메뉴 건너뛰기




Volumn 1761, Issue 5-6, 2006, Pages 560-569

Nuclear PI(4,5)P2: A new place for an old signal

Author keywords

Cell cycle; Chromatin remodeling; Diacylglycerol; Nuclear speckle; Phosphatidylinositol 4,5 bisphopshate; Phospholipase C

Indexed keywords

DIACYLGLYCEROL; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INOSITOL PHOSPHATE; LIPID; MESSENGER RNA; NERVE GROWTH FACTOR; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE KINASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C BETA1; PHOSPHOLIPASE C GAMMA; PROTEIN KINASE C;

EID: 33746938832     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.03.002     Document Type: Review
Times cited : (59)

References (85)
  • 1
    • 0042817834 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place
    • Doughman R.L., Firestone A.J., and Anderson R.A. Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place. J. Membr. Biol. 194 (2003) 77-89
    • (2003) J. Membr. Biol. , vol.194 , pp. 77-89
    • Doughman, R.L.1    Firestone, A.J.2    Anderson, R.A.3
  • 2
    • 31544482652 scopus 로고    scopus 로고
    • Nuclear phosphoinositide kinases and inositol phospholipids
    • Gonzales M.L., and Anderson R.A. Nuclear phosphoinositide kinases and inositol phospholipids. J. Cell. Biochem. (2005) 252-260
    • (2005) J. Cell. Biochem. , pp. 252-260
    • Gonzales, M.L.1    Anderson, R.A.2
  • 3
    • 0037125879 scopus 로고    scopus 로고
    • Nuclear lipid signaling
    • Irvine R.F. Nuclear lipid signaling. Sci. STKE 2002 (2002) RE13
    • (2002) Sci. STKE , vol.2002
    • Irvine, R.F.1
  • 6
    • 0033537926 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases, a multifaceted family of signaling enzymes
    • Anderson R.A., Boronenkov I.V., Doughman S.D., Kunz J., and Loijens J.C. Phosphatidylinositol phosphate kinases, a multifaceted family of signaling enzymes. J. Biol. Chem. 274 (1999) 9907-9910
    • (1999) J. Biol. Chem. , vol.274 , pp. 9907-9910
    • Anderson, R.A.1    Boronenkov, I.V.2    Doughman, S.D.3    Kunz, J.4    Loijens, J.C.5
  • 7
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh L.E., Tolias K.F., Duckworth B.C., and 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
  • 8
    • 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., and 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
  • 9
    • 0034654363 scopus 로고    scopus 로고
    • Nuclear targeting of the beta isoform of type II phosphatidylinositol phosphate kinase (phosphatidylinositol 5-phosphate 4-kinase) by its alpha-helix 7
    • Ciruela A., Hinchliffe K.A., Divecha N., and Irvine R.F. Nuclear targeting of the beta isoform of type II phosphatidylinositol phosphate kinase (phosphatidylinositol 5-phosphate 4-kinase) by its alpha-helix 7. Biochem. J. 3 (2000) 587-591
    • (2000) Biochem. J. , vol.3 , pp. 587-591
    • Ciruela, A.1    Hinchliffe, K.A.2    Divecha, N.3    Irvine, R.F.4
  • 10
    • 0026730882 scopus 로고
    • A differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix
    • Payrastre B., Nievers M., Boonstra J., Breton M., Verkleij A.J., and Van Bergen en Henegouwen P.M. A differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix. J. Biol. Chem. 267 (1992) 5078-5084
    • (1992) J. Biol. Chem. , vol.267 , pp. 5078-5084
    • Payrastre, B.1    Nievers, M.2    Boonstra, J.3    Breton, M.4    Verkleij, A.J.5    Van Bergen en Henegouwen, P.M.6
  • 11
    • 0032541172 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases synthesize the novel lipids phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 5-phosphate
    • Tolias K.F., Rameh L.E., Ishihara H., Shibasaki Y., Chen J., Prestwich G.D., Cantley L.C., and Carpenter C.L. Type I phosphatidylinositol-4-phosphate 5-kinases synthesize the novel lipids phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 5-phosphate. J. Biol. Chem. 273 (1998) 18040-18046
    • (1998) J. Biol. Chem. , vol.273 , pp. 18040-18046
    • Tolias, K.F.1    Rameh, L.E.2    Ishihara, H.3    Shibasaki, Y.4    Chen, J.5    Prestwich, G.D.6    Cantley, L.C.7    Carpenter, C.L.8
  • 13
    • 0030690395 scopus 로고    scopus 로고
    • Metabolism and possible compartmentalization of inositol lipids in isolated rat-liver nuclei
    • Vann L.R., Wooding F.B., Irvine R.F., and Divecha N. Metabolism and possible compartmentalization of inositol lipids in isolated rat-liver nuclei. Biochem. J. 327 Pt. 2 (1997) 569-576
    • (1997) Biochem. J. , vol.327 , Issue.PART 2 , pp. 569-576
    • Vann, L.R.1    Wooding, F.B.2    Irvine, R.F.3    Divecha, N.4
  • 16
    • 0032497839 scopus 로고    scopus 로고
    • Phospholipid signalling in the nucleus. Een DAG uit het leven van de inositide signalering in de nucleus
    • D'Santos C.S., Clarke J.H., and Divecha N. 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
  • 17
    • 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
    • Deleris P., Bacqueville D., Gayral S., Carrez L., Salles J.P., Perret B., and Breton-Douillon M. 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
  • 19
    • 0033600855 scopus 로고    scopus 로고
    • Agonists cause nuclear translocation of phosphatidylinositol 3-kinase gamma. A Gbetagamma-dependent pathway that requires the p110gamma amino terminus
    • Metjian A., Roll R.L., Ma A.D., and Abrams C.S. Agonists cause nuclear translocation of phosphatidylinositol 3-kinase gamma. A Gbetagamma-dependent pathway that requires the p110gamma amino terminus. J. Biol. Chem. 274 (1999) 27943-27947
    • (1999) J. Biol. Chem. , vol.274 , pp. 27943-27947
    • Metjian, A.1    Roll, R.L.2    Ma, A.D.3    Abrams, C.S.4
  • 21
    • 0023794607 scopus 로고
    • Rapid changes in phospholipid metabolism in the nuclei of Swiss 3T3 cells induced by treatment of the cells with insulin-like growth factor I
    • Cocco L., Martelli A.M., Gilmour R.S., Ognibene A., Manzoli F.A., and Irvine R.F. Rapid changes in phospholipid metabolism in the nuclei of Swiss 3T3 cells induced by treatment of the cells with insulin-like growth factor I. Biochem. Biophys. Res. Commun. 154 (1988) 1266-1272
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 1266-1272
    • Cocco, L.1    Martelli, A.M.2    Gilmour, R.S.3    Ognibene, A.4    Manzoli, F.A.5    Irvine, R.F.6
  • 22
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus
    • Divecha N., Banfic H., and Irvine R.F. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J. 10 (1991) 3207-3214
    • (1991) EMBO J. , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 23
    • 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., and 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
  • 25
    • 0025936626 scopus 로고
    • Associations between distinct pre-mRNA splicing components and the cell nucleus
    • Spector D.L., Fu X.D., and Maniatis T. Associations between distinct pre-mRNA splicing components and the cell nucleus. EMBO J. 10 (1991) 3467-3481
    • (1991) EMBO J. , vol.10 , pp. 3467-3481
    • Spector, D.L.1    Fu, X.D.2    Maniatis, T.3
  • 26
    • 0027135889 scopus 로고
    • Macromolecular domains within the cell nucleus
    • Spector D.L. Macromolecular domains within the cell nucleus. Annu. Rev. Cell Biol. 9 (1993) 265-315
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 265-315
    • Spector, D.L.1
  • 27
    • 0029826064 scopus 로고    scopus 로고
    • Dynamic organization of pre-mRNA splicing factors
    • Huang S., and Spector D.L. Dynamic organization of pre-mRNA splicing factors. J. Cell. Biochem. 62 (1996) 191-197
    • (1996) J. Cell. Biochem. , vol.62 , pp. 191-197
    • Huang, S.1    Spector, D.L.2
  • 28
    • 0030589682 scopus 로고    scopus 로고
    • The localization of sites containing nascent RNA and splicing factors
    • Pombo A., and Cook P.R. The localization of sites containing nascent RNA and splicing factors. Exp. Cell Res. 229 (1996) 201-203
    • (1996) Exp. Cell Res. , vol.229 , pp. 201-203
    • Pombo, A.1    Cook, P.R.2
  • 29
    • 0027488514 scopus 로고
    • Reversible disassembly of transcription domains in lymphocyte nuclei during inhibition of RNA synthesis by DRB
    • Davis L., Cadrin M., Brown D.L., and Chaly N. Reversible disassembly of transcription domains in lymphocyte nuclei during inhibition of RNA synthesis by DRB. Biol. Cell 78 (1993) 163-180
    • (1993) Biol. Cell , vol.78 , pp. 163-180
    • Davis, L.1    Cadrin, M.2    Brown, D.L.3    Chaly, N.4
  • 30
    • 0021082681 scopus 로고
    • Immunoelectron microscopic localization of snRNPs
    • Spector D.L., Schrier W.H., and Busch H. Immunoelectron microscopic localization of snRNPs. Biol. Cell 49 (1983) 1-10
    • (1983) Biol. Cell , vol.49 , pp. 1-10
    • Spector, D.L.1    Schrier, W.H.2    Busch, H.3
  • 31
    • 0035930577 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase c2alpha contains a nuclear localization sequence and associates with nuclear speckles
    • Didichenko S.A., and Thelen M. Phosphatidylinositol 3-kinase c2alpha contains a nuclear localization sequence and associates with nuclear speckles. J. Biol. Chem. 276 (2001) 48135-48142
    • (2001) J. Biol. Chem. , vol.276 , pp. 48135-48142
    • Didichenko, S.A.1    Thelen, M.2
  • 34
    • 0031846441 scopus 로고    scopus 로고
    • Functional association of nuclear protein 4.1 with pre-mRNA splicing factors
    • Lallena M.J., Martinez C., Valcarcel J., and Correas I. Functional association of nuclear protein 4.1 with pre-mRNA splicing factors. J. Cell Sci. 111 (1998) 1963-1971
    • (1998) J. Cell Sci. , vol.111 , pp. 1963-1971
    • Lallena, M.J.1    Martinez, C.2    Valcarcel, J.3    Correas, I.4
  • 35
    • 0013842227 scopus 로고
    • Composition and metabolism of lipids within repressed and active chromatin of interphase lymphocytes
    • Rose H.G., and Frenster J.H. Composition and metabolism of lipids within repressed and active chromatin of interphase lymphocytes. Biochim. Biophys. Acta 106 (1965) 577-591
    • (1965) Biochim. Biophys. Acta , vol.106 , pp. 577-591
    • Rose, H.G.1    Frenster, J.H.2
  • 36
    • 0019345299 scopus 로고
    • Effect of phospholipid vesicles on endogenous RNA polymerase activity of isolated rat liver nuclei
    • Capitani S., Caramelli E., Felaco M., Miscia S., and Manzoli F.A. Effect of phospholipid vesicles on endogenous RNA polymerase activity of isolated rat liver nuclei. Physiol. Chem. Phys. 13 (1981) 153-158
    • (1981) Physiol. Chem. Phys. , vol.13 , pp. 153-158
    • Capitani, S.1    Caramelli, E.2    Felaco, M.3    Miscia, S.4    Manzoli, F.A.5
  • 37
    • 0036877042 scopus 로고    scopus 로고
    • DNA-lipid interactions in vitro and in vivo
    • Kuvichkin V.V. DNA-lipid interactions in vitro and in vivo. Bioelectrochemistry 58 (2002) 3-12
    • (2002) Bioelectrochemistry , vol.58 , pp. 3-12
    • Kuvichkin, V.V.1
  • 38
    • 0032518571 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate reverses the inhibition of RNA transcription caused by histone H1
    • Yu H., Fukami K., Watanabe Y., Ozaki C., and Takenawa T. Phosphatidylinositol 4,5-bisphosphate reverses the inhibition of RNA transcription caused by histone H1. Eur. J. Biochem. 251 (1998) 281-287
    • (1998) Eur. J. Biochem. , vol.251 , pp. 281-287
    • Yu, H.1    Fukami, K.2    Watanabe, Y.3    Ozaki, C.4    Takenawa, T.5
  • 39
    • 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., and 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
  • 40
    • 0029157378 scopus 로고
    • Evolution of the SNF2 family of proteins: subfamilies with distinct sequences and functions
    • Eisen J.A., Sweder K.S., and Hanawalt P.C. Evolution of the SNF2 family of proteins: subfamilies with distinct sequences and functions. Nucleic Acids Res. 23 (1995) 2715-2723
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2715-2723
    • Eisen, J.A.1    Sweder, K.S.2    Hanawalt, P.C.3
  • 41
    • 0042671282 scopus 로고    scopus 로고
    • Involvement of actin-related proteins in ATP-dependent chromatin remodeling
    • Shen X., Ranallo R., Choi E., and Wu C. Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol. Cell 12 (2003) 147-155
    • (2003) Mol. Cell , vol.12 , pp. 147-155
    • Shen, X.1    Ranallo, R.2    Choi, E.3    Wu, C.4
  • 42
    • 0037022632 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex
    • Rando O.J., Zhao K., Janmey P., and Crabtree G.R. Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 2824-2829
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2824-2829
    • Rando, O.J.1    Zhao, K.2    Janmey, P.3    Crabtree, G.R.4
  • 43
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin H.L., and Janmey P.A. Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65 (2003) 761-789
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 44
    • 0037006803 scopus 로고    scopus 로고
    • Type I PIPkinases interact with and are regulated by the retinoblastoma susceptibility gene product-pRB
    • Divecha N., Roefs M., Los A., Halstead J., Bannister A., and D'Santos C. Type I PIPkinases interact with and are regulated by the retinoblastoma susceptibility gene product-pRB. Curr. Biol. 12 (2002) 582-587
    • (2002) Curr. Biol. , vol.12 , pp. 582-587
    • Divecha, N.1    Roefs, M.2    Los, A.3    Halstead, J.4    Bannister, A.5    D'Santos, C.6
  • 45
    • 1642540254 scopus 로고    scopus 로고
    • BRG1 controls the activity of the retinoblastoma protein via regulation of p21CIP1/WAF1/SDI
    • Kang H., Cui K., and Zhao K. BRG1 controls the activity of the retinoblastoma protein via regulation of p21CIP1/WAF1/SDI. Mol. Cell. Biol. 24 (2004) 1188-1199
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1188-1199
    • Kang, H.1    Cui, K.2    Zhao, K.3
  • 46
    • 0028861418 scopus 로고
    • The PHD finger: implications for chromatin-mediated transcriptional regulation
    • Aasland R., Gibson T.J., and 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
  • 48
    • 0036850549 scopus 로고    scopus 로고
    • Different HATS of the ING1 gene family
    • Feng X., Hara Y., and 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
  • 49
    • 0035962648 scopus 로고    scopus 로고
    • Chromatin silencing and activation by Polycomb and trithorax group proteins
    • Mahmoudi T., and Verrijzer C.P. Chromatin silencing and activation by Polycomb and trithorax group proteins. Oncogene 20 (2001) 3055-3066
    • (2001) Oncogene , vol.20 , pp. 3055-3066
    • Mahmoudi, T.1    Verrijzer, C.P.2
  • 50
    • 3843053639 scopus 로고    scopus 로고
    • The direct interaction between ASH2, a Drosophila trithorax group protein, and SKTL, a nuclear phosphatidylinositol 4-phosphate 5-kinase, implies a role for phosphatidylinositol 4,5-bisphosphate in maintaining transcriptionally active chromatin
    • Cheng M.K., and Shearn A. The direct interaction between ASH2, a Drosophila trithorax group protein, and SKTL, a nuclear phosphatidylinositol 4-phosphate 5-kinase, implies a role for phosphatidylinositol 4,5-bisphosphate in maintaining transcriptionally active chromatin. Genetics 167 (2004) 1213-1223
    • (2004) Genetics , vol.167 , pp. 1213-1223
    • Cheng, M.K.1    Shearn, A.2
  • 51
    • 0033975839 scopus 로고    scopus 로고
    • Histone H1 is a specific repressor of core histone acetylation in chromatin
    • Herrera J.E., West K.L., Schiltz R.L., Nakatani Y., and Bustin M. Histone H1 is a specific repressor of core histone acetylation in chromatin. Mol. Cell. Biol. 20 (2000) 523-529
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 523-529
    • Herrera, J.E.1    West, K.L.2    Schiltz, R.L.3    Nakatani, Y.4    Bustin, M.5
  • 52
    • 0042967817 scopus 로고    scopus 로고
    • Regulation of PI4,5P2 synthesis by nuclear-cytoplasmic shuttling of the Mss4 lipid kinase
    • Audhya A., and Emr S.D. Regulation of PI4,5P2 synthesis by nuclear-cytoplasmic shuttling of the Mss4 lipid kinase. EMBO J. 22 (2003) 4223-4236
    • (2003) EMBO J. , vol.22 , pp. 4223-4236
    • Audhya, A.1    Emr, S.D.2
  • 53
    • 0033516604 scopus 로고    scopus 로고
    • A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
    • York J.D., Odom A.R., Murphy R., Ives E.B., and Wente S.R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285 (1999) 96-100
    • (1999) Science , vol.285 , pp. 96-100
    • York, J.D.1    Odom, A.R.2    Murphy, R.3    Ives, E.B.4    Wente, S.R.5
  • 54
    • 0034677903 scopus 로고    scopus 로고
    • A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control
    • Odom A.R., Stahlberg A., Wente S.R., and York J.D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287 (2000) 2026-2029
    • (2000) Science , vol.287 , pp. 2026-2029
    • Odom, A.R.1    Stahlberg, A.2    Wente, S.R.3    York, J.D.4
  • 55
  • 56
    • 0037414839 scopus 로고    scopus 로고
    • Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates
    • Shen X., Xiao H., Ranallo R., Wu W.H., and 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
  • 57
    • 0036711574 scopus 로고    scopus 로고
    • The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization
    • Nalaskowski M.M., Deschermeier C., Fanick W., and Mayr G.W. The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization. Biochem. J. 366 (2002) 549-556
    • (2002) Biochem. J. , vol.366 , pp. 549-556
    • Nalaskowski, M.M.1    Deschermeier, C.2    Fanick, W.3    Mayr, G.W.4
  • 58
    • 0035970013 scopus 로고    scopus 로고
    • Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export
    • Feng Y., Wente S.R., and Majerus P.W. Overexpression of the inositol phosphatase SopB in human 293 cells stimulates cellular chloride influx and inhibits nuclear mRNA export. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 875-879
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 875-879
    • Feng, Y.1    Wente, S.R.2    Majerus, P.W.3
  • 59
    • 0024673503 scopus 로고
    • S-phase induction and transformation of quiescent NIH 3T3 cells by microinjection of phospholipase C
    • Smith M.R., Ryu S.H., Suh P.G., Rhee S.G., and Kung H.F. S-phase induction and transformation of quiescent NIH 3T3 cells by microinjection of phospholipase C. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 3659-3663
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 3659-3663
    • Smith, M.R.1    Ryu, S.H.2    Suh, P.G.3    Rhee, S.G.4    Kung, H.F.5
  • 60
    • 0031843418 scopus 로고    scopus 로고
    • Overexpression of phosphoinositide-specific phospholipase Cgamma in NIH 3T3 cells promotes transformation and tumorigenicity
    • Smith M.R., Court D.W., Kim H.K., Park J.B., Rhee S.G., Rhim J.S., and Kung H.F. Overexpression of phosphoinositide-specific phospholipase Cgamma in NIH 3T3 cells promotes transformation and tumorigenicity. Carcinogenesis 19 (1998) 177-185
    • (1998) Carcinogenesis , vol.19 , pp. 177-185
    • Smith, M.R.1    Court, D.W.2    Kim, H.K.3    Park, J.B.4    Rhee, S.G.5    Rhim, J.S.6    Kung, H.F.7
  • 61
    • 0028845272 scopus 로고
    • Changes in the components of a nuclear inositide cycle during differentiation in murine erythroleukaemia cells
    • Divecha N., Letcher A.J., Banfic H.H., Rhee S.G., and Irvine R.F. Changes in the components of a nuclear inositide cycle during differentiation in murine erythroleukaemia cells. Biochem. J. 312 Pt. 1 (1995) 63-67
    • (1995) Biochem. J. , vol.312 , Issue.PART 1 , pp. 63-67
    • Divecha, N.1    Letcher, A.J.2    Banfic, H.H.3    Rhee, S.G.4    Irvine, R.F.5
  • 63
    • 0026538252 scopus 로고
    • Existence of phosphoinositide-specific phospholipase C in rat liver nuclei and its change during liver regeneration
    • Kuriki H., Tamiya-Koizumi K., Asano M., Yoshida S., Kojima K., and Nimura Y. Existence of phosphoinositide-specific phospholipase C in rat liver nuclei and its change during liver regeneration. J. Biochem. (Tokyo) 111 (1992) 283-286
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 283-286
    • Kuriki, H.1    Tamiya-Koizumi, K.2    Asano, M.3    Yoshida, S.4    Kojima, K.5    Nimura, Y.6
  • 64
    • 0242317413 scopus 로고    scopus 로고
    • Involvement of nuclear phosphatidylinositol-dependent phospholipases C in cell cycle progression during rat liver regeneration
    • Albi E., Rossi G., Maraldi N.M., Magni M.V., Cataldi S., Solimando L., and Zini N. Involvement of nuclear phosphatidylinositol-dependent phospholipases C in cell cycle progression during rat liver regeneration. J. Cell. Physiol. 197 (2003) 181-188
    • (2003) J. Cell. Physiol. , vol.197 , pp. 181-188
    • Albi, E.1    Rossi, G.2    Maraldi, N.M.3    Magni, M.V.4    Cataldi, S.5    Solimando, L.6    Zini, N.7
  • 65
    • 0034672643 scopus 로고    scopus 로고
    • Insulin selectively stimulates nuclear phosphoinositide-specific phospholipase C (PI-PLC) beta1 activity through a mitogen-activated protein (MAP) kinase-dependent serine phosphorylation
    • Martelli A.M., Billi A.M., Manzoli L., Faenza I., Aluigi M., Falconi M., De Pol A., Gilmour R.S., and Cocco L. Insulin selectively stimulates nuclear phosphoinositide-specific phospholipase C (PI-PLC) beta1 activity through a mitogen-activated protein (MAP) kinase-dependent serine phosphorylation. FEBS Lett. 486 (2000) 230-236
    • (2000) FEBS Lett. , vol.486 , pp. 230-236
    • Martelli, A.M.1    Billi, A.M.2    Manzoli, L.3    Faenza, I.4    Aluigi, M.5    Falconi, M.6    De Pol, A.7    Gilmour, R.S.8    Cocco, L.9
  • 66
    • 0035052817 scopus 로고    scopus 로고
    • Phosphorylation of nuclear phospholipase C beta1 by extracellular signal-regulated kinase mediates the mitogenic action of insulin-like growth factor I
    • Xu A., Suh P.G., Marmy-Conus N., Pearson R.B., Seok O.Y., Cocco L., and Gilmour R.S. Phosphorylation of nuclear phospholipase C beta1 by extracellular signal-regulated kinase mediates the mitogenic action of insulin-like growth factor I. Mol. Cell. Biol. 21 (2001) 2981-2990
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2981-2990
    • Xu, A.1    Suh, P.G.2    Marmy-Conus, N.3    Pearson, R.B.4    Seok, O.Y.5    Cocco, L.6    Gilmour, R.S.7
  • 67
    • 0035805635 scopus 로고    scopus 로고
    • Protein kinase C alpha -mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C beta1 in Swiss 3T3 cells
    • Xu A., Wang Y., Xu L.Y., and Gilmour R.S. Protein kinase C alpha -mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C beta1 in Swiss 3T3 cells. J. Biol. Chem. 276 (2001) 14980-14986
    • (2001) J. Biol. Chem. , vol.276 , pp. 14980-14986
    • Xu, A.1    Wang, Y.2    Xu, L.Y.3    Gilmour, R.S.4
  • 68
  • 71
    • 18944395803 scopus 로고    scopus 로고
    • Nucleophosmin/B23, a nuclear PI(3,4,5)P(3) receptor, mediates the antiapoptotic actions of NGF by inhibiting CAD
    • Ahn J.Y., Liu X., Cheng D., Peng J., Chan P.K., Wade P.A., and Ye K. Nucleophosmin/B23, a nuclear PI(3,4,5)P(3) receptor, mediates the antiapoptotic actions of NGF by inhibiting CAD. Mol. Cell 18 (2005) 435-445
    • (2005) Mol. Cell , vol.18 , pp. 435-445
    • Ahn, J.Y.1    Liu, X.2    Cheng, D.3    Peng, J.4    Chan, P.K.5    Wade, P.A.6    Ye, K.7
  • 72
    • 0028301412 scopus 로고
    • Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells
    • York J.D., and Majerus P.W. Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells. J. Biol. Chem. 269 (1994) 7847-7850
    • (1994) J. Biol. Chem. , vol.269 , pp. 7847-7850
    • York, J.D.1    Majerus, P.W.2
  • 73
    • 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 S.C., Halstead J.R., Irvine R.F., and 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, S.C.3    Halstead, J.R.4    Irvine, R.F.5    Divecha, N.6
  • 74
    • 0030722721 scopus 로고    scopus 로고
    • A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition
    • Sun B., Murray N.R., and Fields A.P. A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition. J. Biol. Chem. 272 (1997) 26313-26317
    • (1997) J. Biol. Chem. , vol.272 , pp. 26313-26317
    • Sun, B.1    Murray, N.R.2    Fields, A.P.3
  • 75
    • 18044398191 scopus 로고    scopus 로고
    • Nuclear phospholipase C-beta1b activation during G2/M and late G1 phase in nocodazole-synchronized HL-60 cells
    • Lukinovic-Skudar V., Donlagic L., Banfic H., and Visnjic D. Nuclear phospholipase C-beta1b activation during G2/M and late G1 phase in nocodazole-synchronized HL-60 cells. Biochim. Biophys. Acta 1733 (2005) 148-156
    • (2005) Biochim. Biophys. Acta , vol.1733 , pp. 148-156
    • Lukinovic-Skudar, V.1    Donlagic, L.2    Banfic, H.3    Visnjic, D.4
  • 77
    • 0042971700 scopus 로고    scopus 로고
    • PTEN induces cell cycle arrest by decreasing the level and nuclear localization of cyclin D1
    • Radu A., Neubauer V., Akagi T., Hanafusa H., and Georgescu M.M. PTEN induces cell cycle arrest by decreasing the level and nuclear localization of cyclin D1. Mol. Cell. Biol. 23 (2003) 6139-6149
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6139-6149
    • Radu, A.1    Neubauer, V.2    Akagi, T.3    Hanafusa, H.4    Georgescu, M.M.5
  • 78
    • 24944568790 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic partitioning of phosphatase and tensin homologue deleted on chromosome 10 (PTEN) differentially regulates the cell cycle and apoptosis
    • Chung J.H., and Eng C. Nuclear-cytoplasmic partitioning of phosphatase and tensin homologue deleted on chromosome 10 (PTEN) differentially regulates the cell cycle and apoptosis. Cancer Res. 65 (2005) 8096-8100
    • (2005) Cancer Res. , vol.65 , pp. 8096-8100
    • Chung, J.H.1    Eng, C.2
  • 79
  • 80
    • 0020702214 scopus 로고
    • Association of actin with the nuclear matrix from bovine lymphocytes
    • Nakayasu H., and Ueda K. Association of actin with the nuclear matrix from bovine lymphocytes. Exp. Cell Res. 143 (1983) 55-62
    • (1983) Exp. Cell Res. , vol.143 , pp. 55-62
    • Nakayasu, H.1    Ueda, K.2
  • 81
    • 0022416568 scopus 로고
    • Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells
    • Nakayasu H., and Ueda K. Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells. Cell Struct. Funct. 10 (1985) 305-309
    • (1985) Cell Struct. Funct. , vol.10 , pp. 305-309
    • Nakayasu, H.1    Ueda, K.2
  • 82
    • 10644245953 scopus 로고    scopus 로고
    • Use of mass spectrometry-based lipidomics to probe PITPalpha (phosphatidylinositol transfer protein alpha) function inside the nuclei of PITPalpha+/+ and PITPalpha-/- cells
    • Hunt A.N., Alb J.G., Koster G., Postle A.D., and Bankaitis V.A. Use of mass spectrometry-based lipidomics to probe PITPalpha (phosphatidylinositol transfer protein alpha) function inside the nuclei of PITPalpha+/+ and PITPalpha-/- cells. Biochem. Soc. Trans. 32 (2004) 1063-1065
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 1063-1065
    • Hunt, A.N.1    Alb, J.G.2    Koster, G.3    Postle, A.D.4    Bankaitis, V.A.5
  • 83
    • 0031566185 scopus 로고    scopus 로고
    • Phosphoinositide signalling in nuclei of Friend cells: DMSO-induced differentiation reduces the association of phosphatidylinositol-transfer protein with the nucleus
    • Rubbini S., Cocco L., Manzoli L., Lutterman J., Billi A.M., Matteucci A., and Wirtz K.W. Phosphoinositide signalling in nuclei of Friend cells: DMSO-induced differentiation reduces the association of phosphatidylinositol-transfer protein with the nucleus. Biochem. Biophys. Res. Commun. 230 (1997) 302-305
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 302-305
    • Rubbini, S.1    Cocco, L.2    Manzoli, L.3    Lutterman, J.4    Billi, A.M.5    Matteucci, A.6    Wirtz, K.W.7
  • 84
    • 9644281048 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins: emerging roles in cell proliferation, cell death and survival
    • Snoek G.T. Phosphatidylinositol transfer proteins: emerging roles in cell proliferation, cell death and survival. IUBMB Life 56 (2004) 467-475
    • (2004) IUBMB Life , vol.56 , pp. 467-475
    • Snoek, G.T.1
  • 85
    • 0032576758 scopus 로고    scopus 로고
    • Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein
    • Sha B., Phillips S.E., Bankaitis V.A., and Luo M. Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Nature 391 (1998) 506-510
    • (1998) Nature , vol.391 , pp. 506-510
    • Sha, B.1    Phillips, S.E.2    Bankaitis, V.A.3    Luo, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.