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Volumn 4, Issue 5, 2003, Pages 349-360

Nuclear lipid signalling

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DIACYLGLYCEROL KINASE; INOSITOL; ISOPROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C; PHOSPHOLIPID; PROTEIN KINASE C;

EID: 0037880798     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1100     Document Type: Review
Times cited : (316)

References (135)
  • 1
    • 0032497839 scopus 로고    scopus 로고
    • Een DAG uit het leven van de inositide signalering in de nucleus
    • D'Santos, C. S., Clarke, J. H. & Divecha, N. Phospholipid signalling in the nucleus. Een DAG uit het leven van de inositide signalering in de nucleus. Biochim. Biophys. Acta 1436, 201-232 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 201-232
    • D'Santos, C.S.1    Clarke, J.H.2    Divecha, N.3
  • 3
    • 0035823037 scopus 로고    scopus 로고
    • Re-examination of the mechanisms regulating nuclear inositol lipid metabolism
    • Martelli, A. M. et al. Re-examination of the mechanisms regulating nuclear inositol lipid metabolism. FEBS Lett. 505, 1-6 (2001).
    • (2001) FEBS Lett. , vol.505 , pp. 1-6
    • Martelli, A.M.1
  • 4
    • 0038799935 scopus 로고    scopus 로고
    • Nuclear lipid signalling
    • Irvine, R. F. Nuclear lipid signalling STKE «http://stke.sciencemag.org/cgi/content/full/sigtrans;2002/ 150/re13» (2002).
    • (2002) STKE
    • Irvine, R.F.1
  • 5
    • 0037009847 scopus 로고    scopus 로고
    • Nuclear inositol lipid signaling and its potential involvement in malignant transformation
    • Martelli, A. et al. Nuclear inositol lipid signaling and its potential involvement in malignant transformation. Biochim. Biophys. Acta 1603, 11-17 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1603 , pp. 11-17
    • Martelli, A.1
  • 6
    • 0038462155 scopus 로고
    • Phosphorylation of rat liver envelopes, characterisation of in vitro phosphorylation
    • Smith, C. D. & Wells, W. W. Phosphorylation of rat liver envelopes, characterisation of in vitro phosphorylation. J. Biol. Chem. 258, 765-770 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 765-770
    • Smith, C.D.1    Wells, W.W.2
  • 7
    • 0023657043 scopus 로고
    • Synthesis of polyphosphoinositides in the nuclei of Friend cells
    • 2-based signalling system that is distinct from that in the cytoplasm.
    • (1987) Biochem. J. , vol.248 , pp. 765-770
    • Cocco, L.1
  • 8
    • 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. et al. 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. 154, 1266-1272 (1988).
    • (1988) Biochem. Biophys. Res. , vol.154 , pp. 1266-1272
    • Cocco, L.1
  • 9
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-1) 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. & Irvine, R. F. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-1) 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, 3207-3214 (1991).
    • (1991) EMBO J. , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 10
    • 0025799978 scopus 로고
    • Temporal changes in intracellular distribution of protein kinase C in Swiss 3T3 cells during mitogenic stimulation with insulin-like growth factor I and bombesin: Translocation to the nucleus follows rapid changes in nuclear polyphosphoinositides
    • Martelli, A. M. et al. Temporal changes in intracellular distribution of protein kinase C in Swiss 3T3 cells during mitogenic stimulation with insulin-like growth factor I and bombesin: translocation to the nucleus follows rapid changes in nuclear polyphosphoinositides. Biochem. Biophys. Res. Commun. 177, 480-487 (1991).
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 480-487
    • Martelli, A.M.1
  • 11
    • 0032497831 scopus 로고    scopus 로고
    • PIPkins, their substrates and their products: New functions for old enzymes
    • Hinchliffe, K. A., Ciruela, A. & Irvine, R. F. PIPkins, their substrates and their products: new functions for old enzymes. Biochim. Biophys. Acta 1436, 87-104 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 87-104
    • Hinchliffe, K.A.1    Ciruela, A.2    Irvine, R.F.3
  • 12
    • 0034911881 scopus 로고    scopus 로고
    • Synthesis and function of 3-phosphorylated inositol lipids
    • Vanhaesebroeck, B. et al. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70, 535-602 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 535-602
    • Vanhaesebroeck, B.1
  • 13
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: The return of the inositol phosphates
    • Irvine, R. F. & Schell, M. J. Back in the water: the return of the inositol phosphates. Nature Rev. Mol. Cell Biol. 2, 327-338 (2001).
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 14
    • 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. & Divecha, N. Metabolism and possible compartmentalization of inositol lipids in isolated rat-liver nuclei. Biochem. J. 327, 569-576 (1997).
    • (1997) Biochem. J. , vol.327 , pp. 569-576
    • Vann, L.R.1    Wooding, F.B.2    Irvine, R.F.3    Divecha, N.4
  • 15
    • 0036566427 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C-δ 1
    • 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-δ1. Biochem. J. 363, 657-666 (2002).
    • (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
  • 16
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Jamney, P. A. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56, 169-191 (1994).
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Jamney, P.A.1
  • 17
    • 0033546210 scopus 로고    scopus 로고
    • The organization of replication and transcription
    • Cook, P. R. The organization of replication and transcription. Science 284, 1790-1795 (1999).
    • (1999) Science , vol.284 , pp. 1790-1795
    • Cook, P.R.1
  • 18
    • 0034160165 scopus 로고    scopus 로고
    • Searching for a function for nuclear actin
    • Rando, O. J., Zhao, K. & Crabtree, G. R. searching for a function for nuclear actin. Trends Cell Biol. 10, 92-97 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 92-97
    • Rando, O.J.1    Zhao, K.2    Crabtree, G.R.3
  • 20
    • 0031051629 scopus 로고    scopus 로고
    • Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope
    • Fricker, M., Hollinshead, M., White, N. & Vaux, D. Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope. J. Cell Biol. 136, 531-544 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 531-544
    • Fricker, M.1    Hollinshead, M.2    White, N.3    Vaux, D.4
  • 21
    • 0029791261 scopus 로고    scopus 로고
    • Functional compartmentalization of the nucleus
    • Strouboulis, J. & Wolffe, A. P. Functional compartmentalization of the nucleus. J. Cell Sci. 109, 1991-2000 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 1991-2000
    • Strouboulis, J.1    Wolffe, A.P.2
  • 22
    • 0034644651 scopus 로고    scopus 로고
    • Nuclear localization of enzymatically active green fluorescent protein - CTP: Phosphocholine cytidylyltransferase-α fusion protein is independent of cell cycle conditions and cell types
    • DeLong, C. J., Qin, L. & Cui, Z. Nuclear localization of enzymatically active green fluorescent protein - CTP: phosphocholine cytidylyltransferase-α fusion protein is independent of cell cycle conditions and cell types. J. Biol. Chem. 275, 32325-32330 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 32325-32330
    • DeLong, C.J.1    Qin, L.2    Cui, Z.3
  • 23
    • 0035896516 scopus 로고    scopus 로고
    • Highly saturated endonuclear phosphatidylcholine is synthesized in situ and colocated with CDP-choline pathway enzymes
    • Hunt, A. N., Clark, G. T., Attard, G. S. & Postle, A. D. Highly saturated endonuclear phosphatidylcholine is synthesized in situ and colocated with CDP-choline pathway enzymes. J. Biol. Chem. 276, 8492-8499 (2001). By using mass-spectrometric analysis of deuterated species, this paper follows the distinct nuclear remodelling of PtdCho so that its fatty acyl chains are predominantly saturated. In this form it might have an important structural role.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8492-8499
    • Hunt, A.N.1    Clark, G.T.2    Attard, G.S.3    Postle, A.D.4
  • 24
    • 0035008878 scopus 로고    scopus 로고
    • A comparison of the molecular species compositions of mammalian lung surfactant phospholipids
    • Postle, A. D., Heeley, E. L. & Wilton, D. C. A comparison of the molecular species compositions of mammalian lung surfactant phospholipids. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129, 65-73 (2001).
    • (2001) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.129 , pp. 65-73
    • Postle, A.D.1    Heeley, E.L.2    Wilton, D.C.3
  • 25
    • 0026730882 scopus 로고
    • A Differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix
    • Payrastre, B. et al. A Differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix. J. Biol. Chem. 267, 5078-5084 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 5078-5084
    • Payrastre, B.1
  • 26
    • 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, 3547-3560 (1998).
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 3547-3560
    • Boronenkov, I.V.1    Loijens, J.C.2    Umeda, M.3    Anderson, R.A.4
  • 28
    • 0026693238 scopus 로고
    • Nuclear localisation and signalling activity of phosphoinositidase Cβ in Swiss 3T3 cells
    • Martelli, A. M. et al. Nuclear localisation and signalling activity of phosphoinositidase Cβ in Swiss 3T3 cells. Nature 358, 242-244 (1992).
    • (1992) Nature , vol.358 , pp. 242-244
    • Martelli, A.M.1
  • 29
    • 0027446592 scopus 로고
    • Phosphoinositide signalling enzymes in rat liver nuclei: Phosphoinositidase C isoform β1 is specifically, but not predominately, located in the nucleus
    • Divecha, N., Rhee, S. G., Letcher, A. J. & Irvine, R. F. Phosphoinositide signalling enzymes in rat liver nuclei: phosphoinositidase C isoform β1 is specifically, but not predominately, located in the nucleus. Biochem. J. 289, 617-620 (1993).
    • (1993) Biochem. J. , vol.289 , pp. 617-620
    • Divecha, N.1    Rhee, S.G.2    Letcher, A.J.3    Irvine, R.F.4
  • 30
    • 0032533857 scopus 로고    scopus 로고
    • Nuclear but not cytoplasmic phospholipase C-β 1 inhibits differentiation of erythroleukemia cells
    • Matteucci, A. et al. Nuclear but not cytoplasmic phospholipase C-β1 inhibits differentiation of erythroleukemia cells. Cancer Res. 58, 5057-5060 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 5057-5060
    • Matteucci, A.1
  • 31
    • 0037203868 scopus 로고    scopus 로고
    • Phospholipase C-γ 1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE
    • Ye, K. et al. Phospholipase C-γ1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE. Nature 415, 541-544 (2002).
    • (2002) Nature , vol.415 , pp. 541-544
    • Ye, K.1
  • 32
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee, S. G. & Bae, Y. S. Regulation of phosphoinositide- specific phospholipase C isozymes. J. Biol. Chem. 272, 15045-15048 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 33
    • 0034730764 scopus 로고    scopus 로고
    • A role for nuclear phospholipase C-β 1 in cell cycle control
    • Faenza, I. et al. A role for nuclear phospholipase C-β1 in cell cycle control. J. Biol. Chem. 275, 30520-30524 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 30520-30524
    • Faenza, I.1
  • 34
    • 0027995232 scopus 로고
    • Two forms of phospholipase C-β 1 generated by alternative splicing
    • Bahk, Y. Y. et al. Two forms of phospholipase C-β1 generated by alternative splicing. J. Biol. Chem. 269, 8240-8245 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 8240-8245
    • Bahk, Y.Y.1
  • 35
    • 0029841118 scopus 로고    scopus 로고
    • qα-dependent activation, particulate association, and nuclear localization of phospholipase C-β1
    • qα-dependent activation, particulate association, and nuclear localization of phospholipase C-β1. J. Biol. Chem. 271, 21187-21192 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 21187-21192
    • Kim, C.G.1    Park, D.2    Rhee, S.G.3
  • 36
    • 0032484668 scopus 로고    scopus 로고
    • Localization of two forms of phospholipase C-β1, a and b, in C6Bu-1 cells
    • Bahk, Y. Y. et al. Localization of two forms of phospholipase C-β1, a and b, in C6Bu-1 cells. Biochim. Biophys. Acta 1389, 76-80 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1389 , pp. 76-80
    • Bahk, Y.Y.1
  • 38
    • 0033103936 scopus 로고    scopus 로고
    • Insulin-like growth factor-I-dependent stimulation of nuclear phospholipase C-β1 activity in Swiss 3T3 cells requires an intact cytoskeleton and is paralleled by increased phosphorylation of the phospholipase
    • Martelli, A. M. et al. Insulin-like growth factor-I-dependent stimulation of nuclear phospholipase C-β1 activity in Swiss 3T3 cells requires an intact cytoskeleton and is paralleled by increased phosphorylation of the phospholipase. J. Cell. Biochem. 72, 339-348 (1999).
    • (1999) J. Cell. Biochem. , vol.72 , pp. 339-348
    • Martelli, A.M.1
  • 39
    • 0034672643 scopus 로고    scopus 로고
    • Insulin selectively stimulates nuclear phosphoinositide-specific phospholipase C (PI-PLC) β1 activity through a mitogen-activated protein (MAP) kinase-dependent serine phosphorylation
    • Martelli, A. M. et al. Insulin selectively stimulates nuclear phosphoinositide-specific phospholipase C (PI-PLC) β1 activity through a mitogen-activated protein (MAP) kinase-dependent serine phosphorylation. FEBS Lett. 486, 230-236 (2000).
    • (2000) FEBS Lett. , vol.486 , pp. 230-236
    • Martelli, A.M.1
  • 40
    • 0035052817 scopus 로고    scopus 로고
    • Phosphorylation of nuclear phospholipase C-β1 by extracellular signal-regulated kinase mediates the mitogenic action of insulin-like growth factor I
    • 1 - it is phosphorylated by extracellular signal-regulated protein kinases.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2981-2990
    • Xu, A.1
  • 41
    • 0030913613 scopus 로고    scopus 로고
    • Essential role for nuclear phospholipase C-β1 in insulin-like growth factor I-induced mitogenesis
    • Manzoli, L. et al. Essential role for nuclear phospholipase C-β1 in insulin-like growth factor I-induced mitogenesis. Cancer Res. 57, 2137-2139 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 2137-2139
    • Manzoli, L.1
  • 42
    • 0035805635 scopus 로고    scopus 로고
    • Protein kinase C-α-mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C-β1 in Swiss 3T3 cells
    • Xu, A., Wang, Y., Xu, L. Y. & Gilmour, P. S. Protein kinase C-α-mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C-β1 in Swiss 3T3 cells. J. Biol. Chem. 276, 14980-14986 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 14980-14986
    • Xu, A.1    Wang, Y.2    Xu, L.Y.3    Gilmour, P.S.4
  • 43
    • 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., Rhea, S. G. & Irvine, R. F. Changes in the components of a nuclear inositide cycle during differentiation in murine erythroleukaemia cells. Biochem. J. 312, 63-67 (1995).
    • (1995) Biochem. J. , vol.312 , pp. 63-67
    • Divecha, N.1    Letcher, A.J.2    Banfic, H.H.3    Rhea, S.G.4    Irvine, R.F.5
  • 44
    • 0037042379 scopus 로고    scopus 로고
    • Nuclear PLC-β1 acts as a negative regulator of p45/NF-E 2 expression levels in Friend erythroleukemia cells
    • Faenza, I. et al. Nuclear PLC-β1 acts as a negative regulator of p45/NF-E2 expression levels in Friend erythroleukemia cells. Biochim. Biophys. Acta 1589, 305-310 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 305-310
    • Faenza, I.1
  • 45
    • 0033635799 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear phospholipase C-β1 relocation: Role in resumption of meiosis in the mouse oocyte
    • Avazeri, N., Courtot, A. M., Pasty, A., Duquenne, C. & Lefevre, B. Cytoplasmic and nuclear phospholipase C-β1 relocation: role in resumption of meiosis in the mouse oocyte. Mol. Biol. Cell 11, 4369-4380 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4369-4380
    • Avazeri, N.1    Courtot, A.M.2    Pasty, A.3    Duquenne, C.4    Lefevre, B.5
  • 46
    • 1842373861 scopus 로고    scopus 로고
    • Phospholipase C isozymes selectively couple to specific neurotransmitter receptors
    • Kim, D. et al. Phospholipase C isozymes selectively couple to specific neurotransmitter receptors. Nature 389, 290-293 (1997).
    • (1997) Nature , vol.389 , pp. 290-293
    • Kim, D.1
  • 47
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison, C. J. Lamins: building blocks or regulators of gene expression? Nature Rev. Mol. Cell Biol. 3, 848-858 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 48
    • 0030060801 scopus 로고    scopus 로고
    • A new phospholipase C-δ4 is induced at S-phase of the cell cycle and appears in the nucleus
    • Liu, N., Fukami, K., Yu, H. & Takenawa, T. A new phospholipase C-δ4 is induced at S-phase of the cell cycle and appears in the nucleus. J. Biol. Chem. 271, 355-360 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 355-360
    • Liu, N.1    Fukami, K.2    Yu, H.3    Takenawa, T.4
  • 49
    • 0001275961 scopus 로고    scopus 로고
    • Molecular cloning, splice variants, expression, and purification of phospholipase C-δ4
    • Lee, S. B. & Rhee, S. G. Molecular cloning, splice variants, expression, and purification of phospholipase C-δ4. J. Biol. Chem. 271, 25-31 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 25-31
    • Lee, S.B.1    Rhee, S.G.2
  • 50
    • 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. & Wente, S. R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 295, 96-100 (1999).
    • (1999) Science , vol.295 , pp. 96-100
    • York, J.D.1    Odom, A.R.2    Murphy, R.3    Ives, E.B.4    Wente, S.R.5
  • 51
    • 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. & York, J. D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287, 2026-2029 (2000).
    • (2000) Science , vol.287 , pp. 2026-2029
    • Odom, A.R.1    Stahlberg, A.2    Wente, S.R.3    York, J.D.4
  • 52
    • 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, 112-114 (2003).
    • (2003) Science , vol.299 , pp. 112-114
    • Shen, X.1    Xiao, H.2    Ranallo, R.3    Wu, W.-H.4    Wu, C.5
  • 53
    • 0037414868 scopus 로고    scopus 로고
    • Regulation of chromatin remodeling by inositol polyphosphates
    • 3, which is then phosphorylated to higher inositol phosphates. These in turn might have functions in mRNA export, transcriptional regulation and/or chromatin structure.
    • (2003) Science , vol.299 , pp. 114-116
    • Steger, D.J.1    Haswell, E.S.2    Miller, A.L.3    Wente, S.R.4    O'Shea, E.K.5
  • 54
    • 0033201449 scopus 로고    scopus 로고
    • Phospholipase C-δ1 contains a functional nuclear export signal sequence
    • Yamaga, M., Fujii, M., Kamata, H., Hirata, H. & Yagisawa, H. Phospholipase C-δ1 contains a functional nuclear export signal sequence. J. Biol. Chem. 274, 28537-28541 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28537-28541
    • Yamaga, M.1    Fujii, M.2    Kamata, H.3    Hirata, H.4    Yagisawa, H.5
  • 56
    • 0021750054 scopus 로고
    • Inositol trisphosphate, a novel second messenger in cellular signal transduction
    • Berridge, M. J. & Irvine, R. F. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature 312, 315-321 (1984).
    • (1984) Nature , vol.312 , pp. 315-321
    • Berridge, M.J.1    Irvine, R.F.2
  • 57
    • 0026801172 scopus 로고
    • α-thrombin stimulates nuclear diglyceride levels and differential nuclear localisation of protein kinese C isozymes in IIC9 Cells
    • Leach, K. L. et al. α-thrombin stimulates nuclear diglyceride levels and differential nuclear localisation of protein kinese C isozymes in IIC9 Cells. J. Biol. Chem. 267, 21816-21822 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 21816-21822
    • Leach, K.L.1
  • 58
    • 0033594398 scopus 로고    scopus 로고
    • Nuclei contain two differentially regulated pools of diacylglycerol
    • D'Santos, C. S., Clarke, J. H., Irvine, R. F. & Divecha, N. Nuclei contain two differentially regulated pools of diacylglycerol. Curr. Biol. 9, 437-440 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 437-440
    • D'Santos, C.S.1    Clarke, J.H.2    Irvine, R.F.3    Divecha, N.4
  • 61
    • 0032491522 scopus 로고    scopus 로고
    • Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-α
    • Neri, L. M., Borgatti, P., Capitani, S. & Martelli, A. M. Nuclear diacylglycerol produced by phosphoinositide-specific phospholipase C is responsible for nuclear translocation of protein kinase C-α. J. Biol. Chem. 273, 29738-29744 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 29738-29744
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 62
    • 0036200219 scopus 로고    scopus 로고
    • Proliferating or differentiating stimuli act on different lipid-dependent signaling pathways in nuclei of human leukemia cells
    • Neri, L. M. et al. Proliferating or differentiating stimuli act on different lipid-dependent signaling pathways in nuclei of human leukemia cells. Mol. Biol. Cell 13, 947-964 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 947-964
    • Neri, L.M.1
  • 63
    • 0027536483 scopus 로고
    • Nuclear diacylglycerol is increased during cell proliferation in vivo
    • Banfic, B., Zizak, M., Divecha, N. & Irvine, R. F. Nuclear diacylglycerol is increased during cell proliferation in vivo. Biochem. J. 290, 633-636 (1993).
    • (1993) Biochem. J. , vol.290 , pp. 633-636
    • Banfic, B.1    Zizak, M.2    Divecha, N.3    Irvine, R.F.4
  • 64
    • 0028301412 scopus 로고
    • Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells
    • York, J. D. & Majerus, P. W. Nuclear phosphatidylinositols decrease during S-phase of the cell cycle in HeLa cells. J. Biol. Chem. 269, 7847-7850 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 7847-7850
    • York, J.D.1    Majerus, P.W.2
  • 65
    • 0026909541 scopus 로고
    • Phospholipids in the nucleus-metabolism and possible functions
    • Irvine, R. F. & Divecha, N. Phospholipids in the nucleus -metabolism and possible functions. Semin. Cell Biol. 3, 225-235 (1992).
    • (1992) Semin. Cell Biol. , vol.3 , pp. 225-235
    • Irvine, R.F.1    Divecha, N.2
  • 66
    • 0029418383 scopus 로고
    • The regulation of mitotic nuclear envelope breakdown: A role for multiple lamin kinases
    • Fields, A. P. & Thompson, L. J. The regulation of mitotic nuclear envelope breakdown: a role for multiple lamin kinases. Prog. Cell Cycle Res. 1, 271-286 (1995).
    • (1995) Prog. Cell Cycle Res. , vol.1 , pp. 271-286
    • Fields, A.P.1    Thompson, L.J.2
  • 67
    • 0029666264 scopus 로고    scopus 로고
    • βII protein kinase C is required for the G2/M phase transition of cell cycle
    • 2-M. This in turn recruits PKCβII to the nucleus, where it phosphorylates lamins and participates in the regulation of nuclear-envelope breakdown.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15045-15053
    • Thompson, L.J.1    Fields, A.P.2
  • 68
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi, W., Haas, J., Wagner, M., Krohne, G. & Koszinowski, U. H. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 297, 854-857 (2002).
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 69
    • 0037166312 scopus 로고    scopus 로고
    • Protein kinase C-βII Is an apoptotic lamin kinase in polyomavirus-transformed, etoposide-treated pyF111 rat fibroblasts
    • Chiarini, A., Whitfield, J. F., Armato, U. & Dal Pra, I. Protein kinase C-βII Is an apoptotic lamin kinase in polyomavirus-transformed, etoposide-treated pyF111 rat fibroblasts. J. Biol. Chem. 277, 18827-18839 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 18827-18839
    • Chiarini, A.1    Whitfield, J.F.2    Armato, U.3    Dal Pra, I.4
  • 70
    • 0026067787 scopus 로고
    • Selective translocation of βII-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells
    • Hocevar, B. A. & Fields, A. P. Selective translocation of βII-protein kinase C to the nucleus of human promyelocytic (HL60) leukemia cells. J. Biol. Chem. 266, 28-33 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 28-33
    • Hocevar, B.A.1    Fields, A.P.2
  • 71
    • 0025363850 scopus 로고
    • Role of nuclear protein kinase C in the mitogenic response to platelet-derived growth factor
    • Fields, A. P., Tyler, G., Kraft, A. S. & May, W. S. Role of nuclear protein kinase C in the mitogenic response to platelet-derived growth factor. J. Cell Sci. 96, 107-114 (1990).
    • (1990) J. Cell Sci. , vol.96 , pp. 107-114
    • Fields, A.P.1    Tyler, G.2    Kraft, A.S.3    May, W.S.4
  • 72
    • 0032797276 scopus 로고    scopus 로고
    • Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-ζ translocation to the nucleus of NGF-treated PC12 cells
    • Neri, L. M. et al. Increase in nuclear phosphatidylinositol 3-kinase activity and phosphatidylinositol (3,4,5) trisphosphate synthesis precede PKC-ζ translocation to the nucleus of NGF-treated PC12 cells. FASEB J. 13, 2299-2310 (1999).
    • (1999) FASEB J. , vol.13 , pp. 2299-2310
    • Neri, L.M.1
  • 73
    • 0028175887 scopus 로고
    • Identification of nuclear βII protein kinase C as a mitotic lamin kinase
    • Goss, V. L. et al. Identification of nuclear βII protein kinase C as a mitotic lamin kinase. J. Biol. Chem. 269, 19074-19080 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 19074-19080
    • Goss, V.L.1
  • 74
    • 0035986315 scopus 로고    scopus 로고
    • Molecular characterization of protein kinase C-α binding to lamin A
    • Martelli, A. M. et al. Molecular characterization of protein kinase C-α binding to lamin A. J. Cell. Biochem. 86, 320-330 (2002).
    • (2002) J. Cell. Biochem. , vol.86 , pp. 320-330
    • Martelli, A.M.1
  • 75
    • 0027257457 scopus 로고
    • Molecular cloning and expression of a 90-kDa diacylglycerol kinase that predominantly localizes in neurons
    • Goto, K. & Kondo, H. Molecular cloning and expression of a 90-kDa diacylglycerol kinase that predominantly localizes in neurons. Proc. Natl. Acad. Sci. USA 90, 7598-7602 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7598-7602
    • Goto, K.1    Kondo, H.2
  • 76
    • 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. et al. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95, 625-636 (1998).
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1
  • 77
    • 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. & Takenawa, T. Phosphatidylinositol 4,5-bisphosphate reverses the inhibition of RNA transcription caused by histone H1. Eur. J. Biochem. 251, 281-287 (1998).
    • (1998) Eur. J. Biochem. , vol.251 , pp. 281-287
    • Yu, H.1    Fukami, K.2    Watanabe, Y.3    Ozaki, C.4    Takenawa, T.5
  • 78
    • 0032554623 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase in rat liver nuclei
    • Lu, P. J. et al. Phosphoinositide 3-kinase in rat liver nuclei. Biochemistry 37, 5738-5745 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5738-5745
    • Lu, P.J.1
  • 79
    • 0033600855 scopus 로고    scopus 로고
    • Agonists cause nuclear translocation of phosphatidylinositol 3-kinase-γ. A G β/γ-dependent pathway that requires the p110γ amino terminus
    • Metjian, A., Roll, R. L., Ma, A. D. & Abrams, C. S. Agonists cause nuclear translocation of phosphatidylinositol 3-kinase-γ. A G β/γ-dependent pathway that requires the p110γ amino terminus. J. Biol. Chem. 274, 27943-27947 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27943-27947
    • Metjian, A.1    Roll, R.L.2    Ma, A.D.3    Abrams, C.S.4
  • 80
    • 0035933834 scopus 로고    scopus 로고
    • Characterization of a G protein-activated phosphoinositide 3-kinase in vascular smooth muscle cell nuclei
    • Bacqueville, D. et al. Characterization of a G protein- activated phosphoinositide 3-kinase in vascular smooth muscle cell nuclei. J. Biol. Chem. 276, 22170-22176 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 22170-22176
    • Bacqueville, D.1
  • 81
    • 0034652102 scopus 로고    scopus 로고
    • A role for nuclear PTEN in neuronal differentiation
    • Lachyankar, M. B. et al. A role for nuclear PTEN in neuronal differentiation. J. Neurosci. 20, 1404-1413 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 1404-1413
    • Lachyankar, M.B.1
  • 82
    • 0033843623 scopus 로고    scopus 로고
    • Differential nuclear and cytoplasmic expression of PTEN in normal thyroid tissue, and benign and malignant epithelial thyroid tumors
    • Gimm, O. et al. Differential nuclear and cytoplasmic expression of PTEN in normal thyroid tissue, and benign and malignant epithelial thyroid tumors. Am. J. Pathol. 156, 1693-1700 (2000).
    • (2000) Am. J. Pathol. , vol.156 , pp. 1693-1700
    • Gimm, O.1
  • 83
    • 0033637979 scopus 로고    scopus 로고
    • PIKE. A nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4.1N
    • Ye, K. et al. PIKE. A nuclear GTPase that enhances PI3kinase activity and is regulated by protein 4. 1N. Cell 103, 919-930 (2000).
    • (2000) Cell , vol.103 , pp. 919-930
    • Ye, K.1
  • 84
    • 0346629933 scopus 로고    scopus 로고
    • Src homology domains of phospholipase C-γ1 inhibit nerve growth factor-induced differentiation of PC12 cells
    • Bae, S. S. et al. Src homology domains of phospholipase C-γ1 inhibit nerve growth factor-induced differentiation of PC12 cells. J. Neurochem. 71, 178-185 (1998).
    • (1998) J. Neurochem. , vol.71 , pp. 178-185
    • Bae, S.S.1
  • 85
    • 0035930577 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase c2α contains a nuclear localization sequence and associates with nuclear speckles
    • Didichenko, S. A. & Thelen, M. Phosphatidylinositol 3-kinase c2α contains a nuclear localization sequence and associates with nuclear speckles. J. Biol. Chem. 276, 48135-48142 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48135-48142
    • Didichenko, S.A.1    Thelen, M.2
  • 86
    • 0035947645 scopus 로고    scopus 로고
    • Presence and activation of nuclear phosphoinositide 3-kinase C2β during compensatory liver growth
    • Sindic, A., Aleksandrova, A., Fields, A. P., Volinia, S. & Banfic, H. Presence and activation of nuclear phosphoinositide 3-kinase C2β during compensatory liver growth. J. Biol. Chem. 276, 17754-17761 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 17754-17761
    • Sindic, A.1    Aleksandrova, A.2    Fields, A.P.3    Volinia, S.4    Banfic, H.5
  • 87
    • 0037048652 scopus 로고    scopus 로고
    • The activation of nuclear phosphoinositide 3-kinase C2β in all-trans-retinoic acid-differentiated HL-60 cells
    • Visnjic, D. et al. The activation of nuclear phosphoinositide 3-kinase C2β in all-trans-retinoic acid-differentiated HL-60 cells. FEBS Lett. 529, 268 (2002).
    • (2002) FEBS Lett. , vol.529 , pp. 268
    • Visnjic, D.1
  • 89
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • Gillooly, D. J. et al. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19, 4577-4588 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4577-4588
    • Gillooly, D.J.1
  • 90
    • 0033785054 scopus 로고    scopus 로고
    • Association of phosphatidylinositol 3-kinase with nuclear transcription sites in higher plants
    • Bunney, T. D. et al. Association of phosphatidylinositol 3-kinase with nuclear transcription sites in higher plants. Plant Cell 12, 1679-1688 (2000).
    • (2000) Plant Cell , vol.12 , pp. 1679-1688
    • Bunney, T.D.1
  • 91
    • 0033548232 scopus 로고    scopus 로고
    • Evidence that a phosphatidylinositol 3,4,5-trisphosphate-binding protein can function in nucleus
    • Tanaka, K. et al. Evidence that a phosphatidylinositol 3,4,5-trisphosphate-binding protein can function in nucleus. J. Biol. Chem. 274, 3919-3922 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3919-3922
    • Tanaka, K.1
  • 92
    • 0037057801 scopus 로고    scopus 로고
    • The nuclear phosphoinositide 3-kinase/AKT pathway: A new second messenger system
    • Neri, L. M., Borgatti, P., Capitani, S. & Martelli, A. M. The nuclear phosphoinositide 3-kinase/AKT pathway: a new second messenger system. Biochim. Biophys. Acta 1584, 73 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1584 , pp. 73
    • Neri, L.M.1    Borgatti, P.2    Capitani, S.3    Martelli, A.M.4
  • 93
    • 0029020361 scopus 로고
    • Translocation of the 85-kDa phospholipase A2 from cytosol to the nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen
    • Glover, S. et al. Translocation of the 85-kDa phospholipase A2 from cytosol to the nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen. J. Biol. Chem. 270, 15359-15367 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 15359-15367
    • Glover, S.1
  • 94
    • 0029587744 scopus 로고
    • Calcium-mediated translocation of cytosolic phospholipase A2 to the nuclear envelope and endoplasmic reticulum
    • Schievella, A. R., Regier, M. K., Smith, W. L. & Lin, L. L. Calcium-mediated translocation of cytosolic phospholipase A2 to the nuclear envelope and endoplasmic reticulum. J. Biol. Chem. 270, 30749-30754 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 30749-30754
    • Schievella, A.R.1    Regier, M.K.2    Smith, W.L.3    Lin, L.L.4
  • 95
    • 0029767977 scopus 로고    scopus 로고
    • Translocation of cytosolic phospholipase A2 to the nuclear envelope elicits topographically localized phospholipid hydrolysis
    • Peters-Golden, M., Song, K., Marshall, T. & Brock, T. Translocation of cytosolic phospholipase A2 to the nuclear envelope elicits topographically localized phospholipid hydrolysis. Biochem. J. 318, 797-803 (1996).
    • (1996) Biochem. J. , vol.318 , pp. 797-803
    • Peters-Golden, M.1    Song, K.2    Marshall, T.3    Brock, T.4
  • 96
    • 13044263122 scopus 로고    scopus 로고
    • Nuclear localization of prostaglandin E2 receptors
    • Bhattacharya, M. et al. Nuclear localization of prostaglandin E2 receptors. Proc. Natl. Acad. Sci. USA 95, 15792-15797 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15792-15797
    • Bhattacharya, M.1
  • 99
    • 0035860822 scopus 로고    scopus 로고
    • Co-localization of leukotriene A4 hydrolase with 5-lipoxygenase in nuclei of alveolar macrophages and rat basophilic leukemia cells but not neutrophils
    • Brock, T. G., Maydanski, E., McNish, R. W. & Peters- Golden, M. Co-localization of leukotriene A4 hydrolase with 5-lipoxygenase in nuclei of alveolar macrophages and rat basophilic leukemia cells but not neutrophils. J. Biol. Chem. 276, 35071-35077 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35071-35077
    • Brock, T.G.1    Maydanski, E.2    McNish, R.W.3    Peters-Golden, M.4
  • 100
    • 0035976575 scopus 로고    scopus 로고
    • Prostaglandins and leukotrienes: Advances in eicosanoid biology
    • Funk, C. D. Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 294, 1871-1875 (2001).
    • (2001) Science , vol.294 , pp. 1871-1875
    • Funk, C.D.1
  • 101
    • 0037422595 scopus 로고    scopus 로고
    • Identification of an intracellular receptor for lysophosphatidic acid (LPA): LPA is a transcellular PPARγ agonist
    • McIntyre, T. M. et al. Identification of an intracellular receptor for lysophosphatidic acid (LPA): LPA is a transcellular PPARγ agonist. Proc. Natl. Acad. Sci. USA 100, 131-136 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 131-136
    • McIntyre, T.M.1
  • 102
    • 0028179969 scopus 로고
    • α-thrombin-induced nuclear sn-1,2-diacylglycerols are derived from phosphatidylcholine hydrolysis in cultured fibroblasts
    • Jarpe, M. B., Leach, K. L. & Raben, D. M. α-thrombin-induced nuclear sn-1,2-diacylglycerols are derived from phosphatidylcholine hydrolysis in cultured fibroblasts. Biochemistry 33, 526-534 (1994).
    • (1994) Biochemistry , vol.33 , pp. 526-534
    • Jarpe, M.B.1    Leach, K.L.2    Raben, D.M.3
  • 103
    • 0032496141 scopus 로고    scopus 로고
    • Phosphatidylglycerol is a physiologic activator of nuclear protein kinase C
    • Murray, N. R. & Fields, A. P. Phosphatidylglycerol is a physiologic activator of nuclear protein kinase C. J. Biol. Chem. 273, 11514-11520 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 11514-11520
    • Murray, N.R.1    Fields, A.P.2
  • 104
    • 0032493823 scopus 로고    scopus 로고
    • Mapping of a molecular determinant for protein kinase C βII isozyme function
    • Gokmen-Polar, Y. & Fields, A. P. Mapping of a molecular determinant for protein kinase C βII isozyme function. J. Biol. Chem. 273, 20261-20266 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 20261-20266
    • Gokmen-Polar, Y.1    Fields, A.P.2
  • 107
    • 0034759191 scopus 로고    scopus 로고
    • Nuclear localization of neutral sphingomyelinase 1: Biochemical and immunocytochemical analyses
    • Mizutani, Y. et al. Nuclear localization of neutral sphingomyelinase 1: biochemical and immunocytochemical analyses. J. Cell Sci. 114, 3727-3736 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3727-3736
    • Mizutani, Y.1
  • 108
    • 0032996374 scopus 로고    scopus 로고
    • A possible role of nuclear ceramide and sphingosine in hepatocyte apoptosis in rat liver
    • Tsugane, K., Tamiya-Koizumi, K., Nagino, M., Nimura, Y. & Yoshida, S. A possible role of nuclear ceramide and sphingosine in hepatocyte apoptosis in rat liver. J. Hepatol. 31, 8-17 (1999).
    • (1999) J. Hepatol. , vol.31 , pp. 8-17
    • Tsugane, K.1    Tamiya-Koizumi, K.2    Nagino, M.3    Nimura, Y.4    Yoshida, S.5
  • 109
    • 0027933154 scopus 로고
    • Sphingosine inhibits the synthesis of RNA primers by primase in vitro
    • Simbulan, C. M. et al. Sphingosine inhibits the synthesis of RNA primers by primase in vitro. Biochemistry 33, 9007-9012 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9007-9012
    • Simbulan, C.M.1
  • 110
    • 0030601310 scopus 로고    scopus 로고
    • Fluorescently labeled phosphatidylinositol transfer protein isoforms (α and β), microinjected into fetal bovine heart endothelial cells, are targeted to distinct intracellular sites
    • De Vries, K. J. et al. Fluorescently labeled phosphatidylinositol transfer protein isoforms (α and β), microinjected into fetal bovine heart endothelial cells, are targeted to distinct intracellular sites. Exp. Cell Res. 227, 33-39 (1996).
    • (1996) Exp. Cell Res. , vol.227 , pp. 33-39
    • De Vries, K.J.1
  • 111
    • 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. et al. 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, 302-305 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 302-305
    • Rubbini, S.1
  • 112
    • 0025731596 scopus 로고
    • Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils
    • Stephens, L. R., Hughes, K. T. & Irvine, R. F. Pathway of phosphatidylinositol(3,4,5)-trisphosphate synthesis in activated neutrophils. Nature 351, 33-39 (1991).
    • (1991) Nature , vol.351 , pp. 33-39
    • Stephens, L.R.1    Hughes, K.T.2    Irvine, R.F.3
  • 113
    • 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, 192-196 (1997).
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 114
    • 0037033079 scopus 로고    scopus 로고
    • Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells
    • Sbrissa, D., Ikonomov, O. C., Deeb, R. & Shisheva, A. Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells. J. Biol. Chem. 277, 47276-47284 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47276-47284
    • Sbrissa, D.1    Ikonomov, O.C.2    Deeb, R.3    Shisheva, A.4
  • 115
    • 0034654363 scopus 로고    scopus 로고
    • Nuclear targeting of the β isoform of Type II phosphatidylinositol phosphate kinase (phosphatidylinositol 5-phosphate 4-kinase) by its α-helix 7
    • Ciruela, A., Hinchliffe, K. A., Divecha, N. & Irvine, R. F. Nuclear targeting of the β isoform of Type II phosphatidylinositol phosphate kinase (phosphatidylinositol 5-phosphate 4-kinase) by its α-helix 7. Biochem. J. 346, 587-591 (2000).
    • (2000) Biochem. J. , vol.346 , pp. 587-591
    • Ciruela, A.1    Hinchliffe, K.A.2    Divecha, N.3    Irvine, R.F.4
  • 116
    • 0035425190 scopus 로고    scopus 로고
    • Inositol lipids are regulated during cell cycle progression in the nuclei of murine erythroleukaemia cells
    • Clarke, J. H. et al. Inositol lipids are regulated during cell cycle progression in the nuclei of murine erythroleukaemia cells. Biochem. J. 357, 905-910 (2001).
    • (2001) Biochem. J. , vol.357 , pp. 905-910
    • Clarke, J.H.1
  • 117
    • 0037089091 scopus 로고    scopus 로고
    • Nuclear localization of phosphatidylinositol 4-kinase-β
    • de Graaf, P. et al. Nuclear localization of phosphatidylinositol 4-kinase-β. J. Cell Sci. 115, 1769-1775 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 1769-1775
    • De Graaf, P.1
  • 118
    • 0031968293 scopus 로고    scopus 로고
    • Mechanisms controlling gene expression by nuclear calcium signals
    • Hardingham, G. E., Cruzalegui, F. H., Chawla, S. & Bading, H. Mechanisms controlling gene expression by nuclear calcium signals. Cell Calcium 23, 131-134 (1998).
    • (1998) Cell Calcium , vol.23 , pp. 131-134
    • Hardingham, G.E.1    Cruzalegui, F.H.2    Chawla, S.3    Bading, H.4
  • 119
    • 0032498269 scopus 로고    scopus 로고
    • "Tell me where is calcium bred?": Clarifying the roles of nuclear calcium
    • Malviya, A. N. & Rogue, P. J. "Tell me where is calcium bred?": clarifying the roles of nuclear calcium. Cell 92, 17-23 (1998).
    • (1998) Cell , vol.92 , pp. 17-23
    • Malviya, A.N.1    Rogue, P.J.2
  • 122
    • 17544381440 scopus 로고    scopus 로고
    • 2+ transport through IP(3)Rs and RyRs in osteoblasts
    • 2+ transport through IP(3)Rs and RyRs in osteoblasts. Am. J. Physiol. Renal Physiol. 278, 784-791 (2000)
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278 , pp. 784-791
    • Adebanjo, O.A.1
  • 124
    • 0030860031 scopus 로고    scopus 로고
    • 2+ transients and meiosis resumption in starfish oocytes are mimicked by the nuclear injection of inositol 1,4,5-trisphosphate and cADP-ribose
    • 2+ transients and meiosis resumption in starfish oocytes are mimicked by the nuclear injection of inositol 1,4,5-trisphosphate and cADP-ribose. Cell Calcium 22, 11-20 (1997).
    • (1997) Cell Calcium , vol.22 , pp. 11-20
    • Santella, L.1    Kyozuka, K.2
  • 125
  • 126
    • 0030006597 scopus 로고    scopus 로고
    • Spatiotemporal analysis of calcium dynamics in the nucleus of hamster oocytes
    • Shirakawa, H. & Miyazaki, S. Spatiotemporal analysis of calcium dynamics in the nucleus of hamster oocytes. J. Physiol. 494, 29-40 (1996).
    • (1996) J. Physiol. , vol.494 , pp. 29-40
    • Shirakawa, H.1    Miyazaki, S.2
  • 127
    • 0030702896 scopus 로고    scopus 로고
    • Nuclear calcium signalling by individual cytoplasmic calcium puffs
    • Lipp, P., Thomas, D., Berridge, M. J. & Bootman, M. D. Nuclear calcium signalling by individual cytoplasmic calcium puffs. EMBO J. 16, 7166-7173 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7166-7173
    • Lipp, P.1    Thomas, D.2    Berridge, M.J.3    Bootman, M.D.4
  • 128
    • 0032514484 scopus 로고    scopus 로고
    • Protein kinase C regulates the nuclear localization of diacylglycerol kinase-ζ
    • Topham, M. K. et al. Protein kinase C regulates the nuclear localization of diacylglycerol kinase-ζ. Nature 394, 697-700 (1998). This paper describes an interesting regulation of the nuclear localization of a DAG kinase (the ζ-isoform), which attenuates a DAG signal by phosphorylating it to phosphatidic acid. DAG kinase-ζ is phosphorylated by PKC, and this leads to its exclusion from the nucleus.
    • (1998) Nature , vol.394 , pp. 697-700
    • Topham, M.K.1
  • 129
    • 0034652722 scopus 로고    scopus 로고
    • Enhanced nuclear diacylglycerol kinase activity in response to a mitogenic stimulation of quiescent Swiss 3T3 cells with insulin-like growth factor I
    • Martelli, A. M. et al. Enhanced nuclear diacylglycerol kinase activity in response to a mitogenic stimulation of quiescent Swiss 3T3 cells with insulin-like growth factor I. Cancer Res. 80, 815-821 (2000).
    • (2000) Cancer Res. , vol.80 , pp. 815-821
    • Martelli, A.M.1
  • 130
    • 0030576989 scopus 로고    scopus 로고
    • Translocation of diacylglycerol kinase-α to the nuclear matrix of rat thymocytes and peripheral T-lymphocytes
    • Wada, I., Kai, M., Imai, S., Sakane, F. & Kanoh, H. Translocation of diacylglycerol kinase-α to the nuclear matrix of rat thymocytes and peripheral T-lymphocytes. FEBS Lett. 393, 48-52 (1996).
    • (1996) FEBS Lett. , vol.393 , pp. 48-52
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 131
    • 0035968159 scopus 로고    scopus 로고
    • Nuclear diacylglycerol kinase-θ is activated in response to α-thrombin
    • Bregoli, L., Baldassare, J. J. & Raben, D. M. Nuclear diacylglycerol kinase-θ is activated in response to α-thrombin. J. Biol. Chem. 276, 23288-23295 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23288-23295
    • Bregoli, L.1    Baldassare, J.J.2    Raben, D.M.3
  • 132
    • 0036634368 scopus 로고    scopus 로고
    • Diacylglycerol kinases in nuclear lipid-dependent signal transduction pathways
    • Martelli, A. M. et al. Diacylglycerol kinases in nuclear lipid-dependent signal transduction pathways. Cell Mol. Life Sci. 59, 1129-1137 (2002).
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1129-1137
    • Martelli, A.M.1
  • 135
    • 0035916811 scopus 로고    scopus 로고
    • A novel pathway of cellular phosphatidylinositol(3,4,5)-trisphosphate synthesis is regulated by oxidative stress
    • Halstead, J. R. et al. A novel pathway of cellular phosphatidylinositol(3,4,5)-trisphosphate synthesis is regulated by oxidative stress. Curr. Biol. 11, 386-395 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 386-395
    • Halstead, J.R.1


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