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Volumn 287, Issue 2, 2003, Pages 301-313

Forced expression of RNF36 induces cell apoptosis

Author keywords

Apoptosis; Caspases; PML; RING zinc finger protein

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; CASPASE 2; DNA FRAGMENT; ONCOPROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN; PROTEIN BAX; PROTEIN INHIBITOR; RING FINGER PROTEIN 36; SYNAPTOPHYSIN; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN; BAX PROTEIN, HUMAN; CASPASE; DNA BINDING PROTEIN; ENZYME INHIBITOR; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; IMIDAZOLE DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOTOPROTEIN; PROTEIN BCL 2; PYRIDINE DERIVATIVE; RNF36 PROTEIN, MOUSE; TUMOR PROTEIN;

EID: 0041703139     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00110-1     Document Type: Article
Times cited : (17)

References (58)
  • 1
    • 0034830955 scopus 로고    scopus 로고
    • A novel member of the RBCC family, Trif, expressed specifically in the spermatids of mouse testis
    • Shyu H.W., Hsu S.H., Hsieh-Li H.M., Li H. A novel member of the RBCC family, Trif, expressed specifically in the spermatids of mouse testis. Mech. Dev. 108:2001;213-216.
    • (2001) Mech. Dev. , vol.108 , pp. 213-216
    • Shyu, H.W.1    Hsu, S.H.2    Hsieh-Li, H.M.3    Li, H.4
  • 3
    • 0030751654 scopus 로고    scopus 로고
    • Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution
    • Cao T., Borden K.L., Freemont P.S., Etkin L.D. Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution. J. Cell Sci. 110:(Pt 14):1997;1563-1571.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 14 , pp. 1563-1571
    • Cao, T.1    Borden, K.L.2    Freemont, P.S.3    Etkin, L.D.4
  • 4
    • 0034602928 scopus 로고    scopus 로고
    • RING domains: Master builders of molecular scaffolds?
    • Borden K.L. RING domains master builders of molecular scaffolds? J. Mol. Biol. 295:2000;1103-1112.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1103-1112
    • Borden, K.L.1
  • 5
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont P.S. RING for destruction? Curr. Biol. 10:2000;R84-R87.
    • (2000) Curr. Biol. , vol.10
    • Freemont, P.S.1
  • 6
    • 0029977716 scopus 로고    scopus 로고
    • The RING finger domain: A recent example of a sequence-structure family
    • Borden K.L., Freemont P.S. The RING finger domain a recent example of a sequence-structure family. Curr. Opin. Struct. Biol. 6:1996;395-401.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 395-401
    • Borden, K.L.1    Freemont, P.S.2
  • 7
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors
    • Le Douarin B., Nielsen A.L., Garnier J.M., Ichinose H., Jeanmougin F., Losson R., Chambon P. A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. EMBO J. 15:1996;6701-6715.
    • (1996) EMBO J. , vol.15 , pp. 6701-6715
    • Le Douarin, B.1    Nielsen, A.L.2    Garnier, J.M.3    Ichinose, H.4    Jeanmougin, F.5    Losson, R.6    Chambon, P.7
  • 8
    • 0028095410 scopus 로고
    • PML, a growth suppressor disrupted in acute promyelocytic leukemia
    • Mu Z.M., Chin K.V., Liu J.H., Lozano G., Chang K.S. PML, a growth suppressor disrupted in acute promyelocytic leukemia. Mol. Cell. Biol. 14:1994;6858-6867.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6858-6867
    • Mu, Z.M.1    Chin, K.V.2    Liu, J.H.3    Lozano, G.4    Chang, K.S.5
  • 9
    • 0029053743 scopus 로고
    • PML suppresses oncogenic transformation of NIH/3T3 cells by activated neu
    • Liu J.H., Mu Z.M., Chang K.S. PML suppresses oncogenic transformation of NIH/3T3 cells by activated neu. J. Exp. Med. 181:1995;1965-1973.
    • (1995) J. Exp. Med. , vol.181 , pp. 1965-1973
    • Liu, J.H.1    Mu, Z.M.2    Chang, K.S.3
  • 10
    • 0032499256 scopus 로고    scopus 로고
    • Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis
    • Le X.F., Vallian S., Mu Z.M., Hung M.C., Chang K.S. Recombinant PML adenovirus suppresses growth and tumorigenicity of human breast cancer cells by inducing G1 cell cycle arrest and apoptosis. Oncogene. 16:1998;1839-1849.
    • (1998) Oncogene , vol.16 , pp. 1839-1849
    • Le, X.F.1    Vallian, S.2    Mu, Z.M.3    Hung, M.C.4    Chang, K.S.5
  • 12
    • 0033053037 scopus 로고    scopus 로고
    • Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling
    • Doucas V., Tini M., Egan D.A., Evans R.M. Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. Proc. Natl. Acad. Sci. USA. 96:1999;2627-2632.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2627-2632
    • Doucas, V.1    Tini, M.2    Egan, D.A.3    Evans, R.M.4
  • 13
    • 0035099686 scopus 로고    scopus 로고
    • The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases
    • Wu W.S., Vallian S., Seto E., Yang W.M., Edmondson D., Roth S., Chang K.S. The growth suppressor PML represses transcription by functionally and physically interacting with histone deacetylases. Mol. Cell. Biol. 21:2001;2259-2268.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2259-2268
    • Wu, W.S.1    Vallian, S.2    Seto, E.3    Yang, W.M.4    Edmondson, D.5    Roth, S.6    Chang, K.S.7
  • 14
    • 0032574737 scopus 로고    scopus 로고
    • Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte V.J., Dyck J.A., Ochs R.L., Evans R.M. Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc. Natl. Acad. Sci. USA. 95:1998;4991-4996.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4991-4996
    • LaMorte, V.J.1    Dyck, J.A.2    Ochs, R.L.3    Evans, R.M.4
  • 15
    • 0033055056 scopus 로고    scopus 로고
    • Human T-cell leukemia retrovirus-Tax protein is a repressor of nuclear receptor signaling
    • Doucas V., Evans R.M. Human T-cell leukemia retrovirus-Tax protein is a repressor of nuclear receptor signaling. Proc. Natl. Acad. Sci. USA. 96:1999;2633-2638.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2633-2638
    • Doucas, V.1    Evans, R.M.2
  • 17
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • Boisvert F.M., Kruhlak M.J., Box A.K., Hendzel M.J., Bazett-Jones D.P. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J. Cell Biol. 152:2001;1099-1106.
    • (2001) J. Cell Biol. , vol.152 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3    Hendzel, M.J.4    Bazett-Jones, D.P.5
  • 18
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert F.M., Hendzel M.J., Bazett-Jones D.P. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J. Cell Biol. 148:2000;283-292.
    • (2000) J. Cell Biol. , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 19
    • 0032482440 scopus 로고    scopus 로고
    • Modulation of Fos-mediated AP-1 transcription by the promyelocytic leukemia protein
    • Vallian S., Gaken J.A., Gingold E.B., Kouzarides T., Chang K.S., Farzaneh F. Modulation of Fos-mediated AP-1 transcription by the promyelocytic leukemia protein. Oncogene. 16:1998;2843-2853.
    • (1998) Oncogene , vol.16 , pp. 2843-2853
    • Vallian, S.1    Gaken, J.A.2    Gingold, E.B.3    Kouzarides, T.4    Chang, K.S.5    Farzaneh, F.6
  • 22
    • 0033842166 scopus 로고    scopus 로고
    • Potentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein (PML) and the t(15;17)-generated PML-retinoic acid receptor alpha oncoprotein
    • Tsuzuki S., Towatari M., Saito H., Enver T. Potentiation of GATA-2 activity through interactions with the promyelocytic leukemia protein (PML) and the t(15;17)-generated PML-retinoic acid receptor alpha oncoprotein. Mol. Cell. Biol. 20:2000;6276-6286.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6276-6286
    • Tsuzuki, S.1    Towatari, M.2    Saito, H.3    Enver, T.4
  • 24
    • 0031755628 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter
    • Vallian S., Chin K.V., Chang K.S. The promyelocytic leukemia protein interacts with Sp1 and inhibits its transactivation of the epidermal growth factor receptor promoter. Mol. Cell. Biol. 18:1998;7147-7156.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7147-7156
    • Vallian, S.1    Chin, K.V.2    Chang, K.S.3
  • 25
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.J., Chen J.D. Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 20:2000;1784-1796.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5    Park, E.J.6    Chen, J.D.7
  • 28
    • 0026504147 scopus 로고
    • Social controls on cell survival and cell death
    • Raff M.C. Social controls on cell survival and cell death. Nature. 356:1992;397-400.
    • (1992) Nature , vol.356 , pp. 397-400
    • Raff, M.C.1
  • 29
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
    • Vaux D.L., Cory S., Adams J.M. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature. 335:1988;440-442.
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 30
    • 0031911258 scopus 로고    scopus 로고
    • Experimental cryptorchidism induces testicular germ cell apoptosis by p53-dependent and -independent pathways in mice
    • Yin Y., DeWolf W.C., Morgentaler A. Experimental cryptorchidism induces testicular germ cell apoptosis by p53-dependent and -independent pathways in mice. Biol. Reprod. 58:1998;492-496.
    • (1998) Biol. Reprod. , vol.58 , pp. 492-496
    • Yin, Y.1    DeWolf, W.C.2    Morgentaler, A.3
  • 32
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell. 80:1995;285-291.
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 34
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai Z.N., Milliman C.L., Korsmeyer S.J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 74:1993;609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 35
    • 0025331929 scopus 로고
    • The effect of submandibular gland removal on testicular and epididymal parameters
    • Russell L.D., Weiss T., Goh J.C., Curl J.L. The effect of submandibular gland removal on testicular and epididymal parameters. Tissue Cell. 22:1990;263-268.
    • (1990) Tissue Cell , vol.22 , pp. 263-268
    • Russell, L.D.1    Weiss, T.2    Goh, J.C.3    Curl, J.L.4
  • 38
    • 0029081428 scopus 로고
    • Efficacy of tetracycline-controlled gene expression is influenced by cell type: Commentary
    • discussion 216-217
    • Gossen M., Bujard H. Efficacy of tetracycline-controlled gene expression is influenced by cell type commentary. Biotechniques. 19:1995;213-216 discussion 216-217.
    • (1995) Biotechniques , vol.19 , pp. 213-216
    • Gossen, M.1    Bujard, H.2
  • 39
    • 0037205441 scopus 로고    scopus 로고
    • Phosphorylation-dependent cellular localization and thermoprotective role of heat shock protein 25 in hippocampal progenitor cells
    • Geum D., Son G.H., Kim K. Phosphorylation-dependent cellular localization and thermoprotective role of heat shock protein 25 in hippocampal progenitor cells. J. Biol. Chem. 277:2002;19913-19921.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19913-19921
    • Geum, D.1    Son, G.H.2    Kim, K.3
  • 41
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong S., Salomoni P., Pandolfi P.P. The transcriptional role of PML and the nuclear body. Nat. Cell Biol. 2:2000;E85-E90.
    • (2000) Nat. Cell Biol. , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 44
    • 0031418659 scopus 로고    scopus 로고
    • Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells
    • Mu Z.M., Le X.F., Vallian S., Glassman A.B., Chang K.S. Stable overexpression of PML alters regulation of cell cycle progression in HeLa cells. Carcinogenesis. 18:1997;2063-2069.
    • (1997) Carcinogenesis , vol.18 , pp. 2063-2069
    • Mu, Z.M.1    Le, X.F.2    Vallian, S.3    Glassman, A.B.4    Chang, K.S.5
  • 46
    • 0034671525 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein-3 modulates expression of Bax and Bcl-2 and potentiates p53-independent radiation-induced apoptosis in human breast cancer cells
    • Butt A.J., Firth S.M., King M.A., Baxter R.C. Insulin-like growth factor-binding protein-3 modulates expression of Bax and Bcl-2 and potentiates p53-independent radiation-induced apoptosis in human breast cancer cells. J. Biol. Chem. 275:2000;39174-39181.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39174-39181
    • Butt, A.J.1    Firth, S.M.2    King, M.A.3    Baxter, R.C.4
  • 47
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T., Reed J.C. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell. 80:1995;293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 48
    • 0028072523 scopus 로고
    • DNA damage can induce apoptosis in proliferating lymphoid cells via p53-independent mechanisms inhibitable by Bcl-2
    • Strasser A., Harris A.W., Jacks T., Cory S. DNA damage can induce apoptosis in proliferating lymphoid cells via p53-independent mechanisms inhibitable by Bcl-2. Cell. 79:1994;329-339.
    • (1994) Cell , vol.79 , pp. 329-339
    • Strasser, A.1    Harris, A.W.2    Jacks, T.3    Cory, S.4
  • 49
    • 0030956061 scopus 로고    scopus 로고
    • Evidence that expression of a mutated p53 gene attenuates apoptotic cell deat in human gastric intestinal-type carcinomas in vivo
    • Ishida M., Gomyo Y., Ohfuji S., Ikeda M., Kawasaki H., Ito H. Evidence that expression of a mutated p53 gene attenuates apoptotic cell deat in human gastric intestinal-type carcinomas in vivo. Jpn. J. Cancer Res. 88:1997;468-475.
    • (1997) Jpn. J. Cancer Res. , vol.88 , pp. 468-475
    • Ishida, M.1    Gomyo, Y.2    Ohfuji, S.3    Ikeda, M.4    Kawasaki, H.5    Ito, H.6
  • 50
    • 0033786442 scopus 로고    scopus 로고
    • Apoptosis: Overview and signal transduction pathways
    • Bredesen D.E. Apoptosis overview and signal transduction pathways. J Neurotrauma. 17:2000;801-810.
    • (2000) J Neurotrauma , vol.17 , pp. 801-810
    • Bredesen, D.E.1
  • 51
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H., Dixit V.M. RAIDD is a new 'death' adaptor molecule. Nature. 385:1997;86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 52
    • 0029760732 scopus 로고    scopus 로고
    • RIP and FADD: Two "death domain" -containing proteins can induce apoptosis by convergent, but dissociable, pathways
    • Grimm S., Stanger B.Z., Leder P. RIP and FADD two "death domain" -containing proteins can induce apoptosis by convergent, but dissociable, pathways. Proc. Natl. Acad. Sci. USA. 93:1996;10923-10937.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10923-10937
    • Grimm, S.1    Stanger, B.Z.2    Leder, P.3
  • 53
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu H., Huang J., Shu H.B., Baichwal V., Goeddel D.V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity. 4:1996;387-396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 54
    • 0026709129 scopus 로고
    • Spermatogonial apoptosis has three morphologically recognizable phases and shows no circadian rhythm during normal spermatogenesis in the rat
    • Allan D.J., Harmon B.V., Roberts S.A. Spermatogonial apoptosis has three morphologically recognizable phases and shows no circadian rhythm during normal spermatogenesis in the rat. Cell Proliferation. 25:1992;241-250.
    • (1992) Cell Proliferation , vol.25 , pp. 241-250
    • Allan, D.J.1    Harmon, B.V.2    Roberts, S.A.3
  • 55
    • 0028291686 scopus 로고
    • Temporal relationship between androgen-dependent changes in the volume of seminiferous tubule fluid, lumen size and seminiferous tubule protein secretion in rats
    • Sharpe R.M., Kerr J.B., McKinnell C., Millar M. Temporal relationship between androgen-dependent changes in the volume of seminiferous tubule fluid, lumen size and seminiferous tubule protein secretion in rats. J. Reprod. Fertil. 101:1994;193-198.
    • (1994) J. Reprod. Fertil. , vol.101 , pp. 193-198
    • Sharpe, R.M.1    Kerr, J.B.2    McKinnell, C.3    Millar, M.4
  • 56
    • 0035205090 scopus 로고    scopus 로고
    • Apoptosis during spermatogenesis: The thrill of being alive
    • Kierszenbaum A.L. Apoptosis during spermatogenesis the thrill of being alive. Mol. Reprod. Dev. 58:2001;1-3.
    • (2001) Mol. Reprod. Dev. , vol.58 , pp. 1-3
    • Kierszenbaum, A.L.1
  • 57
    • 0034713745 scopus 로고    scopus 로고
    • Involvement of Bcl-2 family proteins in germ cell apoptosis during testicular development in the rat and pro-survival effect of stem cell factor on germ cells in vitro
    • Yan W., Suominen J., Samson M., Jegou B., Toppari J. Involvement of Bcl-2 family proteins in germ cell apoptosis during testicular development in the rat and pro-survival effect of stem cell factor on germ cells in vitro. Mol. Cell. Endocrinol. 165:2000;115-129.
    • (2000) Mol. Cell. Endocrinol. , vol.165 , pp. 115-129
    • Yan, W.1    Suominen, J.2    Samson, M.3    Jegou, B.4    Toppari, J.5
  • 58
    • 0035009899 scopus 로고    scopus 로고
    • Expression of Bcl-2 family proteins and spontaneous apoptosis in normal human testis
    • Oldereid N.B., Angelis P.D., Wiger R., Clausen O.P. Expression of Bcl-2 family proteins and spontaneous apoptosis in normal human testis. Mol. Hum. Reprod. 7:2001;403-408.
    • (2001) Mol. Hum. Reprod. , vol.7 , pp. 403-408
    • Oldereid, N.B.1    Angelis, P.D.2    Wiger, R.3    Clausen, O.P.4


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