메뉴 건너뛰기




Volumn 18, Issue 4, 2005, Pages 435-445

Nucleophosmin/B23, a nuclear PI(3,4,5)P3 receptor, mediates the antiapoptotic actions of NGF by inhibiting CAD

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CASPASE ACTIVATED DEOXYRIBONUCLEASE; DNA FRAGMENT; ENZYME; MUTANT PROTEIN; NERVE GROWTH FACTOR; NUCLEOPHOSMIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 18944395803     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.04.010     Document Type: Article
Times cited : (110)

References (43)
  • 1
    • 0027242129 scopus 로고
    • The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential
    • N.N. Ahmed, T.F. Franke, A. Bellacosa, K. Datta, M.E. Gonzalez-Portal, T. Taguchi, J.R. Testa, and P.N. Tsichlis The proteins encoded by c-akt and v-akt differ in post-translational modification, subcellular localization and oncogenic potential Oncogene 8 1993 1957 1963
    • (1993) Oncogene , vol.8 , pp. 1957-1963
    • Ahmed, N.N.1    Franke, T.F.2    Bellacosa, A.3    Datta, K.4    Gonzalez-Portal, M.E.5    Taguchi, T.6    Testa, J.R.7    Tsichlis, P.N.8
  • 2
    • 8144228424 scopus 로고    scopus 로고
    • PIKE/nuclear PI 3-kinase signaling mediates the antiapoptotic actions of NGF in the nucleus
    • J.Y. Ahn, R. Rong, X. Liu, and K. Ye PIKE/nuclear PI 3-kinase signaling mediates the antiapoptotic actions of NGF in the nucleus EMBO J. 23 2004 3995 4006
    • (2004) EMBO J. , vol.23 , pp. 3995-4006
    • Ahn, J.Y.1    Rong, R.2    Liu, X.3    Ye, K.4
  • 5
    • 0033042802 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase translocation to the nucleus is induced by interleukin 1 and prevented by mutation of interleukin 1 receptor in human osteosarcoma Saos-2 cells
    • A. Bavelloni, S. Santi, A. Sirri, M. Riccio, I. Faenza, N. Zini, S. Cecchi, A. Ferri, P. Auron, N.M. Maraldi, and S. Marmiroli Phosphatidylinositol 3-kinase translocation to the nucleus is induced by interleukin 1 and prevented by mutation of interleukin 1 receptor in human osteosarcoma Saos-2 cells J. Cell Sci. 112 1999 631 640
    • (1999) J. Cell Sci. , vol.112 , pp. 631-640
    • Bavelloni, A.1    Santi, S.2    Sirri, A.3    Riccio, M.4    Faenza, I.5    Zini, N.6    Cecchi, S.7    Ferri, A.8    Auron, P.9    Maraldi, N.M.10    Marmiroli, S.11
  • 7
    • 1642499357 scopus 로고    scopus 로고
    • Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23
    • D. Bertwistle, M. Sugimoto, and C.J. Sherr Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23 Mol. Cell. Biol. 24 2004 985 996
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 985-996
    • Bertwistle, D.1    Sugimoto, M.2    Sherr, C.J.3
  • 8
    • 0031771547 scopus 로고    scopus 로고
    • Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors
    • I.V. Boronenkov, J.C. Loijens, M. Umeda, and R.A. Anderson Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors Mol. Biol. Cell 9 1998 3547 3560
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3547-3560
    • Boronenkov, I.V.1    Loijens, J.C.2    Umeda, M.3    Anderson, R.A.4
  • 9
    • 0035369623 scopus 로고    scopus 로고
    • Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway
    • A. Brunet, S.R. Datta, and M.E. Greenberg Transcription-dependent and -independent control of neuronal survival by the PI3K-Akt signaling pathway Curr. Opin. Neurobiol. 11 2001 297 305
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 297-305
    • Brunet, A.1    Datta, S.R.2    Greenberg, M.E.3
  • 10
    • 0032007890 scopus 로고    scopus 로고
    • Evidence for the ability of nucleophosmin/B23 to bind ATP
    • J.H. Chang, J.Y. Lin, M.H. Wu, and B.Y. Yung Evidence for the ability of nucleophosmin/B23 to bind ATP Biochem. J. 329 1998 539 544
    • (1998) Biochem. J. , vol.329 , pp. 539-544
    • Chang, J.H.1    Lin, J.Y.2    Wu, M.H.3    Yung, B.Y.4
  • 11
    • 0035160505 scopus 로고    scopus 로고
    • Increased stability of nucleophosmin/B23 in anti-apoptotic effect of ras during serum deprivation
    • C.C. Chou, and B.Y. Yung Increased stability of nucleophosmin/B23 in anti-apoptotic effect of ras during serum deprivation Mol. Pharmacol. 59 2001 38 45
    • (2001) Mol. Pharmacol. , vol.59 , pp. 38-45
    • Chou, C.C.1    Yung, B.Y.2
  • 13
    • 0032497839 scopus 로고    scopus 로고
    • Phospholipid signalling in the nucleus. Een DAG uit het leven van de inositide signalering in de nucleus
    • C.S. D'Santos, J.H. Clarke, and N. Divecha Phospholipid signalling in the nucleus. Een DAG uit het leven van de inositide signalering in de nucleus Biochim. Biophys. Acta 1436 1998 201 232
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 201-232
    • D'Santos, C.S.1    Clarke, J.H.2    Divecha, N.3
  • 14
    • 0141866729 scopus 로고    scopus 로고
    • SHIP-2 and PTEN are expressed and active in vascular smooth muscle cell nuclei, but only SHIP-2 is associated with nuclear speckles
    • P. Deleris, D. Bacqueville, S. Gayral, L. Carrez, J.P. Salles, B. Perret, and M. Breton-Douillon SHIP-2 and PTEN are expressed and active in vascular smooth muscle cell nuclei, but only SHIP-2 is associated with nuclear speckles J. Biol. Chem. 278 2003 38884 38891
    • (2003) J. Biol. Chem. , vol.278 , pp. 38884-38891
    • Deleris, P.1    Bacqueville, D.2    Gayral, S.3    Carrez, L.4    Salles, J.P.5    Perret, B.6    Breton-Douillon, M.7
  • 15
    • 0026352122 scopus 로고
    • Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: Dissociation by the Rev response element
    • C. Fankhauser, E. Izaurralde, Y. Adachi, P. Wingfield, and U.K. Laemmli Specific complex of human immunodeficiency virus type 1 rev and nucleolar B23 proteins: dissociation by the Rev response element Mol. Cell. Biol. 11 1991 2567 2575
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2567-2575
    • Fankhauser, C.1    Izaurralde, E.2    Adachi, Y.3    Wingfield, P.4    Laemmli, U.K.5
  • 17
    • 0029914227 scopus 로고    scopus 로고
    • Sedimentation analyses of the salt- and divalent metal ion-induced oligomerization of nucleolar protein B23
    • J.E. Herrera, J.J. Correia, A.E. Jones, and M.O. Olson Sedimentation analyses of the salt- and divalent metal ion-induced oligomerization of nucleolar protein B23 Biochemistry 35 1996 2668 2673
    • (1996) Biochemistry , vol.35 , pp. 2668-2673
    • Herrera, J.E.1    Correia, J.J.2    Jones, A.E.3    Olson, M.O.4
  • 18
    • 0034637578 scopus 로고    scopus 로고
    • Mapping the functional domains of nucleolar protein B23
    • K. Hingorani, A. Szebeni, and M.O. Olson Mapping the functional domains of nucleolar protein B23 J. Biol. Chem. 275 2000 24451 24457
    • (2000) J. Biol. Chem. , vol.275 , pp. 24451-24457
    • Hingorani, K.1    Szebeni, A.2    Olson, M.O.3
  • 19
    • 0033810002 scopus 로고    scopus 로고
    • Over-expression of nucleophosmin/B23 decreases the susceptibility of human leukemia HL-60 cells to retinoic acid-induced differentiation and apoptosis
    • C.Y. Hsu, and B.Y. Yung Over-expression of nucleophosmin/B23 decreases the susceptibility of human leukemia HL-60 cells to retinoic acid-induced differentiation and apoptosis Int. J. Cancer 88 2000 392 400
    • (2000) Int. J. Cancer , vol.88 , pp. 392-400
    • Hsu, C.Y.1    Yung, B.Y.2
  • 20
    • 0345276485 scopus 로고    scopus 로고
    • Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation
    • K. Itahana, K.P. Bhat, A. Jin, Y. Itahana, D. Hawke, R. Kobayashi, and Y. Zhang Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation Mol. Cell 12 2003 1151 1164
    • (2003) Mol. Cell , vol.12 , pp. 1151-1164
    • Itahana, K.1    Bhat, K.P.2    Jin, A.3    Itahana, Y.4    Hawke, D.5    Kobayashi, R.6    Zhang, Y.7
  • 21
    • 0034737658 scopus 로고    scopus 로고
    • Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site
    • J.L. Kam, K. Miura, T.R. Jackson, J. Gruschus, P. Roller, S. Stauffer, J. Clark, R. Aneja, and P.A. Randazzo Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site J. Biol. Chem. 275 2000 9653 9663
    • (2000) J. Biol. Chem. , vol.275 , pp. 9653-9663
    • Kam, J.L.1    Miura, K.2    Jackson, T.R.3    Gruschus, J.4    Roller, P.5    Stauffer, S.6    Clark, J.7    Aneja, R.8    Randazzo, P.A.9
  • 22
    • 0029962298 scopus 로고    scopus 로고
    • C23 interacts with B23, a putative nucleolar-localization-signal-binding protein
    • Y.P. Li, R.K. Busch, B.C. Valdez, and H. Busch C23 interacts with B23, a putative nucleolar-localization-signal-binding protein Eur. J. Biochem. 237 1996 153 158
    • (1996) Eur. J. Biochem. , vol.237 , pp. 153-158
    • Li, Y.P.1    Busch, R.K.2    Valdez, B.C.3    Busch, H.4
  • 23
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • X. Liu, H. Zou, C. Slaughter, and X. Wang DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis Cell 89 1997 175 184
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 24
    • 0032545349 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase in HL-60 nuclei is bound to the nuclear matrix and increases during granulocytic differentiation
    • M. Marchisio, V. Bertagnolo, M.L. Colamussi, S. Capitani, and L.M. Neri Phosphatidylinositol 3-kinase in HL-60 nuclei is bound to the nuclear matrix and increases during granulocytic differentiation Biochem. Biophys. Res. Commun. 253 1998 346 351
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 346-351
    • Marchisio, M.1    Bertagnolo, V.2    Colamussi, M.L.3    Capitani, S.4    Neri, L.M.5
  • 26
    • 0030727172 scopus 로고    scopus 로고
    • Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta
    • R. Meier, D.R. Alessi, P. Cron, M. Andjelkovic, and B.A. Hemmings Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta J. Biol. Chem. 272 1997 30491 30497
    • (1997) J. Biol. Chem. , vol.272 , pp. 30491-30497
    • Meier, R.1    Alessi, D.R.2    Cron, P.3    Andjelkovic, M.4    Hemmings, B.A.5
  • 27
    • 0034630317 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation
    • S. Nagata Apoptotic DNA fragmentation Exp. Cell Res. 256 2000 12 18
    • (2000) Exp. Cell Res. , vol.256 , pp. 12-18
    • Nagata, S.1
  • 28
    • 0345193700 scopus 로고
    • Nuclear translocation of phosphatidylinositol 3-kinase in rat pheochromocytoma PC 12 cells after treatment with nerve growth factor
    • L.M. Neri, D. Milani, L. Bertolaso, M. Stroscio, V. Bertagnolo, and S. Capitani Nuclear translocation of phosphatidylinositol 3-kinase in rat pheochromocytoma PC 12 cells after treatment with nerve growth factor Cell Mol. Biol. (Noisy-le-grand) 40 1994 619 626
    • (1994) Cell Mol. Biol. (Noisy-le-grand) , vol.40 , pp. 619-626
    • Neri, L.M.1    Milani, D.2    Bertolaso, L.3    Stroscio, M.4    Bertagnolo, V.5    Capitani, S.6
  • 29
    • 0032491522 scopus 로고    scopus 로고
    • Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-alpha
    • L.M. Neri, P. Borgatti, S. Capitani, and A.M. Martelli Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-alpha J. Biol. Chem. 273 1998 29738 29744
    • (1998) J. Biol. Chem. , vol.273 , pp. 29738-29744
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 30
    • 0025265082 scopus 로고
    • Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase
    • M. Peter, J. Nakagawa, M. Doree, J.C. Labbe, and E.A. Nigg Identification of major nucleolar proteins as candidate mitotic substrates of cdc2 kinase Cell 60 1990 791 801
    • (1990) Cell , vol.60 , pp. 791-801
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 31
    • 0023874702 scopus 로고
    • Casein kinase II accumulation in the nucleolus and its role in nucleolar phosphorylation
    • M. Pfaff, and F.A. Anderer Casein kinase II accumulation in the nucleolus and its role in nucleolar phosphorylation Biochim. Biophys. Acta 969 1988 100 109
    • (1988) Biochim. Biophys. Acta , vol.969 , pp. 100-109
    • Pfaff, M.1    Anderer, F.A.2
  • 32
    • 0023835505 scopus 로고
    • A high-efficiency HeLa cell nuclear transcription extract
    • D.J. Shapiro, P.A. Sharp, W.W. Wahli, and M.J. Keller A high-efficiency HeLa cell nuclear transcription extract DNA 7 1988 47 55
    • (1988) DNA , vol.7 , pp. 47-55
    • Shapiro, D.J.1    Sharp, P.A.2    Wahli, W.W.3    Keller, M.J.4
  • 33
    • 0345097326 scopus 로고    scopus 로고
    • SHIP, SHIP2, and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is up-regulated in macrophages and mast cells by lipopolysaccharide
    • L.M. Sly, M.J. Rauh, J. Kalesnikoff, T. Buchse, and G. Krystal SHIP, SHIP2, and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is up-regulated in macrophages and mast cells by lipopolysaccharide Exp. Hematol. 31 2003 1170 1181
    • (2003) Exp. Hematol. , vol.31 , pp. 1170-1181
    • Sly, L.M.1    Rauh, M.J.2    Kalesnikoff, J.3    Buchse, T.4    Krystal, G.5
  • 34
    • 0028122251 scopus 로고
    • Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23
    • B.C. Valdez, L. Perlaky, D. Henning, Y. Saijo, P.K. Chan, and H. Busch Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein B23 J. Biol. Chem. 269 1994 23776 23783
    • (1994) J. Biol. Chem. , vol.269 , pp. 23776-23783
    • Valdez, B.C.1    Perlaky, L.2    Henning, D.3    Saijo, Y.4    Chan, P.K.5    Busch, H.6
  • 35
    • 0028296553 scopus 로고
    • Synthesis of specific proteins in trophic factor-deprived neurons undergoing apoptosis
    • P. Villa, M. Miehe, M. Sensenbrenner, and B. Pettmann Synthesis of specific proteins in trophic factor-deprived neurons undergoing apoptosis J. Neurochem. 62 1994 1468 1475
    • (1994) J. Neurochem. , vol.62 , pp. 1468-1475
    • Villa, P.1    Miehe, M.2    Sensenbrenner, M.3    Pettmann, B.4
  • 36
    • 0028135012 scopus 로고
    • The nucleic acid binding activity of nucleolar protein B23.1 resides in its carboxyl-terminal end
    • D. Wang, A. Baumann, A. Szebeni, and M.O. Olson The nucleic acid binding activity of nucleolar protein B23.1 resides in its carboxyl-terminal end J. Biol. Chem. 269 1994 30994 30998
    • (1994) J. Biol. Chem. , vol.269 , pp. 30994-30998
    • Wang, D.1    Baumann, A.2    Szebeni, A.3    Olson, M.O.4
  • 37
    • 0038456399 scopus 로고    scopus 로고
    • PTEN signaling pathways in melanoma
    • H. Wu, V. Goel, and F.G. Haluska PTEN signaling pathways in melanoma Oncogene 22 2003 3113 3122
    • (2003) Oncogene , vol.22 , pp. 3113-3122
    • Wu, H.1    Goel, V.2    Haluska, F.G.3
  • 38
    • 0028897292 scopus 로고
    • Translocation of nucleophosmin from nucleoli to nucleoplasm requires ATP
    • M.H. Wu, C.Y. Lam, and B.Y. Yung Translocation of nucleophosmin from nucleoli to nucleoplasm requires ATP Biochem. J. 305 1995 987 992
    • (1995) Biochem. J. , vol.305 , pp. 987-992
    • Wu, M.H.1    Lam, C.Y.2    Yung, B.Y.3
  • 39
    • 0036198225 scopus 로고    scopus 로고
    • Resistance to UV-induced cell-killing in nucleophosmin/B23 over-expressed NIH 3T3 fibroblasts: Enhancement of DNA repair and up-regulation of PCNA in association with nucleophosmin/B23 over-expression
    • M.H. Wu, J.H. Chang, and B.Y. Yung Resistance to UV-induced cell-killing in nucleophosmin/B23 over-expressed NIH 3T3 fibroblasts: enhancement of DNA repair and up-regulation of PCNA in association with nucleophosmin/B23 over-expression Carcinogenesis 23 2002 93 100
    • (2002) Carcinogenesis , vol.23 , pp. 93-100
    • Wu, M.H.1    Chang, J.H.2    Yung, B.Y.3
  • 40
    • 0034921007 scopus 로고    scopus 로고
    • Tumor suppressor PTEN: Modulator of cell signaling, growth, migration and apoptosis
    • K.M. Yamada, and M. Araki Tumor suppressor PTEN: modulator of cell signaling, growth, migration and apoptosis J. Cell Sci. 114 2001 2375 2382
    • (2001) J. Cell Sci. , vol.114 , pp. 2375-2382
    • Yamada, K.M.1    Araki, M.2
  • 41
    • 0034640213 scopus 로고    scopus 로고
    • Evidence that 3′-phosphorylated polyphosphoinositides are generated at the nuclear surface: Use of immunostaining technique with monoclonal antibodies specific for PI 3,4-P(2)
    • T. Yokogawa, S. Nagata, Y. Nishio, T. Tsutsumi, S. Ihara, R. Shirai, K. Morita, M. Umeda, Y. Shirai, N. Saitoh, and Y. Fukui Evidence that 3′-phosphorylated polyphosphoinositides are generated at the nuclear surface: use of immunostaining technique with monoclonal antibodies specific for PI 3,4-P(2) FEBS Lett. 473 2000 222 226
    • (2000) FEBS Lett. , vol.473 , pp. 222-226
    • Yokogawa, T.1    Nagata, S.2    Nishio, Y.3    Tsutsumi, T.4    Ihara, S.5    Shirai, R.6    Morita, K.7    Umeda, M.8    Shirai, Y.9    Saitoh, N.10    Fukui, Y.11
  • 42
    • 0025114362 scopus 로고
    • Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells
    • B.Y. Yung, A.M. Bor, and P.K. Chan Short exposure to actinomycin D induces "reversible" translocation of protein B23 as well as "reversible" inhibition of cell growth and RNA synthesis in HeLa cells Cancer Res. 50 1990 5987 5991
    • (1990) Cancer Res. , vol.50 , pp. 5987-5991
    • Yung, B.Y.1    Bor, A.M.2    Chan, P.K.3
  • 43
    • 0029146757 scopus 로고
    • The intranuclear amount of phospholipase C beta 1 decreases following cell differentiation in Friend cells, whereas gamma 1 isoform is not affected
    • N. Zini, A. Ognibene, S. Marmiroli, A. Bavelloni, M.C. Maltarello, I. Faenza, A. Valmori, and N.M. Maraldi The intranuclear amount of phospholipase C beta 1 decreases following cell differentiation in Friend cells, whereas gamma 1 isoform is not affected Eur. J. Cell Biol. 68 1995 25 34
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 25-34
    • Zini, N.1    Ognibene, A.2    Marmiroli, S.3    Bavelloni, A.4    Maltarello, M.C.5    Faenza, I.6    Valmori, A.7    Maraldi, N.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.