메뉴 건너뛰기




Volumn 1773, Issue 6, 2007, Pages 844-852

Polycomb group protein RING1B is a direct substrate of Caspases-3 and -9

Author keywords

Caspase 3; Caspase 9; Nuclear localization; Polycomb group protein; Ring1B; Transcriptional repression

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; CASPASE 3; CASPASE 9; POLYCOMB GROUP PROTEIN; PROTEIN RING1B; UNCLASSIFIED DRUG;

EID: 34249738746     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.02.005     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 0034615555 scopus 로고    scopus 로고
    • Caspases-Controlling intracellular signals by protease zymogen activation
    • Stennicke H.R., and Salvesen G.S. Caspases-Controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta 1477 (2000) 299-306
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 299-306
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 2
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6 (1999) 1028-1042
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 3
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: a comprehensive update of caspase substrates
    • Fischer U., Janicke R.U., and Schulze-Osthoff K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10 (2003) 76-100
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 6
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • (see comment)
    • Sakahira H., Enari M., and Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. (see comment). Nature 391 (1998) 96-99
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 8
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel T., and Bokoch G.M. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276 (1997) 1571-1574
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 9
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., and Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 11
    • 0035798645 scopus 로고    scopus 로고
    • Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development
    • Nakanishi K., Maruyama M., Shibata T., and Morishima N. Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development. J. Biol. Chem. 276 (2001) 41237-41244
    • (2001) J. Biol. Chem. , vol.276 , pp. 41237-41244
    • Nakanishi, K.1    Maruyama, M.2    Shibata, T.3    Morishima, N.4
  • 13
    • 0642314384 scopus 로고    scopus 로고
    • Non-apoptotic functions of caspases in cellular proliferation and differentiation
    • Schwerk C., and Schulze-Osthoff K. Non-apoptotic functions of caspases in cellular proliferation and differentiation. Biochem. Pharmacol. 66 (2003) 1453-1458
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1453-1458
    • Schwerk, C.1    Schulze-Osthoff, K.2
  • 14
    • 0027485470 scopus 로고
    • Mechanisms of heritable gene repression during development of Drosophila
    • Paro R. Mechanisms of heritable gene repression during development of Drosophila. Curr. Opin. Cell Biol. 5 (1993) 999-1005
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 999-1005
    • Paro, R.1
  • 15
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., and Pirrotta V. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111 (2002) 185-196
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 16
    • 1842364897 scopus 로고    scopus 로고
    • Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain
    • Schoorlemmer J., Marcos-Gutierrez C., Were F., Martinez R., Garcia E., Satijn D.P., Otte A.P., and Vidal M. Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain. EMBO J. 16 (1997) 5930-5942
    • (1997) EMBO J. , vol.16 , pp. 5930-5942
    • Schoorlemmer, J.1    Marcos-Gutierrez, C.2    Were, F.3    Martinez, R.4    Garcia, E.5    Satijn, D.P.6    Otte, A.P.7    Vidal, M.8
  • 17
    • 0033956389 scopus 로고    scopus 로고
    • Identification and analysis of a third mouse Polycomb gene, MPc3
    • Hemenway C.S., Halligan B.W., Gould G.C., and Levy L.S. Identification and analysis of a third mouse Polycomb gene, MPc3. Gene 242 (2000) 31-40
    • (2000) Gene , vol.242 , pp. 31-40
    • Hemenway, C.S.1    Halligan, B.W.2    Gould, G.C.3    Levy, L.S.4
  • 18
    • 0032516241 scopus 로고    scopus 로고
    • The Bmi-1 oncoprotein interacts with dinG and MPh2: the role of RING finger domains
    • Hemenway C.S., Halligan B.W., and Levy L.S. The Bmi-1 oncoprotein interacts with dinG and MPh2: the role of RING finger domains. Oncogene 16 (1998) 2541-2547
    • (1998) Oncogene , vol.16 , pp. 2541-2547
    • Hemenway, C.S.1    Halligan, B.W.2    Levy, L.S.3
  • 19
    • 0042329972 scopus 로고    scopus 로고
    • Dissociation of mammalian Polycomb-group proteins, Ring1B and Rae28/Ph1, from the chromatin correlates with configuration changes of the chromatin in mitotic and meiotic prophase
    • Miyagishima H., Isono K., Fujimura Y., Iyo M., Takihara Y., Masumoto H., Vidal M., and Koseki H. Dissociation of mammalian Polycomb-group proteins, Ring1B and Rae28/Ph1, from the chromatin correlates with configuration changes of the chromatin in mitotic and meiotic prophase. Histochem. Cell Biol. 120 (2003) 111-119
    • (2003) Histochem. Cell Biol. , vol.120 , pp. 111-119
    • Miyagishima, H.1    Isono, K.2    Fujimura, Y.3    Iyo, M.4    Takihara, Y.5    Masumoto, H.6    Vidal, M.7    Koseki, H.8
  • 20
    • 0344223442 scopus 로고    scopus 로고
    • RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1
    • Garcia E., Marcos-Gutierrez C., del Mar Lorente M., Moreno J.C., and Vidal M. RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1. EMBO J. 18 (1999) 3404-3418
    • (1999) EMBO J. , vol.18 , pp. 3404-3418
    • Garcia, E.1    Marcos-Gutierrez, C.2    del Mar Lorente, M.3    Moreno, J.C.4    Vidal, M.5
  • 21
    • 0036668471 scopus 로고    scopus 로고
    • MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation
    • Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., and Koga H. MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation. Genes Cells 7 (2002) 835-850
    • (2002) Genes Cells , vol.7 , pp. 835-850
    • Akasaka, T.1    Takahashi, N.2    Suzuki, M.3    Koseki, H.4    Bodmer, R.5    Koga, H.6
  • 23
    • 0035839021 scopus 로고    scopus 로고
    • E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme
    • Lee S.J., Choi J.Y., Sung Y.M., Park H., Rhim H., and Kang S. E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme. FEBS Lett. 503 (2001) 61-64
    • (2001) FEBS Lett. , vol.503 , pp. 61-64
    • Lee, S.J.1    Choi, J.Y.2    Sung, Y.M.3    Park, H.4    Rhim, H.5    Kang, S.6
  • 24
    • 0028209308 scopus 로고
    • Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells
    • Bunker C.A., and Kingston R.E. Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells. Mol. Cell. Biol. 14 (1994) 1721-1732
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1721-1732
    • Bunker, C.A.1    Kingston, R.E.2
  • 25
    • 0028046994 scopus 로고
    • Molecular mechanisms of cellular determination: their relation to chromatin structure and parental imprinting
    • Singh P.B. Molecular mechanisms of cellular determination: their relation to chromatin structure and parental imprinting. J. Cell. Sci. 107 Pt. 10 (1994) 2653-2668
    • (1994) J. Cell. Sci. , vol.107 , Issue.PART 10 , pp. 2653-2668
    • Singh, P.B.1
  • 26
    • 0041624288 scopus 로고    scopus 로고
    • Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
    • Min J., Zhang Y., and Xu R.M. Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev. 17 (2003) 1823-1828
    • (2003) Genes Dev. , vol.17 , pp. 1823-1828
    • Min, J.1    Zhang, Y.2    Xu, R.M.3
  • 27
    • 2342475666 scopus 로고    scopus 로고
    • Polycomb complexes and silencing mechanisms
    • Lund A.H., and van Lohuizen M. Polycomb complexes and silencing mechanisms. Curr. Opin. Cell Biol. 16 (2004) 239-246
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 239-246
    • Lund, A.H.1    van Lohuizen, M.2
  • 28
    • 24744455483 scopus 로고    scopus 로고
    • Epigenome programming by Polycomb and Trithorax proteins
    • Cernilogar F.M., and Orlando V. Epigenome programming by Polycomb and Trithorax proteins. Biochem. Cell Biol. 83 (2005) 322-331
    • (2005) Biochem. Cell Biol. , vol.83 , pp. 322-331
    • Cernilogar, F.M.1    Orlando, V.2
  • 31
    • 11144237618 scopus 로고    scopus 로고
    • Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation
    • Fang J., Chen T., Chadwick B., Li E., and Zhang Y. Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation. J. Biol. Chem. 279 (2004) 52812-52815
    • (2004) J. Biol. Chem. , vol.279 , pp. 52812-52815
    • Fang, J.1    Chen, T.2    Chadwick, B.3    Li, E.4    Zhang, Y.5
  • 34
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: their intracellular localization and translocation during apoptosis
    • Zhivotovsky B., Samali A., Gahm A., and Orrenius S. Caspases: their intracellular localization and translocation during apoptosis. Cell Death Diff. 6 (1999) 644-651
    • (1999) Cell Death Diff. , vol.6 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.