메뉴 건너뛰기




Volumn 319, Issue 1-2, 2008, Pages 69-77

PHB2 interacts with RNF2 and represses CP2c-stimulated transcription

Author keywords

CP2; PHB2; RNF2; Transcriptional repressor

Indexed keywords

ALPHA GLOBIN; LUCIFERASE; POLYCOMB GROUP PROTEIN; PROHIBITIN; PROHIBITIN 2; PROTEIN RNF2; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR CP2C; UNCLASSIFIED DRUG;

EID: 55649097534     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-008-9878-2     Document Type: Article
Times cited : (21)

References (20)
  • 1
    • 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
    • doi: 10.1093/emboj/16.19.5930
    • Schoorlemmer J, Marcos-Gutierrez C, Were F, Martinez R, Garcia E, Satijn DP et al (1997) Ring1A is a transcriptional repressor that interacts with the polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain. EMBO J 16:5930-5942. doi: 10.1093/emboj/ 16.19.5930
    • (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
  • 2
    • 0032927872 scopus 로고    scopus 로고
    • RING1 interacts with multiple polycomb-group proteins and displays tumorigenic activity
    • Satijn DP, Otte AP (1999) RING1 interacts with multiple polycomb-group proteins and displays tumorigenic activity. Mol Cell Biol 19:57-68
    • (1999) Mol Cell Biol , vol.19 , pp. 57-68
    • Satijn, D.P.1    Otte, A.P.2
  • 3
    • 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
    • doi: 10.1093/emboj/18.12.3404
    • Garcia E, Marcos-Gutierrez C, del Mar Lorente M, Moreno JC, Vidal M (1999) RYBP, a new repressor protein that interacts with components of the mammalian polycomb complex, and with the transcription factor YY1. EMBO J 18:3404-3418. doi: 10.1093/emboj/18.12.3404
    • (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
  • 4
    • 0345269795 scopus 로고    scopus 로고
    • Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition
    • doi: 10.1073/pnas.0434312100
    • Voncken JW, Roelen BA, Roefs M, de Vries S, Verhoeven E, Marino S et al (2003) Rnf2 (Ring1b) deficiency causes gastrulation arrest and cell cycle inhibition. Proc Natl Acad Sci USA 100:2468-2473. doi: 10.1073/ pnas.0434312100
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2468-2473
    • Voncken, J.W.1    Roelen, B.A.2    Roefs, M.3    de Vries, S.4    Verhoeven, E.5    Marino, S.6
  • 5
    • 0035839021 scopus 로고    scopus 로고
    • E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme
    • doi: 10.1016/S0014-5793(01)02689-8
    • Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S (2001) E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme. FEBS Lett 503:61-64. doi: 10.1016/ S0014-5793(01)02689-8
    • (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
  • 6
    • 7244234099 scopus 로고    scopus 로고
    • Role of histone H2A ubiquitination in polycomb silencing
    • doi: 10.1038/nature02985
    • Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS et al (2004) Role of histone H2A ubiquitination in polycomb silencing. Nature 431:873-878. doi: 10.1038/nature02985
    • (2004) Nature , vol.431 , pp. 873-878
    • Wang, H.1    Wang, L.2    Erdjument-Bromage, H.3    Vidal, M.4    Tempst, P.5    Jones, R.S.6
  • 7
    • 7744228427 scopus 로고    scopus 로고
    • Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation
    • doi: 10.1016/j.devcel.2004.10.005
    • de Napoles M, Mermoud JE, Wakao R, Tang YA, Endoh M, Appanah R et al (2004) Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation. Dev Cell 7:663-676. doi: 10.1016/j.devcel.2004.10.005
    • (2004) Dev Cell , vol.7 , pp. 663-676
    • de Napoles, M.1    Mermoud, J.E.2    Wakao, R.3    Tang, Y.A.4    Endoh, M.5    Appanah, R.6
  • 8
    • 0036177760 scopus 로고    scopus 로고
    • Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors
    • doi: 10.1128/MCB.22.6.1936-1946.2002
    • Tuckfield A, Clouston DR, Wilanowski TM, Zhao LL, Cunningham JM, Jane SM (2002) Binding of the RING polycomb proteins to specific target genes in complex with the grainyhead-like family of developmental transcription factors. Mol Cell Biol 22:1936-1946. doi: 10.1128/MCB.22.6.1936-1946.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 1936-1946
    • Tuckfield, A.1    Clouston, D.R.2    Wilanowski, T.M.3    Zhao, L.L.4    Cunningham, J.M.5    Jane, S.M.6
  • 9
    • 21744459534 scopus 로고    scopus 로고
    • Erythroid cell-specific alpha-globin gene regulation by the CP2 transcription factor family
    • doi: 10.1128/MCB.25.14.6005-6020.2005
    • Kang HC, Chae JH, Lee YH, Park MA, Shin JH, Kim SH et al (2005) Erythroid cell-specific alpha-globin gene regulation by the CP2 transcription factor family. Mol Cell Biol 25:6005-6020. doi: 10.1128/ MCB.25.14.6005-6020.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 6005-6020
    • Kang, H.C.1    Chae, J.H.2    Lee, Y.H.3    Park, M.A.4    Shin, J.H.5    Kim, S.H.6
  • 10
    • 34249715325 scopus 로고    scopus 로고
    • Proteomics analysis of Ring1B/Rnf2 interactors identifies a novel complex with the Fbxl10/Jhdm1B histone demethylase and the Bcl6 interacting corepressor
    • doi: 10.1074/mcp.M600275-MCP200
    • Sanchez C, Sanchez I, Demmers JA, Rodriguez P, Strouboulis J, Vidal M (2007) Proteomics analysis of Ring1B/Rnf2 interactors identifies a novel complex with the Fbxl10/Jhdm1B histone demethylase and the Bcl6 interacting corepressor. Mol Cell Proteomics 6:820-834. doi: 10.1074/ mcp.M600275-MCP200
    • (2007) Mol Cell Proteomics , vol.6 , pp. 820-834
    • Sanchez, C.1    Sanchez, I.2    Demmers, J.A.3    Rodriguez, P.4    Strouboulis, J.5    Vidal, M.6
  • 11
    • 22544466122 scopus 로고    scopus 로고
    • E3 ubiquitin ligase RNF2 interacts with the S6′ proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6′
    • doi: 10.1042/BJ20041982
    • Lee SJ, Choi D, Rhim H, Kang S (2005) E3 ubiquitin ligase RNF2 interacts with the S6′ proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6′. Biochem J 389:457-463. doi: 10.1042/ BJ20041982
    • (2005) Biochem J , vol.389 , pp. 457-463
    • Lee, S.J.1    Choi, D.2    Rhim, H.3    Kang, S.4
  • 12
    • 40749108598 scopus 로고    scopus 로고
    • Prohibitin interacts with RNF2 and regulates E2F1 function via dual pathways
    • doi: 10.1038/sj.onc.1210806
    • Choi D, Lee SJ, Hong S, Kim IH, Kang S (2008) Prohibitin interacts with RNF2 and regulates E2F1 function via dual pathways. Oncogene 27:1716-1725. doi: 10.1038/sj.onc.1210806
    • (2008) Oncogene , vol.27 , pp. 1716-1725
    • Choi, D.1    Lee, S.J.2    Hong, S.3    Kim, I.H.4    Kang, S.5
  • 13
    • 33747196977 scopus 로고    scopus 로고
    • The Prohibitins: Emerging roles in diverse functions
    • doi: 10.1111/j.1582-4934.2006.tb00404.x
    • Mishra S, Murphy LC, Murphy LJ (2006) The Prohibitins: Emerging roles in diverse functions. J Cell Mol Med 10:353-363. doi: 10.1111/ j.1582-4934.2006.tb00404.x
    • (2006) J Cell Mol Med , vol.10 , pp. 353-363
    • Mishra, S.1    Murphy, L.C.2    Murphy, L.J.3
  • 14
    • 0033536054 scopus 로고    scopus 로고
    • An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens
    • doi: 10.1073/pnas.96.12.6947
    • Montano MM, Ekena K, Delage-Mourroux R, Chang W, Martini P, Katzenellenbogen BS (1999) An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens. Proc Natl Acad Sci USA 96:6947-6952. doi: 10.1073/ pnas.96.12.6947
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6947-6952
    • Montano, M.M.1    Ekena, K.2    Delage-Mourroux, R.3    Chang, W.4    Martini, P.5    Katzenellenbogen, B.S.6
  • 15
    • 0036161635 scopus 로고    scopus 로고
    • The mitochondrial PHB complex: Roles in mitochondrial respiratory complex assembly, ageing and degenerative disease
    • doi: 10.1007/s00018-002-8411-0
    • Nijtmans LG, Artal SM, Grivell LA, Coates PJ (2002) The mitochondrial PHB complex: Roles in mitochondrial respiratory complex assembly, ageing and degenerative disease. Cell Mol Life Sci 59:143-155. doi: 10.1007/ s00018-002-8411-0
    • (2002) Cell Mol Life Sci , vol.59 , pp. 143-155
    • Nijtmans, L.G.1    Artal, S.M.2    Grivell, L.A.3    Coates, P.J.4
  • 16
    • 2642511664 scopus 로고    scopus 로고
    • Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases
    • doi: 10.1074/jbc.M312300200
    • Kurtev V, Margueron R, Kroboth K, Ogris E, Cavailles V, Seiser C (2004) Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases. J Biol Chem 279:24834-24843. doi: 10.1074/jbc.M312300200
    • (2004) J Biol Chem , vol.279 , pp. 24834-24843
    • Kurtev, V.1    Margueron, R.2    Kroboth, K.3    Ogris, E.4    Cavailles, V.5    Seiser, C.6
  • 17
    • 0035914344 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm
    • doi: 10.1074/jbc.M105928200
    • Ko YG, Kang YS, Park H, Seol W, Kim J, Kim T et al (2001) Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm. J Biol Chem 276:39103-39106. doi: 10.1074/jbc.M105928200
    • (2001) J Biol Chem , vol.276 , pp. 39103-39106
    • Ko, Y.G.1    Kang, Y.S.2    Park, H.3    Seol, W.4    Kim, J.5    Kim, T.6
  • 18
    • 0034680931 scopus 로고    scopus 로고
    • Analysis of estrogen receptor interaction with a repressor of estrogen receptor activity (REA) and the regulation of estrogen receptor transcriptional activity by REA
    • doi: 10.1074/jbc.M001327200
    • Delage-Mourroux R, Martini PG, Choi I, Kraichely DM, Hoeksema J, Katzenellenbogen BS (2000) Analysis of estrogen receptor interaction with a repressor of estrogen receptor activity (REA) and the regulation of estrogen receptor transcriptional activity by REA. J Biol Chem 275:35848-35856. doi: 10.1074/jbc.M001327200
    • (2000) J Biol Chem , vol.275 , pp. 35848-35856
    • Delage-Mourroux, R.1    Martini, P.G.2    Choi, I.3    Kraichely, D.M.4    Hoeksema, J.5    Katzenellenbogen, B.S.6
  • 19
    • 0038311694 scopus 로고    scopus 로고
    • Mammalian transcription factor LSF is a target of ERK signaling
    • doi: 10.1002/jcb.10549
    • Pagon Z, Volker J, Cooper GM, Hansen U (2003) Mammalian transcription factor LSF is a target of ERK signaling. J Cell Biochem 89:733-746. doi: 10.1002/jcb.10549
    • (2003) J Cell Biochem , vol.89 , pp. 733-746
    • Pagon, Z.1    Volker, J.2    Cooper, G.M.3    Hansen, U.4
  • 20
    • 34249738746 scopus 로고    scopus 로고
    • Polycomb group protein RING1B is a direct substrate of Caspases-3 and -9
    • doi: 10.1016/j.bbamcr.2007.02.005
    • Wong CK, Chen Z, So KL, Li D, Li P (2007) Polycomb group protein RING1B is a direct substrate of Caspases-3 and -9. Biochim Biophys Acta 1773:844-852. doi: 10.1016/j.bbamcr.2007.02.005
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 844-852
    • Wong, C.K.1    Chen, Z.2    So, K.L.3    Li, D.4    Li, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.