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Volumn 189, Issue , 1999, Pages 95-130

Phosphoinositide kinases and the synthesis of polyphosphoinositides in higher plant cells

Author keywords

Biosynthesis; Cell signaling; Inositol; Kinases; Phosphatidylinositol; Phosphatidylinositol transfer proteins; Phospholipids; Plants

Indexed keywords

CARRIER PROTEIN; INOSITOL; LIPID; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL KINASE; PHOSPHOLIPID;

EID: 0032923204     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0074-7696(08)61386-8     Document Type: Review
Times cited : (48)

References (117)
  • 1
    • 0030802292 scopus 로고    scopus 로고
    • Isolation and molecular cloning of wortmannin-sensitive bovine type II phosphatidylinositol 4-kinases
    • Balla, T., Downing, G. J., Jaffe, H., Kim, S., Zolyomi, A., and Galt, K. J. (1997). Isolation and molecular cloning of wortmannin-sensitive bovine type II phosphatidylinositol 4-kinases. J. Biol. Chem. 272, 18358-18366.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18358-18366
    • Balla, T.1    Downing, G.J.2    Jaffe, H.3    Kim, S.4    Zolyomi, A.5    Galt, K.J.6
  • 2
    • 0019887530 scopus 로고
    • Topology of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles
    • Ballas, L., and Bell, R. M. (1981). Topology of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles. Biochem. Biophys. Acta 665,586-595.
    • (1981) Biochem. Biophys. Acta , vol.665 , pp. 586-595
    • Ballas, L.1    Bell, R.M.2
  • 4
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer in yeast Golgi function
    • Bankaitis, V. A., Aitken, J. R., Cleves, A. E., and Dowhan, W. (1990). An essential role for a phospholipid transfer in yeast Golgi function. Nature 347, 561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 5
    • 0028008266 scopus 로고
    • Plasma membrane lipid metabolism of petunia petals during senescence
    • Borochov, A., Cho, M. H., and Boss, W. F. (1994). Plasma membrane lipid metabolism of petunia petals during senescence. Physiol. Plant. 90, 279-284.
    • (1994) Physiol. Plant. , vol.90 , pp. 279-284
    • Borochov, A.1    Cho, M.H.2    Boss, W.F.3
  • 6
    • 0028812255 scopus 로고
    • The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases
    • Boronenkov, I. V., and Andersen, R. A. (1995). The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases. J. Biol. Cliem. 270, 2881-2884.
    • (1995) J. Biol. Cliem. , vol.270 , pp. 2881-2884
    • Boronenkov, I.V.1    Andersen, R.A.2
  • 7
    • 0022426950 scopus 로고
    • Polyphosphoinositides are present in plant tissue culture cells
    • Boss, W. F., and Massel, M. O. (1985). Polyphosphoinositides are present in plant tissue culture cells. Biochem. Biophys. Res. Commun. 132, 1018-1023.
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , pp. 1018-1023
    • Boss, W.F.1    Massel, M.O.2
  • 8
    • 0027478728 scopus 로고
    • The pathway of synthesis of 3,4- And 4,5-phosphory- lated phosphatidylinositols in the duckweed Spirodela polyrhiza L
    • Brearley, C. A., and Hanke, D. E. (1993). The pathway of synthesis of 3,4- and 4,5-phosphory- lated phosphatidylinositols in the duckweed Spirodela polyrhiza L. Biochem. J. 290,145-150.
    • (1993) Biochem. J. , vol.290 , pp. 145-150
    • Brearley, C.A.1    Hanke, D.E.2
  • 10
    • 0025611910 scopus 로고
    • Phosphoinositide kinases
    • Carpenter, C. L., and Cantley, L. C. (1990). Phosphoinositide kinases. Biochemistry 29,11147-11156.
    • (1990) Biochemistry , vol.29 , pp. 11147-11156
    • Carpenter, C.L.1    Cantley, L.C.2
  • 12
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., Traynor-Kaplan, A., Bokoch, G. M., and Schwartz, M. A. (1994). The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79, 507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 14
    • 0029328477 scopus 로고
    • Phosphatidylinositol transfer protein dictates the rate of inositol trisphosphate production by promoting the synthesis of PIP2
    • Cunningham, E., Thomas, G. M. H., Ball, A., Hues, I., and Cockcroft, S. (1995). Phosphatidylinositol transfer protein dictates the rate of inositol trisphosphate production by promoting the synthesis of PIP2. Curr. Biol. 5, 775-783.
    • (1995) Curr. Biol. , vol.5 , pp. 775-783
    • Cunningham, E.1    Thomas, G.M.H.2    Ball, A.3    Hues, I.4    Cockcroft, S.5
  • 15
    • 4244183502 scopus 로고    scopus 로고
    • The yeast and mammalian isoforms of phosphatidylinositol transfer protein can restore phospholipase C-mediated inositol lipid signaling in cytosol-depleted RBL-2H3 and HL60 cells
    • Cunningham, E., Khoon Tan, S., Swigart, P., Hsuan, J., Bankaitis, V., and Cockcroft, S. (1996). The yeast and mammalian isoforms of phosphatidylinositol transfer protein can restore phospholipase C-mediated inositol lipid signaling in cytosol-depleted RBL-2H3 and HL60 cells. Proc. Natl. Acad. Sei. USA 93, 6589-6593.
    • (1996) Proc. Natl. Acad. Sei. USA , vol.93 , pp. 6589-6593
    • Cunningham, E.1    Khoon Tan, S.2    Swigart, P.3    Hsuan, J.4    Bankaitis, V.5    Cockcroft, S.6
  • 16
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli, P., Emr, S. D., McPherson, P. S., and Novick, P. (1996). Phosphoinositides as regulators in membrane traffic. Science 271, 1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 17
    • 0031037109 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphos-phate specifically stimulates pp60c-src catalyzed phosphorylation of gelsolin and related actin-binding proteins
    • De Corte, V., Gettemans, J., and Vanderkerckhove, J. (1997). Phosphatidylinositol 4,5-bisphos-phate specifically stimulates pp60c-src catalyzed phosphorylation of gelsolin and related actin-binding proteins. FEBS Lett. 401, 191-196.
    • (1997) FEBS Lett. , vol.401 , pp. 191-196
    • De Corte, V.1    Gettemans, J.2    Vanderkerckhove, J.3
  • 18
    • 0030790548 scopus 로고    scopus 로고
    • Using structure to define the function of phosphoinosi-tide 3-kinase family members
    • Domin, J., and Waterfield, M. D. (1997). Using structure to define the function of phosphoinosi-tide 3-kinase family members. FEBS Lett. 410, 91-95.
    • (1997) FEBS Lett. , vol.410 , pp. 91-95
    • Domin, J.1    Waterfield, M.D.2
  • 19
    • 0028090666 scopus 로고
    • Identification of a phosphatidylinositol 3-hydroxy kinase in plant cells: Association with the cytoskeleton
    • Dove, S. K., Lloyd, C. W., and Drøbak, B. K. (1994). Identification of a phosphatidylinositol 3-hydroxy kinase in plant cells: Association with the cytoskeleton. Biochem. J. 303,347-350.
    • (1994) Biochem. J. , vol.303 , pp. 347-350
    • Dove, S.K.1    Lloyd, C.W.2    Drøbak, B.K.3
  • 20
    • 0030669546 scopus 로고    scopus 로고
    • Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis
    • Dove, S. K., Cooke, F. T., Douglas, M. R., Sayers, L. G., Parker, P. J., and Michell, R. H. (1997). Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis. Natitre 390, 187-192.
    • (1997) Natitre , vol.390 , pp. 187-192
    • Dove, S.K.1    Cooke, F.T.2    Douglas, M.R.3    Sayers, L.G.4    Parker, P.J.5    Michell, R.H.6
  • 21
    • 0027053814 scopus 로고
    • The plant phosphoinositide system
    • Drøbak, B. K. (1992). The plant phosphoinositide system. Biochem. J. 288, 697-712.
    • (1992) Biochem. J. , vol.288 , pp. 697-712
    • Drøbak, B.K.1
  • 22
    • 0342503287 scopus 로고    scopus 로고
    • Metabolism of plant phosphoinositides and other inositol-containing lipids
    • M. Smallwood, J. P. Knox, and D. J. Bowles, Eds., BIOS Scientific, Oxford, UK
    • Drøbak, B. K. (1996). Metabolism of plant phosphoinositides and other inositol-containing lipids. In "Membranes: Specialized Functions in Plants" (M. Smallwood, J. P. Knox, and D. J. Bowles, Eds.), pp. 195-214. BIOS Scientific, Oxford, UK.
    • (1996) Membranes: Specialized Functions in Plants , pp. 195-214
    • Drøbak, B.K.1
  • 24
    • 0028105664 scopus 로고
    • Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin
    • Drøbak, B. K., Watkins, P. A. C., Valenta, R., Dove, S. K., Lloyd, C. W., and Staiger, C. J. (1994). Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin. Plant J. 6, 389-400.
    • (1994) Plant J. , vol.6 , pp. 389-400
    • Drøbak, B.K.1    Watkins, P.A.C.2    Valenta, R.3    Dove, S.K.4    Lloyd, C.W.5    Staiger, C.J.6
  • 26
    • 0030948743 scopus 로고    scopus 로고
    • New developments in phospholipase D
    • Exton, J. H. (1997). New developments in phospholipase D. J. Biol. Chem. 272,15579-15582.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15579-15582
    • Exton, J.H.1
  • 27
    • 0030156660 scopus 로고    scopus 로고
    • ARF and PITP restore GTP-γS-stimulated protein secretion from cytosol-depleted HL60 cells by promoting PIP2 synthesis
    • Fensome, A., Cunningham, E., Presser, S., Khoon Tan, S., Swigert, P., Thomas, G., Hsuan, J., and Cockcroft, S. (1996). ARF and PITP restore GTP-γS-stimulated protein secretion from cytosol-depleted HL60 cells by promoting PIP2 synthesis. Curr. Biol. 6, 730-738.
    • (1996) Curr. Biol. , vol.6 , pp. 730-738
    • Fensome, A.1    Cunningham, E.2    Presser, S.3    Khoon Tan, S.4    Swigert, P.5    Thomas, G.6    Hsuan, J.7    Cockcroft, S.8
  • 28
    • 0027095980 scopus 로고
    • Purification and characterization of a soluble phospha-tidylinositol 4-kinase from the yeast Saccharomyces cerevisiae
    • Flanagan, C. A., and Thorner, J. (1992). Purification and characterization of a soluble phospha-tidylinositol 4-kinase from the yeast Saccharomyces cerevisiae. J. Dial. Chem. 267, 24117-24125.
    • (1992) J. Dial. Chem. , vol.267 , pp. 24117-24125
    • Flanagan, C.A.1    Thorner, J.2
  • 29
    • 0027768699 scopus 로고
    • Phosphatidylinositol 4-kinase: Gene structure and requirement for yeast cell viability
    • Flanagan, C. A., Schnieders, E. A., Emerick, A. W., Kunisawa, R., Admon, A., and Thorner, J. (1993). Phosphatidylinositol 4-kinase: Gene structure and requirement for yeast cell viability. Science 262, 1444-1448.
    • (1993) Science , vol.262 , pp. 1444-1448
    • Flanagan, C.A.1    Schnieders, E.A.2    Emerick, A.W.3    Kunisawa, R.4    Admon, A.5    Thorner, J.6
  • 30
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt protooncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., Yang, S. L, Chan, T. O., Datta, K., Kazlauskas, A., Morrison, D. K., Kaplan, D. R., and Tsichlis, P. N. (1995). The protein kinase encoded by the Akt protooncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81, 727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.L.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 31
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
    • Franke, T. F., Kaplan, D. R., Cantley, L. C., and Toker, A. (1997). Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate. Science 275, 665-668.
    • (1997) Science , vol.275 , pp. 665-668
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 32
    • 0030004820 scopus 로고    scopus 로고
    • Identification of a 200 kDa polypeptide as type-3 phosphatidylinositol 4-kinase from bovine brain by partial protein and cDNA sequencing
    • Gehrmann, T., Verqab, G., Schmidt, M., Klix, D., Meyer, H. E., Varsanyi, M., and Heilmeyer, L. M. G. (1996). Identification of a 200 kDa polypeptide as type-3 phosphatidylinositol 4-kinase from bovine brain by partial protein and cDNA sequencing. Biochiin. Biopliys. Acta Mol. Cell Res. 1311, 53-63.
    • (1996) Biochiin. Biopliys. Acta Mol. Cell Res. , vol.1311 , pp. 53-63
    • Gehrmann, T.1    Verqab, G.2    Schmidt, M.3    Klix, D.4    Meyer, H.E.5    Varsanyi, M.6    Heilmeyer, L.M.G.7
  • 33
    • 0025308055 scopus 로고
    • The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C
    • Goldschmidt-Clermont, P. J., Machesky, L. M., Baldassare, J. J., and Pollard, T. D. (1990). The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247, 1575-1578.
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1    Machesky, L.M.2    Baldassare, J.J.3    Pollard, T.D.4
  • 34
  • 35
    • 0011697626 scopus 로고
    • Inositol phospholipids and signal transduction
    • D.P.S. Verma, ed., Telford Press, Caldwell, NJ
    • Gross, W., and Boss, W. F. (1992). Inositol phospholipids and signal transduction. In "Control of Plant Gene Expression" (D.P.S. Verma, ed.), pp. 17-32. Telford Press, Caldwell, NJ.
    • (1992) Control of Plant Gene Expression , pp. 17-32
    • Gross, W.1    Boss, W.F.2
  • 36
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A., and Stossel, T. P. (1995). Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82, 643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 37
    • 0001877733 scopus 로고
    • Plant acyl lipids: Structure, distribution and analysis
    • P. K. Stumpf, ed., Academic Press, New York
    • Hanvood, J. L. (1980). Plant acyl lipids: Structure, distribution and analysis. In "The Biochemistry of Plants, Vol. 4" (P. K. Stumpf, ed.), pp. 1-55. Academic Press, New York.
    • (1980) The Biochemistry of Plants , vol.4 , pp. 1-55
    • Hanvood, J.L.1
  • 38
    • 0027765507 scopus 로고
    • Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca2l-activated secretion
    • Hay, J. C., and Martin, T. F. J. (1993). Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca2l-activated secretion. Nature 366, 572-575.
    • (1993) Nature , vol.366 , pp. 572-575
    • Hay, J.C.1    Martin, T.F.J.2
  • 40
    • 0002167846 scopus 로고
    • The polyphosphoinositides, phosphatidylinositol monophosphate and phosphatidylinositol bisphosphate are present in nuclei isolated from carrot protoplasts
    • Hendrix, K. W., Assefa, H., and Boss, W. F. (1989). The polyphosphoinositides, phosphatidylinositol monophosphate and phosphatidylinositol bisphosphate are present in nuclei isolated from carrot protoplasts. Protoplasma 151, 62-72.
    • (1989) Protoplasma , vol.151 , pp. 62-72
    • Hendrix, K.W.1    Assefa, H.2    Boss, W.F.3
  • 41
    • 0031038072 scopus 로고    scopus 로고
    • Multiple roles of MAP kinases in plant signal transduction
    • Hirt, H. (1997). Multiple roles of MAP kinases in plant signal transduction. Trends Plant Sei. 2, 11-15.
    • (1997) Trends Plant Sei. , vol.2 , pp. 11-15
    • Hirt, H.1
  • 42
    • 84960994832 scopus 로고
    • Enzyme secretion and the incorporation of 32P into phospholipids of pancreas slices
    • Hokin, M. R., and Hokin, L. E. (1953). Enzyme secretion and the incorporation of 32P into phospholipids of pancreas slices. J. Dial. Chem. 203, 967-977.
    • (1953) J. Dial. Chem. , vol.203 , pp. 967-977
    • Hokin, M.R.1    Hokin, L.E.2
  • 43
    • 0028169625 scopus 로고
    • A phosphatidylinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation
    • Hong, Z. G., and Verma, D. P. S. (1994). A phosphatidylinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation. Proc. Nal. Acad. Sei. USA 91, 9617-9621.
    • (1994) Proc. Nal. Acad. Sei. USA , vol.91 , pp. 9617-9621
    • Hong, Z.G.1    Verma, D.P.S.2
  • 44
    • 0000517382 scopus 로고
    • Phosphatidylinositol(4,5)bisphosphate and phosphatidylinositol(4)phosphate in plant tissues
    • Irvine, R. F., Letcher, A. J., Lander, D. J., Drobak, B. K., Dawson, A. P., and Musgrave, A. (1989). Phosphatidylinositol(4,5)bisphosphate and phosphatidylinositol(4)phosphate in plant tissues. Plant Pliysiol. 89, 888-892.
    • (1989) Plant Pliysiol. , vol.89 , pp. 888-892
    • Irvine, R.F.1    Letcher, A.J.2    Lander, D.J.3    Drobak, B.K.4    Dawson, A.P.5    Musgrave, A.6
  • 45
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P. A. (1994). Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Pliysiol. 56, 169-191.
    • (1994) Annu. Rev. Pliysiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 50
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon, M. A., Ferguson, K. M., and Schlessinger, J. (1996). PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85, 621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 51
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M., and Cantley, L. C. (1995). Signal transduction and membrane traffic: The PITP/phosphoinositide connection. Cell 81, 659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 52
    • 16944365378 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family
    • Loijens, J. C, and Anderson, R. A. (1996). Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family. J. Biol. Cliem. 271, 32937-32943.
    • (1996) J. Biol. Cliem. , vol.271 , pp. 32937-32943
    • Loijens, J.C.1    Anderson, R.A.2
  • 53
    • 0026513805 scopus 로고
    • Diacylglycerol kinase in plasma membranes from wheat
    • Lundberg, G. A., and Sommarin, M. (1992). Diacylglycerol kinase in plasma membranes from wheat. Biochein. Biopliys. Ada 1123, 177-183.
    • (1992) Biochein. Biopliys. Ada , vol.1123 , pp. 177-183
    • Lundberg, G.A.1    Sommarin, M.2
  • 54
    • 0031455170 scopus 로고    scopus 로고
    • The role of CDP-diacylglycerol synthase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content
    • Lykidis, A., Jackson, P. B., Rock, C. O., and Jackowski, S. (1997). The role of CDP-diacylglycerol synthase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content. J. Biol. Chem. 272, 33402-33409.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33402-33409
    • Lykidis, A.1    Jackson, P.B.2    Rock, C.O.3    Jackowski, S.4
  • 55
    • 85051530432 scopus 로고
    • Sphingolipids
    • T. S. Moore, ed., CRC Press, Boca Raton, FL
    • Lynch, D. V. (1993). Sphingolipids. In "Lipid Metabolism in Plants" (T. S. Moore, ed.), pp. 285-308. CRC Press, Boca Raton, FL.
    • (1993) Lipid Metabolism in Plants , pp. 285-308
    • Lynch, D.V.1
  • 56
    • 0000679931 scopus 로고
    • Plasma membrane lipid interactions associated with cold acclimation of winter rye seedlings (Secale cereale L. cv Puma)
    • Lynch, D. V., and Steponkus, P. L. (1987). Plasma membrane lipid interactions associated with cold acclimation of winter rye seedlings (Secale cereale L. cv Puma). Plant Physiol. S3, 761-767.
    • (1987) Plant Physiol. S , vol.3 , pp. 761-767
    • Lynch, D.V.1    Steponkus, P.L.2
  • 57
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of 2 vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka, K., Bassham, D. C, Raikhel, N. V., and Nakamura, K. (1995). Different sensitivity to wortmannin of 2 vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J. Cell Biol. 130, 1307-1318.
    • (1995) J. Cell Biol. , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Nakamura, K.4
  • 59
    • 0024971191 scopus 로고
    • Inositol phospholipids activate plasma membrane ATPase in plants
    • Memon, A. R., Chen, Q., and Boss, W. F. (1990). Inositol phospholipids activate plasma membrane ATPase in plants. Biochein. Biopliys. Res. Commun. 162, 1295-1301.
    • (1990) Biochein. Biopliys. Res. Commun. , vol.162 , pp. 1295-1301
    • Memon, A.R.1    Chen, Q.2    Boss, W.F.3
  • 60
    • 0016613531 scopus 로고
    • Inositol phospholipids and cell surface receptor function
    • Michell, R. H. (1975). Inositol phospholipids and cell surface receptor function. Biochein. Biophys. Ada 415, 81-147.
    • (1975) Biochein. Biophys. Ada , vol.415 , pp. 81-147
    • Michell, R.H.1
  • 61
    • 0028859163 scopus 로고
    • 2 genes that encode ribosomal-protein-S6 kinase homologs are induced by cold or salinity stress in Arabidopsis thaliana
    • Mizoguchi.T., Hayashida, N., Yamaguchishinozaki, K., Kamada, H., and Shinozaki, K. (1995). 2 genes that encode ribosomal-protein-S6 kinase homologs are induced by cold or salinity stress in Arabidopsis thaliana. FEBS Lett. 358, 199-204.
    • (1995) FEBS Lett. , vol.358 , pp. 199-204
    • MizoguchiT1    Hayashida, N.2    Yamaguchishinozaki, K.3    Kamada, H.4    Shinozaki, K.5
  • 62
    • 0031013737 scopus 로고    scopus 로고
    • Environmental stress response in plants: The role of mitogen-activated protein kinases
    • Mizoguchi, T., Ichimura, K., and Shinozaki, K. (1997). Environmental stress response in plants: The role of mitogen-activated protein kinases. Trends Biotechnol. 15, 15-19.
    • (1997) Trends Biotechnol. , vol.15 , pp. 15-19
    • Mizoguchi, T.1    Ichimura, K.2    Shinozaki, K.3
  • 63
    • 0026497197 scopus 로고
    • Subcellular organization of receptor-mediated phosphoinositide turnover
    • Monaco, M. E., and Gershengorn, M. C. (1992). Subcellular organization of receptor-mediated phosphoinositide turnover. Endocr. Rev. 13, 707-718.
    • (1992) Endocr. Rev. , vol.13 , pp. 707-718
    • Monaco, M.E.1    Gershengorn, M.C.2
  • 65
    • 0000641864 scopus 로고
    • Biosynthesis of phosphatidylinositol
    • D. J. Morre, W. F. Boss, and F. A. Loewus, eds., Wiley-Liss, New York
    • Moore, T. S., Jr. (1990). Biosynthesis of phosphatidylinositol. In "Inositol Metabolism in Plants" (D. J. Morre, W. F. Boss, and F. A. Loewus, eds.), pp. 107-112. Wiley-Liss, New York.
    • (1990) Inositol Metabolism in Plants , pp. 107-112
    • Moore Jr., T.S.1
  • 66
    • 0028219406 scopus 로고
    • Rapid turnover of phosphatidylinositol 3-phosphate in the green alga Chalmydomonas eugametos-Signs of a phosphatidylinositide 3-kinase signalling pathway in lower plants
    • Munnik, T., Irvine, R. F., and Musgrave, A. (1994a). Rapid turnover of phosphatidylinositol 3-phosphate in the green alga Chalmydomonas eugametos-Signs of a phosphatidylinositide 3-kinase signalling pathway in lower plants. Biochein. J. 298, 269-273.
    • (1994) Biochein. J. , vol.298 , pp. 269-273
    • Munnik, T.1    Irvine, R.F.2    Musgrave, A.3
  • 67
    • 0028155598 scopus 로고
    • Rapid turnover of polyphosphoinositides in carnation flower petals
    • Munnik, T., Musgrave, A., and Devrije, T. (1994b). Rapid turnover of polyphosphoinositides in carnation flower petals. Planta 193, 89-98.
    • (1994) Planta , vol.193 , pp. 89-98
    • Munnik, T.1    Musgrave, A.2    Devrije, T.3
  • 69
    • 0029892506 scopus 로고    scopus 로고
    • Cloning, expression, and localization of 230-kDa phosphatidylinositol 4-kinase
    • Nakagawa, T., Goto, K., and Kondo, H. (1996). Cloning, expression, and localization of 230-kDa phosphatidylinositol 4-kinase. J. Biol. Chem. 271,12088-12094.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12088-12094
    • Nakagawa, T.1    Goto, K.2    Kondo, H.3
  • 70
    • 0023214019 scopus 로고
    • Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cervisiae
    • Nikawa, J., Kodaki, T., and Yamashita, S. (1987). Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cervisiae. J. Biol. Chem. 262, 4876-4881.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4876-4881
    • Nikawa, J.1    Kodaki, T.2    Yamashita, S.3
  • 71
    • 0026451081 scopus 로고
    • Intracellular signalling by hydrolysis of phospholipids and the activation of protein kinase C
    • Nishizuka, Y. (1992). Intracellular signalling by hydrolysis of phospholipids and the activation of protein kinase C. Science 258, 607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 72
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., Field, C, and Schekman, R. (1980). Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21, 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 74
    • 0029163837 scopus 로고
    • Purification and characterization of a soluble phosphatidylinositol 4-kinase from carrot suspension culture cells
    • Okpodu, C. M., Gross, W., Burkhart, W., and Boss, W. F. (1995). Purification and characterization of a soluble phosphatidylinositol 4-kinase from carrot suspension culture cells. Plant Physiol. 107, 491-500.
    • (1995) Plant Physiol. , vol.107 , pp. 491-500
    • Okpodu, C.M.1    Gross, W.2    Burkhart, W.3    Boss, W.F.4
  • 75
    • 0029091623 scopus 로고
    • Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate-A comparison with protein kinase-C isotypes
    • Palmer, R. H., Dekker, L. V., Woscholski, R., Legood, J. A., Gigg, R., and Parker, P. J. (1995). Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate-A comparison with protein kinase-C isotypes. J. Biol. Chem. 270, 22412-22416.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22412-22416
    • Palmer, R.H.1    Dekker, L.V.2    Woscholski, R.3    Legood, J.A.4    Gigg, R.5    Parker, P.J.6
  • 76
    • 0031026639 scopus 로고    scopus 로고
    • Characterization of pl50, an adaptor protein for the human phosphatidylinositol (Ptdlns) 5-kinase-Substrate presentation by phosphatedylinositol transfer protein to the plSO-Ptdlns 3-kinase complex
    • Panaretou, C, Domin, J., Cockcroft, S., and Waterfield, M. D. (1997). Characterization of pl50, an adaptor protein for the human phosphatidylinositol (Ptdlns) 5-kinase-Substrate presentation by phosphatedylinositol transfer protein to the plSO-Ptdlns 3-kinase complex. J. Biol. Chem. 272, 2477-2485.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2477-2485
    • Panaretou, C.1    Domin, J.2    Cockcroft, S.3    Waterfield, M.D.4
  • 77
    • 0030954947 scopus 로고    scopus 로고
    • Identification and characterization of a novel plant phospholipase D that requires polyphosphoinositides and submicromolar calcium for activity in Arabidopsis
    • Pappan, K., Zheng, S., and Wang, X. (1997a). Identification and characterization of a novel plant phospholipase D that requires polyphosphoinositides and submicromolar calcium for activity in Arabidopsis. J. Biol. Chem. 272, 7048-7054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7048-7054
    • Pappan, K.1    Zheng, S.2    Wang, X.3
  • 78
    • 0031003039 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of polyphosphoinositide-dependent phospholipase D, PLDβ, from Arabidopsis
    • Pappan, K., Qin, W., Dyer, J. H., Zheng, L., and Wang, X. (1997b). Molecular cloning and functional analysis of polyphosphoinositide-dependent phospholipase D, PLDβ, from Arabidopsis. J. Biol. Chem. 272, 7055-7061.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7055-7061
    • Pappan, K.1    Qin, W.2    Dyer, J.H.3    Zheng, L.4    Wang, X.5
  • 79
    • 0028794729 scopus 로고
    • Differential expression of a glycosylated inositol phospholipid antigen on the peribacteroid membrane during pea nodule development
    • Perotto, S., Donovan, N., Drøbak, B. K., and Brewin, N. J. (1995). Differential expression of a glycosylated inositol phospholipid antigen on the peribacteroid membrane during pea nodule development. Mol. Plant-Microbe Interact. 4, 560-568.
    • (1995) Mol. Plant-Microbe Interact. , vol.4 , pp. 560-568
    • Perotto, S.1    Donovan, N.2    Drøbak, B.K.3    Brewin, N.J.4
  • 80
    • 0026474287 scopus 로고
    • Phosphatidylinositol 4-kinases and the role of polyphosphoinositides in cellular regulation
    • Pike, L. J. (1992). Phosphatidylinositol 4-kinases and the role of polyphosphoinositides in cellular regulation. Endocr. Rev. 13, 692-706.
    • (1992) Endocr. Rev. , vol.13 , pp. 692-706
    • Pike, L.J.1
  • 81
    • 0030614363 scopus 로고    scopus 로고
    • Tubulin, Gq, and phosphatidylinositol 4,5-bisphosphate interact to regulate phospholipase CB1 signaling
    • Popova, J. S., Garrison, J. C, Rhee, S. G., and Rasenick, M. M. (1997). Tubulin, Gq, and phosphatidylinositol 4,5-bisphosphate interact to regulate phospholipase CB1 signaling. J. Biol. Chem. 272, 6760-6765.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6760-6765
    • Popova, J.S.1    Garrison, J.C.2    Rhee, S.G.3    Rasenick, M.M.4
  • 82
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositoI-4,5-bisphosphate
    • Rameh, E. L., Tolias, K. F., Duckworth, B. C., and Cantley, L. C. (1997). A new pathway for synthesis of phosphatidylinositoI-4,5-bisphosphate. Nature 390, 192-196.
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, E.L.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 83
    • 0030944208 scopus 로고    scopus 로고
    • Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate
    • Randazzo, P. A. (1997). Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 272, 7688-7692.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7688-7692
    • Randazzo, P.A.1
  • 84
    • 0000410233 scopus 로고
    • Characteristics of a phosphatidylinositol exchange activity of soybean microsomes
    • Sandelius, A. S., and Morre, D. J. (1987). Characteristics of a phosphatidylinositol exchange activity of soybean microsomes. Plant Physiol. 84, 1022-1027.
    • (1987) Plant Physiol. , vol.84 , pp. 1022-1027
    • Sandelius, A.S.1    Morre, D.J.2
  • 85
    • 0000883286 scopus 로고
    • Phosphorylation of phosphatidylinositol in isolated plant membranes
    • Sandelius, A. S., and Sommarin, M. (1986). Phosphorylation of phosphatidylinositol in isolated plant membranes. FEBS Lett. 201, 282-286.
    • (1986) FEBS Lett. , vol.201 , pp. 282-286
    • Sandelius, A.S.1    Sommarin, M.2
  • 86
    • 0001907648 scopus 로고
    • Membrane-localized reactions involved in poly-phosphoinositide turnover in plants
    • D. J. Morré W. F. Boss, and F. A. Loewus, eds., Wiley-Liss, New York
    • Sandelius, A. S., and Sommarin, M. (1990). Membrane-localized reactions involved in poly-phosphoinositide turnover in plants. In "Inositol Metabolism in Plants" (D. J. Morré W. F. Boss, and F. A. Loewus, eds.), pp. 139-161. Wiley-Liss, New York.
    • (1990) Inositol Metabolism in Plants , pp. 139-161
    • Sandelius, A.S.1    Sommarin, M.2
  • 87
    • 0026576535 scopus 로고
    • Characterization of a calcium- And lipid-dependent protein kinase associated with the plasma membrane in oat
    • Schaller, G. E., Harmon, A., and Sussman, M. R. (1992). Characterization of a calcium- and lipid-dependent protein kinase associated with the plasma membrane in oat. Biochemistry 31, 1721-1727.
    • (1992) Biochemistry , vol.31 , pp. 1721-1727
    • Schaller, G.E.1    Harmon, A.2    Sussman, M.R.3
  • 88
    • 0003033137 scopus 로고
    • 2+-dependent exchange enzyme in castor bean endosperm
    • 2+-dependent exchange enzyme in castor bean endosperm. Plant Physiol. 68, 18-22.
    • (1981) Plant Physiol. , vol.68 , pp. 18-22
    • Sexton, J.C.1    Moore, T.S.2
  • 89
    • 0030040967 scopus 로고    scopus 로고
    • The pleckstrin homology domain: An intriguing multifunctional protein module
    • Shaw, G. (1996). The pleckstrin homology domain: An intriguing multifunctional protein module. Bioessays 18, 35-46.
    • (1996) Bioessays , vol.18 , pp. 35-46
    • Shaw, G.1
  • 90
    • 0031004866 scopus 로고    scopus 로고
    • Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo
    • Shibasaki, Y., Ishihara, H., Kizuki, N., Asano, T., Oka, Y., and Yazaki, Y. (1997). Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo. J. Biol. Chem. 272, 7578-7581.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7578-7581
    • Shibasaki, Y.1    Ishihara, H.2    Kizuki, N.3    Asano, T.4    Oka, Y.5    Yazaki, Y.6
  • 91
    • 0027378857 scopus 로고
    • Phospholipid transfer activity is relevant to but not sufficient for the essential function of the yeast SEC14 gene product
    • Skinner, H. B., Alb, J. G., Whitters, E. A., Helmkamp, G. M., and Bankaitis, V. A. (1993). Phospholipid transfer activity is relevant to but not sufficient for the essential function of the yeast SEC14 gene product. EMBO J. 12, 4775-4784.
    • (1993) EMBO J. , vol.12 , pp. 4775-4784
    • Skinner, H.B.1    Alb, J.G.2    Whitters, E.A.3    Helmkamp, G.M.4    Bankaitis, V.A.5
  • 92
    • 0028906430 scopus 로고
    • The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity
    • Skinner, H. B., McGee, T. P., McMaster, C. R., Fry, M. R., Bell, R. M., and Bankaitis, V. A. (1995). The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity. Proc. Natl. Acad. Sei. USA 92, 112-116.
    • (1995) Proc. Natl. Acad. Sei. USA , vol.92 , pp. 112-116
    • Skinner, H.B.1    McGee, T.P.2    McMaster, C.R.3    Fry, M.R.4    Bell, R.M.5    Bankaitis, V.A.6
  • 93
    • 0001607981 scopus 로고
    • Phosphatidylinositol and phosphatidylinositolphosphate kinases in plant plasma-membranes
    • Sommarin, M., and Sandelius, A. S. (1988). Phosphatidylinositol and phosphatidylinositolphosphate kinases in plant plasma-membranes. Biochim. Biophys. Acta 958, 268-278.
    • (1988) Biochim. Biophys. Acta , vol.958 , pp. 268-278
    • Sommarin, M.1    Sandelius, A.S.2
  • 94
    • 0025731596 scopus 로고
    • Pathway of phosphatidylinositol(3,4,5)triphosphate synthesis in activated neutrophils
    • Stephens, L. R., Hughes, K. T., and Irvine, R. F. (1991). Pathway of phosphatidylinositol(3,4,5)triphosphate synthesis in activated neutrophils. Nature 351, 33-39.
    • (1991) Nature , vol.351 , pp. 33-39
    • Stephens, L.R.1    Hughes, K.T.2    Irvine, R.F.3
  • 95
    • 0032575493 scopus 로고    scopus 로고
    • A Phosphatidylinositol 4-kinase pleckstrin homology (PH) domain that binds phosphatidylinositol 4-monophosphate
    • Stevenson, J. M., Perera, I. Y., and Boss, W. F. (1998). A Phosphatidylinositol 4-kinase pleckstrin homology (PH) domain that binds phosphatidylinositol 4-monophosphate. J. Biol. Chem. 273, 22761-22767.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22761-22767
    • Stevenson, J.M.1    Perera, I.Y.2    Boss, W.F.3
  • 96
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracelluler store in pancreatic acinar-cells by inositol-l,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracelluler store in pancreatic acinar-cells by inositol-l,4,5-trisphosphate. Nature 306, 67-69.
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 97
    • 0023693795 scopus 로고
    • Activation of a low specific activity form of DNA polymerase a by inositol-l,4-bisphosphate
    • Sylvia, V., Curtin, G., Norman, J., Stec, J., and Busbee, D. (1988). Activation of a low specific activity form of DNA polymerase a by inositol-l,4-bisphosphate. Cell 54, 651-658.
    • (1988) Cell , vol.54 , pp. 651-658
    • Sylvia, V.1    Curtin, G.2    Norman, J.3    Stec, J.4    Busbee, D.5
  • 98
    • 0000698690 scopus 로고
    • Association of phosphatidylinositol kinase, phosphatidylinositol monophosphate kinase and diacylglycerol kinase with the cytoskeleton and F-actin fractions of carrot (Daucus carota L.) cells grown in suspension culture: Response to cell wall degrading enzymes
    • Tan, Z., and Boss, W. F. (1992). Association of phosphatidylinositol kinase, phosphatidylinositol monophosphate kinase and diacylglycerol kinase with the cytoskeleton and F-actin fractions of carrot (Daucus carota L.) cells grown in suspension culture: Response to cell wall degrading enzymes. Plant Physiol. 100, 2116-2120.
    • (1992) Plant Physiol. , vol.100 , pp. 2116-2120
    • Tan, Z.1    Boss, W.F.2
  • 99
    • 0030576913 scopus 로고    scopus 로고
    • Molecular cloning of rat phosphatidylinositol synthase cDNA by functional complementation of the yeast Saccharomyces cervisiae pis
    • Tanaka, S., Nikawa, J., Imai, H., Yamashita, S., and Hosaka, K. (1996). Molecular cloning of rat phosphatidylinositol synthase cDNA by functional complementation of the yeast Saccharomyces cervisiae pis. FEES Lett. 393, 89-92.
    • (1996) FEES Lett. , vol.393 , pp. 89-92
    • Tanaka, S.1    Nikawa, J.2    Imai, H.3    Yamashita, S.4    Hosaka, K.5
  • 100
    • 84913341998 scopus 로고
    • Properties of phospholipid exchange proteins from germinated castor bean endosperms
    • J. F. G. M. Wintermans and P. J. C. Kuiper, eds., Elsevier, Amsterdam
    • Tanaka, T., and Yamada, M. (1982). Properties of phospholipid exchange proteins from germinated castor bean endosperms. In "Biochemistry and Metabolism of Plant Lipids" (J. F. G. M. Wintermans and P. J. C. Kuiper, eds.), pp. 99-106. Elsevier, Amsterdam.
    • (1982) Biochemistry and Metabolism of Plant Lipids , pp. 99-106
    • Tanaka, T.1    Yamada, M.2
  • 101
    • 0027185354 scopus 로고
    • An essential role for phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling
    • Thomas, G. M. H., Cunningham, E., Fensome, A., Ball, A., Totty, N. F., Truong, O., Hsuan, J. J., and Cockcroft, S. (1993). An essential role for phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling. Cell 74, 919-928.
    • (1993) Cell , vol.74 , pp. 919-928
    • Thomas, G.M.H.1    Cunningham, E.2    Fensome, A.3    Ball, A.4    Totty, N.F.5    Truong, O.6    Hsuan, J.J.7    Cockcroft, S.8
  • 102
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., Cantley, L. C., and Carpenter, C. L. (1995). Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270, 17656-17659.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 103
    • 0023352515 scopus 로고
    • Phosphatidylinositol-transfer protein and cellular phosphatidylinositol metabolism
    • Van Paridon, P. A., Somerharju, P., and Wirtz, K. W. A. (1987). Phosphatidylinositol-transfer protein and cellular phosphatidylinositol metabolism. Biochem. Soc. Trans. 15, 321-323.
    • (1987) Biochem. Soc. Trans. , vol.15 , pp. 321-323
    • Van Paridon, P.A.1    Somerharju, P.2    Wirtz, K.W.A.3
  • 104
    • 0022443823 scopus 로고
    • Polyamines stimulate the phosphorylation of phosphatidylinositol in membranes from A431 cells
    • Vogel, S., and Hoppe, J. (1986). Polyamines stimulate the phosphorylation of phosphatidylinositol in membranes from A431 cells. Eur. J. Biochem. 154, 253-257.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 253-257
    • Vogel, S.1    Hoppe, J.2
  • 105
    • 0027942615 scopus 로고
    • ATVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calciumdependent lipid-binding domain
    • Welters, P., Takegawa, K., Emr, S. D., and Chrispeels, M. J. (1994). ATVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calciumdependent lipid-binding domain. Proc. Natl. Acad. Sei. USA 91, 11398-11402.
    • (1994) Proc. Natl. Acad. Sei. USA , vol.91 , pp. 11398-11402
    • Welters, P.1    Takegawa, K.2    Emr, S.D.3    Chrispeels, M.J.4
  • 106
    • 0030944761 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate defines a novel PI 3-kinase pathway in resting mouse fibroblasts
    • Whiteford, C. C., Brearley, C. A., and Ulug, E. T. (1997). Phosphatidylinositol 3,5-bisphosphate defines a novel PI 3-kinase pathway in resting mouse fibroblasts. Biochem. J. 323,597-601.
    • (1997) Biochem. J. , vol.323 , pp. 597-601
    • Whiteford, C.C.1    Brearley, C.A.2    Ulug, E.T.3
  • 107
    • 0023897684 scopus 로고
    • Type 1 phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol 3-phosphate
    • Whitman, M., Downes, C. P., Keeler, M., Keller, T., and Cantley, L. C. (1988). Type 1 phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol 3-phosphate. Nature 332, 644-646.
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.C.5
  • 108
    • 0025766081 scopus 로고
    • Phospholipid transfer proteins
    • Wirtz, K. W. A. (1991). Phospholipid transfer proteins. Anna. Rev. Biochem. 60, 73-99.
    • (1991) Anna. Rev. Biochem. , vol.60 , pp. 73-99
    • Wirtz, K.W.A.1
  • 109
    • 0028032480 scopus 로고
    • Cloning and characterization of a human phosphatidylinositol 4-kinase
    • Wong, K., and Cantley, L. C. (1994). Cloning and characterization of a human phosphatidylinositol 4-kinase. J. Biol. Chem. 269, 28878-28884.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28878-28884
    • Wong, K.1    Cantley, L.C.2
  • 110
    • 0030989280 scopus 로고    scopus 로고
    • Subcellular localizations of phosphatidylinositol 4-kinase isoforms
    • Wong, K., Meyers, R., and Cantley, L. C. (1997). Subcellular localizations of phosphatidylinositol 4-kinase isoforms. J. Biol. Chem. 272, 13236-13241.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13236-13241
    • Wong, K.1    Meyers, R.2    Cantley, L.C.3
  • 111
    • 0000514378 scopus 로고
    • Association of phosphatidylinositol 4-kinase with the plant cytoskeleton
    • Xu, P., Lloyd, C. W., Staiger, C. J., and Dr0bak, B. K. (1992). Association of phosphatidylinositol 4-kinase with the plant cytoskeleton. Plant Cell 4, 941-951.
    • (1992) Plant Cell , vol.4 , pp. 941-951
    • Xu, P.1    Lloyd, C.W.2    Staiger, C.J.3    Drobak, B.K.4
  • 112
    • 0028015608 scopus 로고
    • Regulation of the plasma membrane type III phosphatidylinositol 4-kinase by positively charged compounds
    • Yang, W., and Boss, W. F. (1994a). Regulation of the plasma membrane type III phosphatidylinositol 4-kinase by positively charged compounds. Arch. Biochem. Biophys. 313,112-119.
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 112-119
    • Yang, W.1    Boss, W.F.2
  • 113
    • 0028111491 scopus 로고
    • Regulation of the phosphatidylinositol 4-kinase activity by the protein activator PIK-A49. Activation requires protein phosphorylation
    • Yang, W., and Boss, W. F. (1994b). Regulation of the phosphatidylinositol 4-kinase activity by the protein activator PIK-A49. Activation requires protein phosphorylation. J. Biol. Chem. 269, 3852-2857.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3852-12857
    • Yang, W.1    Boss, W.F.2
  • 114
    • 0027463634 scopus 로고
    • Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells
    • Yang, W., Burkhart, W., Cavallius, J., Merrick, W. C., and Boss, W. F. (1993). Purification and characterization of a phosphatidylinositol 4-kinase activator in carrot cells. J. Biol. Chem. 268, 392-398.
    • (1993) J. Biol. Chem. , vol.268 , pp. 392-398
    • Yang, W.1    Burkhart, W.2    Cavallius, J.3    Merrick, W.C.4    Boss, W.F.5
  • 115
    • 0028218165 scopus 로고
    • Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae
    • Yoshida, S., Ohya, Y., Nakano, A., and Anraku, Y. (1994). Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae. Mol. Gen. Genet. 242, 631-640.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 631-640
    • Yoshida, S.1    Ohya, Y.2    Nakano, A.3    Anraku, Y.4
  • 117
    • 0029835783 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5bisphosphate provides an alternative to guanine-nucleotide exchange factors by stimulating the dissociation of GDP from CDC42HS
    • Zheng, Y., Glaven, J. A., Wu, W. J., and Cerione, R. A. (1996). Phosphatidylinositol 4,5bisphosphate provides an alternative to guanine-nucleotide exchange factors by stimulating the dissociation of GDP from CDC42HS. J. Biol. Chem. 271, 23815-23819.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23815-23819
    • Zheng, Y.1    Glaven, J.A.2    Wu, W.J.3    Cerione, R.A.4


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