메뉴 건너뛰기




Volumn 1761, Issue 5-6, 2006, Pages 505-508

Nuclear inositide signalling-expansion, structures and clarification

Author keywords

Inositol; Inositol hexakisphosphate; Inositol lipids; Nuclear envelope; Nucleus; Phosphatidylinositol 4,5 bisphosphate

Indexed keywords

CALCIUM; DNA; LIPID; MAGNESIUM; PHOSPHATIDYLINOSITOL; PHYTIC ACID; RNA;

EID: 33745228758     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.02.008     Document Type: Review
Times cited : (54)

References (27)
  • 1
    • 0023657043 scopus 로고
    • Synthesis of polyphosphoinositides in nuclei of Friend cells. Evidence for polyphosphoinositide metabolism inside the nucleus which changes with cell differentiation
    • Cocco L., Gilmour R.S., Ognibene A., Letcher A.J., Manzoli F.A., and Irvine R.F. Synthesis of polyphosphoinositides in nuclei of Friend cells. Evidence for polyphosphoinositide metabolism inside the nucleus which changes with cell differentiation. Biochem. J. 248 (1987) 765-770
    • (1987) Biochem. J. , vol.248 , pp. 765-770
    • Cocco, L.1    Gilmour, R.S.2    Ognibene, A.3    Letcher, A.J.4    Manzoli, F.A.5    Irvine, R.F.6
  • 3
    • 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
  • 4
    • 0035975965 scopus 로고    scopus 로고
    • Modular phosphoinositide-binding domains-their role in signalling and membrane trafficking
    • Cullen P.J., Cozier G.E., Banting G., and Mellor H. Modular phosphoinositide-binding domains-their role in signalling and membrane trafficking. Curr. Biol. 11 (2001) R882-R893
    • (2001) Curr. Biol. , vol.11
    • Cullen, P.J.1    Cozier, G.E.2    Banting, G.3    Mellor, H.4
  • 5
    • 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., and Postle A.D. Highly saturated endonuclear phosphatidylcholine is synthesized in situ and colocated with CDP-choline pathway enzymes. J. Biol. Chem. 276 (2001) 8492-8499
    • (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
  • 7
    • 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., and Vaux D. Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope. J. Cell Biol. 136 (1997) 531-544
    • (1997) J. Cell Biol. , vol.136 , pp. 531-544
    • Fricker, M.1    Hollinshead, M.2    White, N.3    Vaux, D.4
  • 8
    • 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
  • 9
    • 0036566427 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C δ1
    • Watt S.A., Kular G., Fleming I.N., Downes C.P., and Lucocq J.M. Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C δ1. 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
  • 10
    • 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
  • 11
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: a model for nuclear organelles
    • Lamond A.I., and Spector D.L. Nuclear speckles: a model for nuclear organelles. Nat. Rev., Mol. Cell Biol. 4 (2003) 605-612
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 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 (1997) 569-576
    • (1997) Biochem. J. , vol.327 , pp. 569-576
    • Vann, L.R.1    Wooding, F.B.2    Irvine, R.F.3    Divecha, N.4
  • 14
    • 0033594398 scopus 로고    scopus 로고
    • Nuclei contain two differentially regulated pools of diacylglycerol
    • D'Santos C.S., Clarke J.H., Irvine R.F., and Divecha N. Nuclei contain two differentially regulated pools of diacylglycerol. Curr. Biol. 9 (1999) 437-440
    • (1999) Curr. Biol. , vol.9 , pp. 437-440
    • D'Santos, C.S.1    Clarke, J.H.2    Irvine, R.F.3    Divecha, N.4
  • 15
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S., and Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438 (2005) 605-611
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 16
    • 3342882581 scopus 로고    scopus 로고
    • Presence of different phospholipase C isoforms in the nucleus and their activation during compensatory liver growth
    • Crljen V., Visnjic D., and Banfic H. Presence of different phospholipase C isoforms in the nucleus and their activation during compensatory liver growth. FEBS Lett. 571 (2004) 35-42
    • (2004) FEBS Lett. , vol.571 , pp. 35-42
    • Crljen, V.1    Visnjic, D.2    Banfic, H.3
  • 17
    • 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
  • 18
    • 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
  • 19
    • 20444497331 scopus 로고    scopus 로고
    • Nuclear translocation of phospholipase C-delta1 is linked to the cell cycle and nuclear phosphatidylinositol 4,5-bisphosphate
    • Stallings J.D., Tall E.G., Pentyala S., and Rebecchi M.J. Nuclear translocation of phospholipase C-delta1 is linked to the cell cycle and nuclear phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 280 (2005) 22060-22069
    • (2005) J. Biol. Chem. , vol.280 , pp. 22060-22069
    • Stallings, J.D.1    Tall, E.G.2    Pentyala, S.3    Rebecchi, M.J.4
  • 20
    • 0035347166 scopus 로고    scopus 로고
    • Back in the water: the return of the inositol phosphates
    • Irvine R.F., and Schell M.J. Back in the water: the return of the inositol phosphates. Nat. Rev., Mol. Cell Biol. 2 (2001) 327-338
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 327-338
    • Irvine, R.F.1    Schell, M.J.2
  • 21
    • 22744443710 scopus 로고    scopus 로고
    • Inositide evolution-Towards turtle domination?
    • Irvine R.F. Inositide evolution-Towards turtle domination?. J. Physiol. 566 (2005) 295-300
    • (2005) J. Physiol. , vol.566 , pp. 295-300
    • Irvine, R.F.1
  • 23
    • 20844440571 scopus 로고    scopus 로고
    • Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2-kinase gene, associated lethality, and tissue distribution of 2-kinase expression
    • Verbsky J., Lavine K., and Majerus P.W. Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2-kinase gene, associated lethality, and tissue distribution of 2-kinase expression. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8448-8453
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8448-8453
    • Verbsky, J.1    Lavine, K.2    Majerus, P.W.3
  • 24
    • 2442637866 scopus 로고    scopus 로고
    • Visualization of inositol phosphate-dependent mobility of Ku: depletion of the DNA-PK cofactor InsP6 inhibits Ku mobility
    • Byrum J., Jordan S., Safrany S.T., and Rodgers W. Visualization of inositol phosphate-dependent mobility of Ku: depletion of the DNA-PK cofactor InsP6 inhibits Ku mobility. Nucleic Acids Res. 32 (2004) 2776-2784
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2776-2784
    • Byrum, J.1    Jordan, S.2    Safrany, S.T.3    Rodgers, W.4
  • 25
    • 24644519954 scopus 로고    scopus 로고
    • Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
    • Macbeth M.R., Schubert H.L., Vandemark A.P., Lingam A.T., Hill C.P., and Bass B.L. Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science 309 (2005) 1534-1539
    • (2005) Science , vol.309 , pp. 1534-1539
    • Macbeth, M.R.1    Schubert, H.L.2    Vandemark, A.P.3    Lingam, A.T.4    Hill, C.P.5    Bass, B.L.6
  • 26
    • 0035087311 scopus 로고    scopus 로고
    • Assessing the functional omnipotence of inositol hexakisphophosphate
    • Shears S.B. Assessing the functional omnipotence of inositol hexakisphophosphate. Cell. Signal. 13 (2001) 151-158
    • (2001) Cell. Signal. , vol.13 , pp. 151-158
    • Shears, S.B.1
  • 27
    • 13844256151 scopus 로고    scopus 로고
    • Solution behaviour of myo-inositol hexakisphosphate in the presence of multivalent cations. Prediction of a neutral pentamagnesium species under cytosolic/nuclear conditions
    • Torres J., Dominguez S., Cerda M.F., Obal G., Mederos A., Irvine R.F., Diaz A., and Kremer C. Solution behaviour of myo-inositol hexakisphosphate in the presence of multivalent cations. Prediction of a neutral pentamagnesium species under cytosolic/nuclear conditions. J. Inorg. Biochem. 99 (2005) 828-840
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 828-840
    • Torres, J.1    Dominguez, S.2    Cerda, M.F.3    Obal, G.4    Mederos, A.5    Irvine, R.F.6    Diaz, A.7    Kremer, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.