
    • Musacchio, A.1    Hardwick, K.G.2
  • 54
    • 0036902234 scopus 로고    scopus 로고
    • Regulation of APC-Cdc20 by the spindle checkpoint
    • Yu H. Regulation of APC-Cdc20 by the spindle checkpoint. Curr. Opin. Cell Biol. 14:2002;706-714
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 706-714
    • Yu, H.1
  • 55
    • 0035795414 scopus 로고    scopus 로고
    • Cyclin a is destroyed in prometaphase and can delay chromosome alignment and anaphase
    • den Elzen N., Pines J. Cyclin A is destroyed in prometaphase and can delay chromosome alignment and anaphase. J. Cell Biol. 153:2001;121-136
    • (2001) J. Cell Biol. , vol.153 , pp. 121-136
    • Den Elzen, N.1    Pines, J.2
  • 56
    • 0035795408 scopus 로고    scopus 로고
    • Anaphase-promoting complex/cyclosome-dependent proteolysis of human cyclin a starts at the beginning of mitosis and is not subject to the spindle assembly checkpoint
    • Geley S., Kramer E., Gieffers C., Gannon J., Peters J.M., Hunt T. Anaphase-promoting complex/cyclosome-dependent proteolysis of human cyclin A starts at the beginning of mitosis and is not subject to the spindle assembly checkpoint. J. Cell Biol. 153:2001;137-148
    • (2001) J. Cell Biol. , vol.153 , pp. 137-148
    • Geley, S.1    Kramer, E.2    Gieffers, C.3    Gannon, J.4    Peters, J.M.5    Hunt, T.6
  • 57
    • 0037126610 scopus 로고    scopus 로고
    • APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box
    • Hames R.S., Wattam S.L., Yamano H., Bacchieri R., Fry A.M. APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box. EMBO J. 20:2001;7117-7127
    • (2001) EMBO J. , vol.20 , pp. 7117-7127
    • Hames, R.S.1    Wattam, S.L.2    Yamano, H.3    Bacchieri, R.4    Fry, A.M.5
  • 60
    • 0035878111 scopus 로고    scopus 로고
    • MAD2B is an inhibitor of the anaphase-promoting complex
    • Chen J., Fang G. MAD2B is an inhibitor of the anaphase-promoting complex. Genes Dev. 15:2001;1765-1770
    • (2001) Genes Dev. , vol.15 , pp. 1765-1770
    • Chen, J.1    Fang, G.2
  • 61
    • 0035878126 scopus 로고    scopus 로고
    • Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: A novel mechanism for regulating Cdh1
    • Pfleger C.M., Salic A., Lee E., Kirschner M.W. Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1. Genes Dev. 15:2001;1759-1764
    • (2001) Genes Dev. , vol.15 , pp. 1759-1764
    • Pfleger, C.M.1    Salic, A.2    Lee, E.3    Kirschner, M.W.4
  • 62
    • 0035370009 scopus 로고    scopus 로고
    • Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex
    • Reimann J.D., Freed E., Hsu J.Y., Kramer E.R., Peters J.M., Jackson P.K. Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex. Cell. 105:2001;645-655
    • (2001) Cell , vol.105 , pp. 645-655
    • Reimann, J.D.1    Freed, E.2    Hsu, J.Y.3    Kramer, E.R.4    Peters, J.M.5    Jackson, P.K.6
  • 63
    • 0035893917 scopus 로고    scopus 로고
    • Emi1 regulates the anaphase-promoting complex by a different mechanism than Mad2 proteins
    • Reimann J.D., Gardner B.E., Margottin-Goguet F., Jackson P.K. Emi1 regulates the anaphase-promoting complex by a different mechanism than Mad2 proteins. Genes Dev. 15:2001;3278-3285
    • (2001) Genes Dev. , vol.15 , pp. 3278-3285
    • Reimann, J.D.1    Gardner, B.E.2    Margottin-Goguet, F.3    Jackson, P.K.4
  • 64
    • 0036007113 scopus 로고    scopus 로고
    • Rca1 inhibits APC-Cdh1(Fzr) and is required to prevent cyclin degradation in G2
    • Grosskortenhaus R., Sprenger F. Rca1 inhibits APC-Cdh1(Fzr) and is required to prevent cyclin degradation in G2. Dev. Cell. 2:2002;29-40
    • (2002) Dev. Cell , vol.2 , pp. 29-40
    • Grosskortenhaus, R.1    Sprenger, F.2
  • 65
    • 0036095082 scopus 로고    scopus 로고
    • E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APC(Cdh1)
    • Hsu J.Y., Reimann J.D., Sorensen C.S., Lukas J., Jackson P.K. E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APC(Cdh1). Nat. Cell Biol. 4:2002;358-366
    • (2002) Nat. Cell Biol. , vol.4 , pp. 358-366
    • Hsu, J.Y.1    Reimann, J.D.2    Sorensen, C.S.3    Lukas, J.4    Jackson, P.K.5
  • 66
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • Cope G.A., Deshaies R.J. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell. 114:2003;663-671
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 67
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: An assembly and maintenance platform for cullin ubiquitin ligases?
    • Wolf D.A., Zhou C., Wee S. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat. Cell Biol. 5:2003;1029-1033
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 69
    • 0032215237 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases
    • Zhou P., Howley P.M. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell. 2:1998;571-580
    • (1998) Mol. Cell , vol.2 , pp. 571-580
    • Zhou, P.1    Howley, P.M.2
  • 70
    • 0033529757 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism
    • Galan J.M., Peter M. Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc. Natl. Acad. Sci. USA. 96:1999;9124-9129
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9124-9129
    • Galan, J.M.1    Peter, M.2
  • 71
    • 1642442587 scopus 로고    scopus 로고
    • Stability of homologue of Slimb F-box protein is regulated by availability of its substrate
    • Li Y., Gazdoiu S., Pan Z.Q., Fuchs S.Y. Stability of homologue of Slimb F-box protein is regulated by availability of its substrate. J. Biol. Chem. 279:2004;11074-11080
    • (2004) J. Biol. Chem. , vol.279 , pp. 11074-11080
    • Li, Y.1    Gazdoiu, S.2    Pan, Z.Q.3    Fuchs, S.Y.4
  • 72
    • 0037119404 scopus 로고    scopus 로고
    • A molecular basis for stabilization of the von Hippel-Lindau (VHL) tumor suppressor protein by components of the VHL ubiquitin ligase
    • Kamura T., Brower C.S., Conaway R.C., Conaway J.W. A molecular basis for stabilization of the von Hippel-Lindau (VHL) tumor suppressor protein by components of the VHL ubiquitin ligase. J. Biol. Chem. 277:2002;30388-30393
    • (2002) J. Biol. Chem. , vol.277 , pp. 30388-30393
    • Kamura, T.1    Brower, C.S.2    Conaway, R.C.3    Conaway, J.W.4
  • 73
    • 0034675922 scopus 로고    scopus 로고
    • The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: Evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts
    • Wirbelauer C., Sutterluty H., Blondel M., Gstaiger M., Peter M., Reymond F., Krek W. The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts. EMBO J. 19:2000;5362-5375
    • (2000) EMBO J. , vol.19 , pp. 5362-5375
    • Wirbelauer, C.1    Sutterluty, H.2    Blondel, M.3    Gstaiger, M.4    Peter, M.5    Reymond, F.6    Krek, W.7
  • 74
    • 0037534899 scopus 로고    scopus 로고
    • Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase
    • Margottin-Goguet F., Hsu J.Y., Loktev A., Hsieh H.M., Reimann J.D., Jackson P.K. Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase. Dev. Cell. 4:2003;813-826
    • (2003) Dev. Cell , vol.4 , pp. 813-826
    • Margottin-Goguet, F.1    Hsu, J.Y.2    Loktev, A.3    Hsieh, H.M.4    Reimann, J.D.5    Jackson, P.K.6
  • 75
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase
    • Bashir T., Dorrello N.V., Amador V., Guardavaccaro D., Pagano M. Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase. Nature. 428:2004;190-193
    • (2004) Nature , vol.428 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amador, V.3    Guardavaccaro, D.4    Pagano, M.5
  • 76
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
    • Wei W., Ayad N.G., Wan Y., Zhang G.J., Kirschner M.W., Kaelin W.G. Jr. Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature. 428:2004;194-198
    • (2004) Nature , vol.428 , pp. 194-198
    • Wei, W.1    Ayad, N.G.2    Wan, Y.3    Zhang, G.J.4    Kirschner, M.W.5    Kaelin Jr., W.G.6
  • 78
    • 0030679670 scopus 로고    scopus 로고
    • Cell cycle-regulated expression, phosphorylation, and degradation of p55Cdc. A mammalian homolog of CDC20/Fizzy/slp1
    • Weinstein J. Cell cycle-regulated expression, phosphorylation, and degradation of p55Cdc. A mammalian homolog of CDC20/Fizzy/slp1. J. Biol. Chem. 272:1997;28501-28511
    • (1997) J. Biol. Chem. , vol.272 , pp. 28501-28511
    • Weinstein, J.1
  • 79
    • 0032543552 scopus 로고    scopus 로고
    • The regulation of Cdc20 proteolysis reveals a role for APC components Cdc23 and Cdc27 during S phase and early mitosis
    • Prinz S., Hwang E.S., Visintin R., Amon A. The regulation of Cdc20 proteolysis reveals a role for APC components Cdc23 and Cdc27 during S phase and early mitosis. Curr. Biol. 8:1998;750-760
    • (1998) Curr. Biol. , vol.8 , pp. 750-760
    • Prinz, S.1    Hwang, E.S.2    Visintin, R.3    Amon, A.4
  • 80
    • 0032473568 scopus 로고    scopus 로고
    • The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae
    • Shirayama M., Zachariae W., Ciosk R., Nasmyth K. The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae. EMBO J. 17:1998;1336-1349
    • (1998) EMBO J. , vol.17 , pp. 1336-1349
    • Shirayama, M.1    Zachariae, W.2    Ciosk, R.3    Nasmyth, K.4
  • 81
    • 0033969432 scopus 로고    scopus 로고
    • Cdc20 protein contains a destruction-box but, unlike Clb2, its proteolysisis not acutely dependent on the activity of anaphase-promoting complex
    • Goh P.Y., Lim H.H., Surana U. Cdc20 protein contains a destruction-box but, unlike Clb2, its proteolysisis not acutely dependent on the activity of anaphase-promoting complex. Eur. J. Biochem. 267:2000;434-449
    • (2000) Eur. J. Biochem. , vol.267 , pp. 434-449
    • Goh, P.Y.1    Lim, H.H.2    Surana, U.3
  • 82
    • 0034721656 scopus 로고    scopus 로고
    • Two distinct pathways remove mammalian cohesin from chromosome arms in prophase and from centromeres in anaphase
    • Waizenegger I.C., Hauf S., Meinke A., Peters J.M. Two distinct pathways remove mammalian cohesin from chromosome arms in prophase and from centromeres in anaphase. Cell. 103:2000;399-410
    • (2000) Cell , vol.103 , pp. 399-410
    • Waizenegger, I.C.1    Hauf, S.2    Meinke, A.3    Peters, J.M.4
  • 83
    • 2942690009 scopus 로고    scopus 로고
    • Spindle checkpoint regulates Cdc20p stability in Saccharomyces cerevisiae
    • Pan J., Chen R.H. Spindle checkpoint regulates Cdc20p stability in Saccharomyces cerevisiae. Genes Dev. 18:2004;1439-1451
    • (2004) Genes Dev. , vol.18 , pp. 1439-1451
    • Pan, J.1    Chen, R.H.2
  • 85
    • 0034254639 scopus 로고    scopus 로고
    • Fission yeast Fizzy-related protein srw1p is a G(1)-specific promoter of mitotic cyclin B degradation
    • Yamaguchi S., Okayama H., Nurse P. Fission yeast Fizzy-related protein srw1p is a G(1)-specific promoter of mitotic cyclin B degradation. EMBO J. 19:2000;3968-3977
    • (2000) EMBO J. , vol.19 , pp. 3968-3977
    • Yamaguchi, S.1    Okayama, H.2    Nurse, P.3
  • 86
    • 0033844911 scopus 로고    scopus 로고
    • Cell cycle-dependent expression of mammalian E2-C regulated by the anaphase-promoting complex/cyclosome
    • Yamanaka A., Hatakeyama S., Kominami K., Kitagawa M., Matsumoto M., Nakayama K. Cell cycle-dependent expression of mammalian E2-C regulated by the anaphase-promoting complex/cyclosome. Mol. Biol. Cell. 11:2000;2821-2831
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2821-2831
    • Yamanaka, A.1    Hatakeyama, S.2    Kominami, K.3    Kitagawa, M.4    Matsumoto, M.5    Nakayama, K.6
  • 87
    • 0034515308 scopus 로고    scopus 로고
    • The spike of S phase cyclin Cig2 expression at the G1-S border in fission yeast requires both APC and SCF ubiquitin ligases
    • Yamano H., Kitamura K., Kominami K., Lehmann A., Katayama S., Hunt T., Toda T. The spike of S phase cyclin Cig2 expression at the G1-S border in fission yeast requires both APC and SCF ubiquitin ligases. Mol. Cell. 6:2000;1377-1387
    • (2000) Mol. Cell , vol.6 , pp. 1377-1387
    • Yamano, H.1    Kitamura, K.2    Kominami, K.3    Lehmann, A.4    Katayama, S.5    Hunt, T.6    Toda, T.7
  • 88
    • 2442483802 scopus 로고    scopus 로고
    • Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the fission yeast S-phase cyclin Cig2
    • Yamano H., Kominami K.I., Harrison C., Kitamura K., Katayama S., Dhut S., Hunt T., Toda T. Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the fission yeast S-phase cyclin Cig2. J. Biol. Chem. 279:2004;18974-18980
    • (2004) J. Biol. Chem. , vol.279 , pp. 18974-18980
    • Yamano, H.1    Kominami, K.I.2    Harrison, C.3    Kitamura, K.4    Katayama, S.5    Dhut, S.6    Hunt, T.7    Toda, T.8
  • 91
    • 0347361537 scopus 로고    scopus 로고
    • SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase
    • Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W. SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase. Genes Dev. 17:2003;3062-3074
    • (2003) Genes Dev. , vol.17 , pp. 3062-3074
    • Jin, J.1    Shirogane, T.2    Xu, L.3    Nalepa, G.4    Qin, J.5    Elledge, S.J.6    Harper, J.W.7
  • 93
    • 2542617641 scopus 로고    scopus 로고
    • Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome
    • Moshe Y., Boulaire J., Pagano M., Hershko A. Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome. Proc. Natl. Acad. Sci. USA. 101:2004;7937-7942
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7937-7942
    • Moshe, Y.1    Boulaire, J.2    Pagano, M.3    Hershko, A.4
  • 94
    • 0346882614 scopus 로고    scopus 로고
    • Wee1-dependent mechanisms required for coordination of cell growth and cell division
    • Kellogg D.R. Wee1-dependent mechanisms required for coordination of cell growth and cell division. J. Cell Sci. 116:2003;4883-4890
    • (2003) J. Cell Sci. , vol.116 , pp. 4883-4890
    • Kellogg, D.R.1
  • 95
    • 0032484097 scopus 로고    scopus 로고
    • Coupling of mitosis to the completion of S phase through Cdc34-mediated degradation of Wee1
    • Michael W.M., Newport J. Coupling of mitosis to the completion of S phase through Cdc34-mediated degradation of Wee1. Science. 282:1998;1886-1889
    • (1998) Science , vol.282 , pp. 1886-1889
    • Michael, W.M.1    Newport, J.2
  • 98
    • 0037452658 scopus 로고    scopus 로고
    • Conservation of mechanisms controlling entry into mitosis: Budding yeast wee1 delays entry into mitosis and is required for cell size control
    • Harvey S.L., Kellogg D.R. Conservation of mechanisms controlling entry into mitosis: budding yeast wee1 delays entry into mitosis and is required for cell size control. Curr. Biol. 13:2003;264-275
    • (2003) Curr. Biol. , vol.13 , pp. 264-275
    • Harvey, S.L.1    Kellogg, D.R.2
  • 99
    • 0034082458 scopus 로고    scopus 로고
    • Hsl1p, a Swe1p inhibitor, is degraded via the anaphase-promoting complex
    • Burton J.L., Solomon M.J. Hsl1p, a Swe1p inhibitor, is degraded via the anaphase-promoting complex. Mol. Cell. Biol. 20:2000;4614-4625
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4614-4625
    • Burton, J.L.1    Solomon, M.J.2
  • 100
    • 0035282915 scopus 로고    scopus 로고
    • GSK-3 kinase Mck1 and calcineurin coordinately mediate Hsl1 down-regulation by Ca2+ in budding yeast
    • Mizunuma M., Hirata D., Miyaoka R., Miyakawa T. GSK-3 kinase Mck1 and calcineurin coordinately mediate Hsl1 down-regulation by Ca2+ in budding yeast. EMBO J. 20:2001;1074-1085
    • (2001) EMBO J. , vol.20 , pp. 1074-1085
    • Mizunuma, M.1    Hirata, D.2    Miyaoka, R.3    Miyakawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.