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Volumn 114, Issue 1, 2003, Pages 99-111

The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor

(23)  Gozani, Or a   Karuman, Philip a   Jones, David R c   Ivanov, Dmitri a   Cha, James a   Lugovskoy, Alexey A a   Baird, Cheryl L b   Zhu, Hong a   Field, Seth J d   Lessnick, Stephen L e   Villasenor, Jennifer a   Mehrotra, Bharat b   Chen, Jian b   Rao, Vikram R a   Brugge, Joan S a   Ferguson, Colin G b,f   Payrastre, Bernard g   Myszka, David G b   Cantley, Lewis C a,d   Wagner, Gerhard a   more..


Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; HOMEODOMAIN PROTEIN; INOSITOL DERIVATIVE; PHOSPHATIDYLINOSITIDE RECEPTOR; PHOSPHATIDYLINOSITOL 5 PHOSPHATE; TUMOR SUPPRESSOR PROTEIN; TUMOR SUPPRESSOR PROTEIN ING2; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 0038784526     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00480-X     Document Type: Article
Times cited : (436)

References (56)
  • 1
    • 0028861418 scopus 로고
    • The PHD finger: Implications for chromatin-mediated transcriptional regulation
    • Aasland R., Gibson T.J., Stewart A.F. The PHD finger. implications for chromatin-mediated transcriptional regulation Trends Biochem. Sci. 20:1995;56-59.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 56-59
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 2
    • 0037972167 scopus 로고    scopus 로고
    • Scores of RINGS but no PHDs in ubiquitin signaling
    • Aravind L., Iyer L.M., Koonin E.V. Scores of RINGS but no PHDs in ubiquitin signaling. Cell Cycle. 2:2003;123-126.
    • (2003) Cell Cycle , vol.2 , pp. 123-126
    • Aravind, L.1    Iyer, L.M.2    Koonin, E.V.3
  • 3
    • 0031771547 scopus 로고    scopus 로고
    • Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors
    • Boronenkov I.V., Loijens J.C., Umeda M., Anderson R.A. 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
  • 4
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp T.R., Bernards R., Agami R. A system for stable expression of short interfering RNAs in mammalian cells. Science. 296:2002;550-553.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 5
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science. 296:2002;1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 6
    • 0035863152 scopus 로고    scopus 로고
    • Solution structure of the PHD domain from the KAP-1 corepressor: Structural determinants for PHD, RING and LIM zinc-binding domains
    • Capili A.D., Schultz D.C., Rauscher I.F., Borden K.L. Solution structure of the PHD domain from the KAP-1 corepressor. structural determinants for PHD, RING and LIM zinc-binding domains EMBO J. 20:2001;165-177.
    • (2001) EMBO J. , vol.20 , pp. 165-177
    • Capili, A.D.1    Schultz, D.C.2    Rauscher, I.F.3    Borden, K.L.4
  • 8
    • 0035425190 scopus 로고    scopus 로고
    • Inositol lipids are regulated during cell cycle progression in the nuclei of murine erythroleukaemia cells
    • Clarke J.H., Letcher A.J., D'Santos C.S., Halstead J.R., Irvine R.F., Divecha N. Inositol lipids are regulated during cell cycle progression in the nuclei of murine erythroleukaemia cells. Biochem. J. 357:2001;905-910.
    • (2001) Biochem. J. , vol.357 , pp. 905-910
    • Clarke, J.H.1    Letcher, A.J.2    D'Santos, C.S.3    Halstead, J.R.4    Irvine, R.F.5    Divecha, N.6
  • 9
    • 0037213013 scopus 로고    scopus 로고
    • PHD domains and E3 ubiquitin ligases: Viruses make the connection
    • Coscoy L., Ganem D. PHD domains and E3 ubiquitin ligases. viruses make the connection Trends Cell Biol. 13:2003;7-12.
    • (2003) Trends Cell Biol. , vol.13 , pp. 7-12
    • Coscoy, L.1    Ganem, D.2
  • 11
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P., Alessi D.R. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem. J. 351:2000;19-31.
    • (2000) Biochem. J. , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5    Downes, C.P.6    Alessi, D.R.7
  • 14
    • 0036850549 scopus 로고    scopus 로고
    • Different HATS of the ING1 gene family
    • Feng X., Hara Y., Riabowol K. Different HATS of the ING1 gene family. Trends Cell Biol. 12:2002;532-538.
    • (2002) Trends Cell Biol. , vol.12 , pp. 532-538
    • Feng, X.1    Hara, Y.2    Riabowol, K.3
  • 15
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke T.F., Kaplan D.R., Cantley L.C., Toker A. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science. 275:1997;665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 16
    • 0036723627 scopus 로고    scopus 로고
    • Binding of Acf1 to DNA involves a WAC motif and is important for ACF-mediated chromatin assembly
    • Fyodorov D.V., Kadonaga J.T. Binding of Acf1 to DNA involves a WAC motif and is important for ACF-mediated chromatin assembly. Mol. Cell. Biol. 22:2002;6344-6353.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6344-6353
    • Fyodorov, D.V.1    Kadonaga, J.T.2
  • 18
    • 0034637460 scopus 로고    scopus 로고
    • Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes. Role of conserved residues
    • Gaullier J.M., Ronning E., Gillooly D.J., Stenmark H. Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes. Role of conserved residues. J. Biol. Chem. 275:2000;24595-24600.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24595-24600
    • Gaullier, J.M.1    Ronning, E.2    Gillooly, D.J.3    Stenmark, H.4
  • 20
    • 0037090684 scopus 로고    scopus 로고
    • Specific interaction of IP6 with human Ku70/80, the DNA-binding subunit of DNA-PK
    • Hanakahi L.A., West S.C. Specific interaction of IP6 with human Ku70/80, the DNA-binding subunit of DNA-PK. EMBO J. 21:2002;2038-2044.
    • (2002) EMBO J. , vol.21 , pp. 2038-2044
    • Hanakahi, L.A.1    West, S.C.2
  • 21
    • 0033887478 scopus 로고    scopus 로고
    • Signaling and subcellular targeting by membrane-binding domains
    • Hurley J.H., Misra S. Signaling and subcellular targeting by membrane-binding domains. Annu. Rev. Biophys. Biomol. Struct. 29:2000;49-79.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 49-79
    • Hurley, J.H.1    Misra, S.2
  • 23
    • 0029993517 scopus 로고    scopus 로고
    • Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation
    • James S.R., Downes C.P., Gigg R., Grove S.J., Holmes A.B., Alessi D.R. Specific binding of the Akt-1 protein kinase to phosphatidylinositol 3,4,5-trisphosphate without subsequent activation. Biochem. J. 315:1996;709-713.
    • (1996) Biochem. J. , vol.315 , pp. 709-713
    • James, S.R.1    Downes, C.P.2    Gigg, R.3    Grove, S.J.4    Holmes, A.B.5    Alessi, D.R.6
  • 26
    • 0035793903 scopus 로고    scopus 로고
    • Structural mechanism of endosome docking by the FYVE domain
    • Kutateladze T., Overduin M. Structural mechanism of endosome docking by the FYVE domain. Science. 291:2001;1793-1796.
    • (2001) Science , vol.291 , pp. 1793-1796
    • Kutateladze, T.1    Overduin, M.2
  • 27
    • 0036143859 scopus 로고    scopus 로고
    • Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)
    • Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D. Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1). Mol. Cell. Biol. 22:2002;835-848.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 835-848
    • Kuzmichev, A.1    Zhang, Y.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 28
    • 0031788832 scopus 로고    scopus 로고
    • A genetic study of signaling processes for repression of PHO5 transcription in Saccharomyces cerevisiae
    • Lau W.W., Schneider K.R., O'Shea E.K. A genetic study of signaling processes for repression of PHO5 transcription in Saccharomyces cerevisiae. Genetics. 150:1998;1349-1359.
    • (1998) Genetics , vol.150 , pp. 1349-1359
    • Lau, W.W.1    Schneider, K.R.2    O'Shea, E.K.3
  • 29
    • 0036279167 scopus 로고    scopus 로고
    • The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2
    • Lu Z., Xu S., Joazeiro C., Cobb M.H., Hunter T. The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2. Mol. Cell. 9:2002;945-956.
    • (2002) Mol. Cell , vol.9 , pp. 945-956
    • Lu, Z.1    Xu, S.2    Joazeiro, C.3    Cobb, M.H.4    Hunter, T.5
  • 30
    • 0037192767 scopus 로고    scopus 로고
    • Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs
    • Ma Y., Lieber M.R. Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs. J. Biol. Chem. 277:2002;10756-10759.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10756-10759
    • Ma, Y.1    Lieber, M.R.2
  • 31
    • 0033756308 scopus 로고    scopus 로고
    • Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: Assembly of prereplication complexes in late mitosis
    • Mendez J., Stillman B. Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle. assembly of prereplication complexes in late mitosis Mol. Cell. Biol. 20:2000;8602-8612.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8602-8612
    • Mendez, J.1    Stillman, B.2
  • 32
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • Mirzoeva O.K., Petrini J.H. DNA damage-dependent nuclear dynamics of the Mre11 complex. Mol. Cell. Biol. 21:2001;281-288.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 33
    • 0035977098 scopus 로고    scopus 로고
    • Recognizing phosphatidylinositol 3-phosphate
    • Misra S., Miller G.J., Hurley J.H. Recognizing phosphatidylinositol 3-phosphate. Cell. 107:2001;559-562.
    • (2001) Cell , vol.107 , pp. 559-562
    • Misra, S.1    Miller, G.J.2    Hurley, J.H.3
  • 34
    • 0034625489 scopus 로고    scopus 로고
    • Thrombin stimulation of platelets causes an increase in phosphatidylinositol 5-phosphate revealed by mass assay
    • Morris J.B., Hinchliffe K.A., Ciruela A., Letcher A.J., Irvine R.F. Thrombin stimulation of platelets causes an increase in phosphatidylinositol 5-phosphate revealed by mass assay. FEBS Lett. 475:2000;57-60.
    • (2000) FEBS Lett. , vol.475 , pp. 57-60
    • Morris, J.B.1    Hinchliffe, K.A.2    Ciruela, A.3    Letcher, A.J.4    Irvine, R.F.5
  • 37
    • 0034743127 scopus 로고    scopus 로고
    • Nuclear PtdIns(4,5)P2 assembles in a mitotically regulated particle involved in pre-mRNA splicing
    • Osborne S.L., Thomas C.L., Gschmeissner S., Schiavo G. Nuclear PtdIns(4,5)P2 assembles in a mitotically regulated particle involved in pre-mRNA splicing. J. Cell Sci. 114:2001;2501-2511.
    • (2001) J. Cell Sci. , vol.114 , pp. 2501-2511
    • Osborne, S.L.1    Thomas, C.L.2    Gschmeissner, S.3    Schiavo, G.4
  • 38
    • 0034671463 scopus 로고    scopus 로고
    • Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor
    • Pascual J., Martinez-Yamout M., Dyson H.J., Wright P.E. Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor. J. Mol. Biol. 304:2000;723-729.
    • (2000) J. Mol. Biol. , vol.304 , pp. 723-729
    • Pascual, J.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 40
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh L.E., Tolias K.F., Duckworth B.C., Cantley L.C. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature. 390:1997;192-196.
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 43
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 45
    • 0037452874 scopus 로고    scopus 로고
    • Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases
    • Schaletzky J., Dove S.K., Short B., Lorenzo O., Clague M.J., Barr F.A. Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases. Curr. Biol. 13:2003;504-509.
    • (2003) Curr. Biol. , vol.13 , pp. 504-509
    • Schaletzky, J.1    Dove, S.K.2    Short, B.3    Lorenzo, O.4    Clague, M.J.5    Barr, F.A.6
  • 46
    • 0037414839 scopus 로고    scopus 로고
    • Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates
    • Shen X., Xiao H., Ranallo R., Wu W.H., Wu C. Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates. Science. 299:2003;112-114.
    • (2003) Science , vol.299 , pp. 112-114
    • Shen, X.1    Xiao, H.2    Ranallo, R.3    Wu, W.H.4    Wu, C.5
  • 47
    • 0032454301 scopus 로고    scopus 로고
    • Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor
    • Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M. Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor suppressor. Cytogenet. Cell Genet. 83:1998;232-235.
    • (1998) Cytogenet. Cell Genet. , vol.83 , pp. 232-235
    • Shimada, Y.1    Saito, A.2    Suzuki, M.3    Takahashi, E.4    Horie, M.5
  • 49
    • 0037138361 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate-binding FYVE finger
    • Stenmark H., Aasland R., Driscoll P.C. The phosphatidylinositol 3-phosphate-binding FYVE finger. FEBS Lett. 513:2002;77-84.
    • (2002) FEBS Lett. , vol.513 , pp. 77-84
    • Stenmark, H.1    Aasland, R.2    Driscoll, P.C.3
  • 51
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B., Alessi D.R. The PI3K-PDK1 connection. more than just a road to PKB Biochem. J. 346:2000;561-576.
    • (2000) Biochem. J. , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 52
    • 0036566427 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1
    • Watt S.A., Kular G., Fleming I.N., Downes C.P., Lucocq J.M. Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1. Biochem. J. 363:2002;657-666.
    • (2002) Biochem. J. , vol.363 , pp. 657-666
    • Watt, S.A.1    Kular, G.2    Fleming, I.N.3    Downes, C.P.4    Lucocq, J.M.5
  • 53
    • 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)
    • Yokogawa T., Nagata S., Nishio Y., Tsutsumi T., Ihara S., Shirai R., Morita K., Umeda M., Shirai Y., Saitoh N., Fukui Y. 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
  • 56
    • 0032567080 scopus 로고    scopus 로고
    • Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling
    • Zhao K., Wang W., Rando O.J., Xue Y., Swiderek K., Kuo A., Crabtree G.R. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell. 95:1998;625-636.
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1    Wang, W.2    Rando, O.J.3    Xue, Y.4    Swiderek, K.5    Kuo, A.6    Crabtree, G.R.7


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