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Volumn 24, Issue 4, 2009, Pages 231-244

Phosphoinositide signaling: new tools and insights

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITOL;

EID: 69249090082     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00014.2009     Document Type: Review
Times cited : (137)

References (191)
  • 1
    • 46649091539 scopus 로고    scopus 로고
    • Dissecting the role of Ptdlns(4,5)P, in endocytosis and recycling of the transferrin receptor
    • Abe N, Inoue T, Galvez T, Klein L, Meyer T. Dissecting the role of Ptdlns(4,5)P, in endocytosis and recycling of the transferrin receptor. J Cell Sci 121: 1488-1494, 2008.
    • (2008) J Cell Sci , vol.121 , pp. 1488-1494
    • Abe, N.1    Inoue, T.2    Galvez, T.3    Klein, L.4    Meyer, T.5
  • 2
    • 30544432539 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 regulation of phosphatidylinositol-4,5-bisphosphate synthesis, endocytosis, and exocytosis
    • Aikawa Y, Martin TF. ADP-ribosylation factor 6 regulation of phosphatidylinositol-4,5-bisphosphate synthesis, endocytosis, and exocytosis. Methods Enzymol 404: 422-431, 2005.
    • (2005) Methods Enzymol , vol.404 , pp. 422-431
    • Aikawa, Y.1    Martin, T.F.2
  • 4
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro A, Wymann MP. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem J 296: 297-301, 1993.
    • (1993) Biochem J , vol.296 , pp. 297-301
    • Arcaro, A.1    Wymann, M.P.2
  • 6
    • 0036001334 scopus 로고    scopus 로고
    • Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkd-mediated MAP kinase cascade
    • Audhya A, Emr SD. Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkd-mediated MAP kinase cascade. Dev Cell 2: 593-605, 2002.
    • (2002) Dev Cell , vol.2 , pp. 593-605
    • Audhya, A.1    Emr, S.D.2
  • 7
    • 58249089034 scopus 로고    scopus 로고
    • Assembly of the Ptdlns 4-kinase Stt4 complex at the plasma membrane requires Ypp1 and Efr3
    • Baird D, Stefan C, Audhya A, Weys S, Emr SD. Assembly of the Ptdlns 4-kinase Stt4 complex at the plasma membrane requires Ypp1 and Efr3. J Cell Biol 183: 1061-1074, 2008.
    • (2008) J Cell Biol , vol.183 , pp. 1061-1074
    • Baird, D.1    Stefan, C.2    Audhya, A.3    Weys, S.4    Emr, S.D.5
  • 8
    • 33745933535 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinases; old enzymes with emerging functions
    • Balla A, Balla T. Phosphatidylinositol 4-kinases; old enzymes with emerging functions. Trends Cell Biol 16: 351-361, 2006.
    • (2006) Trends Cell Biol , vol.16 , pp. 351-361
    • Balla, A.1    Balla, T.2
  • 9
    • 39449085866 scopus 로고    scopus 로고
    • Maintenance of hormone-sensitive phosphoinositide pools in the plasma membrane requires phosphatidylinositol 4-kinase lllalpha
    • Balla A, Ju Kim Y, Varnai P, Szentpetery Z, Knight Z, Shokat KM, Balla T. Maintenance of hormone-sensitive phosphoinositide pools in the plasma membrane requires phosphatidylinositol 4-kinase lllalpha. Mol Biol Cell 19: 711-721, 2007.
    • (2007) Mol Biol Cell , vol.19 , pp. 711-721
    • Balla, A.1    Ju Kim, Y.2    Varnai, P.3    Szentpetery, Z.4    Knight, Z.5    Shokat, K.M.6    Balla, T.7
  • 10
    • 0037205494 scopus 로고    scopus 로고
    • Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments
    • Balla A, Tuymetova G, Barshishat M, Geiszt M, Balla T. Characterization of type II phosphatidylinositol 4-kinase isoforms reveals association of the enzymes with endosomal vesicular compartments. J Biol Chem 277: 20041-22050, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 20041-22050
    • Balla, A.1    Tuymetova, G.2    Barshishat, M.3    Geiszt, M.4    Balla, T.5
  • 11
    • 14844302797 scopus 로고    scopus 로고
    • A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: Studies with the PH domains of the oxysterol binding protein and FAPP1
    • Balla A, Tuymetova G, Tsiomenko A, Varnai P, Balla T. A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1. Mol Biol Cell 16: 1282-1295, 2005.
    • (2005) Mol Biol Cell , vol.16 , pp. 1282-1295
    • Balla, A.1    Tuymetova, G.2    Tsiomenko, A.3    Varnai, P.4    Balla, T.5
  • 12
    • 21044443928 scopus 로고    scopus 로고
    • Inositol-lipid binding motifs: Signal integrators through protein-lipid and protein-protein interactions
    • Balla T. Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions. J Cell Sci 118: 2093-2104, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 2093-2104
    • Balla, T.1
  • 13
    • 63649110520 scopus 로고    scopus 로고
    • Balla T, Varnai P. Visualization of cellular phosphoinositide pools with GFP-fused protein-domains. Curr Protoc Cell Biol 24: 24.4, 2009.
    • Balla T, Varnai P. Visualization of cellular phosphoinositide pools with GFP-fused protein-domains. Curr Protoc Cell Biol 24: 24.4, 2009.
  • 14
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC 14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • Bankaitis VA, Malehorn DE, Emr SD, Greene R. The Saccharomyces cerevisiae SEC 14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. J Cell Biol 108: 1271-1281, 1989.
    • (1989) J Cell Biol , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 15
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron CL, Malhotra V. Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science 295: 325-328, 2002.
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 17
    • 0030013607 scopus 로고    scopus 로고
    • Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins
    • Belshaw PJ, Ho SN, Crabtree GR, Schreiber SL. Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins. Proc Natl Acad Sci USA 93: 4604-4607, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4604-4607
    • Belshaw, P.J.1    Ho, S.N.2    Crabtree, G.R.3    Schreiber, S.L.4
  • 19
    • 0020636518 scopus 로고
    • Rapid accumulation of inositol trisphosphate reveals that agonists hydrolyze polyphosphoinositides instead of phosphatidylinositol
    • Berridge MJ. Rapid accumulation of inositol trisphosphate reveals that agonists hydrolyze polyphosphoinositides instead of phosphatidylinositol. Biochem J 212: 849-858, 1983.
    • (1983) Biochem J , vol.212 , pp. 849-858
    • Berridge, M.J.1
  • 20
    • 0031771547 scopus 로고    scopus 로고
    • Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors
    • Boronenkov IV, Loijens JC, Umeda M, Anderson RA. 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
  • 21
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic
    • Brown FD, Rozelle AL, Yin HL, Balla T, Donaldson JG. Phosphatidylinositol 4,5-bisphosphate and Arf6-regulated membrane traffic. J Cell Biol 154: 1007-1017, 2001.
    • (2001) J Cell Biol , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 22
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd CG, Emr SD. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol Cell 2: 157-162, 1998.
    • (1998) Mol Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 23
    • 25844454807 scopus 로고    scopus 로고
    • Coincidence detection in phosphoinositide signaling
    • Carlton JG, Cullen PJ. Coincidence detection in phosphoinositide signaling. Trends Cell Biol 15: 540-547, 2005.
    • (2005) Trends Cell Biol , vol.15 , pp. 540-547
    • Carlton, J.G.1    Cullen, P.J.2
  • 24
    • 0025192085 scopus 로고
    • Heterogeneity of [3H]inositol 1,4,5-trisphosphate binding sites in adrenocortical membranes. Characterisation and validation of a radioreceptor assay
    • Challis RAJ, Chilvers ER, Wilcocks AL, Nahorski SR. Heterogeneity of [3H]inositol 1,4,5-trisphosphate binding sites in adrenocortical membranes. Characterisation and validation of a radioreceptor assay. Biochem J 265: 421-427, 1990.
    • (1990) Biochem J , vol.265 , pp. 421-427
    • Challis, R.A.J.1    Chilvers, E.R.2    Wilcocks, A.L.3    Nahorski, S.R.4
  • 25
    • 3843053639 scopus 로고    scopus 로고
    • The direct interaction between ASH2, a Drosophila trithorax group protein, and SKTL, a nuclear phosphatidylinositol 4phosphate 5-kinase, implies a role for phosphatidylinositol 4,5-bisphosphate in maintaining transcriptionally active chromatin
    • Cheng MK, Shearn A. The direct interaction between ASH2, a Drosophila trithorax group protein, and SKTL, a nuclear phosphatidylinositol 4phosphate 5-kinase, implies a role for phosphatidylinositol 4,5-bisphosphate in maintaining transcriptionally active chromatin. Genetics 167: 1213-1223, 2004.
    • (2004) Genetics , vol.167 , pp. 1213-1223
    • Cheng, M.K.1    Shearn, A.2
  • 26
    • 0035927651 scopus 로고    scopus 로고
    • Bradykinin and nerve growth factor release the capsaicin receptor from Ptdlns(4,5)P,-mediated inhibition
    • Chuang HH, Prescott ED, Kong H, Shields S, Jordt SE, Basbaum Al, Chao MV, Julius D. Bradykinin and nerve growth factor release the capsaicin receptor from Ptdlns(4,5)P,-mediated inhibition. Nature 411: 957-962, 2001.
    • (2001) Nature , vol.411 , pp. 957-962
    • Chuang, H.H.1    Prescott, E.D.2    Kong, H.3    Shields, S.4    Jordt, S.E.5    Basbaum, A.6    Chao, M.V.7    Julius, D.8
  • 28
    • 34249784529 scopus 로고    scopus 로고
    • Biochemical and biological functions of class I phosphatidylinositol transfer proteins
    • Cockcroft S, Carvou N. Biochemical and biological functions of class I phosphatidylinositol transfer proteins. Biochim Biophys Acta 1771: 677-691, 2007.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 677-691
    • Cockcroft, S.1    Carvou, N.2
  • 29
    • 44949264001 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-kinase type II alpha contains an AP-3 sorting motif and a kinase domain that are both required for endosome traffic
    • Craige B, Salazar G, Faundez V. Phosphatidylinositol-4-kinase type II alpha contains an AP-3 sorting motif and a kinase domain that are both required for endosome traffic. Mol Biol Cell 19: 1415-1426, 2008.
    • (2008) Mol Biol Cell , vol.19 , pp. 1415-1426
    • Craige, B.1    Salazar, G.2    Faundez, V.3
  • 31
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech MP. Dynamics of phosphoinositides in membrane retrieval and insertion. Annu Rev Physiol 65: 791-815, 2003.
    • (2003) Annu Rev Physiol , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 33
    • 59449084852 scopus 로고    scopus 로고
    • Activity of the neuronal cold sensor TRPM8 is regulated by phospholipase C via the phospholipid phosphoinositol 4,5-bisphosphate
    • Daniels RL, Takashima Y, McKemy DD. Activity of the neuronal cold sensor TRPM8 is regulated by phospholipase C via the phospholipid phosphoinositol 4,5-bisphosphate. J Biol Chem 284: 1570-1582, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 1570-1582
    • Daniels, R.L.1    Takashima, Y.2    McKemy, D.D.3
  • 35
    • 20544464167 scopus 로고    scopus 로고
    • The role of the phosphoinositides at the Golgi complex
    • De Matteis MA, Di Campli A, Godi A. The role of the phosphoinositides at the Golgi complex. Biochim Biophys Acta 1744: 396-405, 2005.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 396-405
    • De Matteis, M.A.1    Di Campli, A.2    Godi, A.3
  • 36
    • 0027209418 scopus 로고
    • Inositides and the nucleus and inositides in the nucleus
    • Divecha N, Banfic H, Irvine RF. Inositides and the nucleus and inositides in the nucleus. Cell 74: 405-407, 1993.
    • (1993) Cell , vol.74 , pp. 405-407
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 37
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (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, Irvine RF. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (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: 3207-3214, 1991.
    • (1991) EMBO J , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 38
    • 0027446592 scopus 로고
    • Phosphoinositide signalling enzymes in rat liver nuclei: Phosphoinositidase C isoform beta1 is specifically, but not predominantly, located in the nucleus
    • Divecha N, Rhee SG, Letcher AJ, Irvine RF. Phosphoinositide signalling enzymes in rat liver nuclei: phosphoinositidase C isoform beta1 is specifically, but not predominantly, 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
  • 39
    • 0042817834 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place
    • Doughman RL, Firestone AJ, Anderson RA. Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place. J Membr Biol 194: 77-89, 2003.
    • (2003) J Membr Biol , vol.194 , pp. 77-89
    • Doughman, R.L.1    Firestone, A.J.2    Anderson, R.A.3
  • 40
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J 351: 19-31, 2000.
    • (2000) Biochem J , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5    Downes, C.P.6    Alessi, D.R.7
  • 41
    • 18044364473 scopus 로고    scopus 로고
    • Probing phosphoinositide functions in signaling and membrane trafficking
    • Downes CP, Gray A, Lucocq JM. Probing phosphoinositide functions in signaling and membrane trafficking. Trends Cell Biol 15: 259-268, 2005.
    • (2005) Trends Cell Biol , vol.15 , pp. 259-268
    • Downes, C.P.1    Gray, A.2    Lucocq, J.M.3
  • 42
    • 0344234375 scopus 로고    scopus 로고
    • Advances in procedures for the detection and localization of inositol phospholipid signals in cells, tissues, and enzyme assays
    • Downes CP, Gray A, Watt SA, Lucocq JM. Advances in procedures for the detection and localization of inositol phospholipid signals in cells, tissues, and enzyme assays. Methods Enzymol 366: 64-84, 2003.
    • (2003) Methods Enzymol , vol.366 , pp. 64-84
    • Downes, C.P.1    Gray, A.2    Watt, S.A.3    Lucocq, J.M.4
  • 43
    • 0025330471 scopus 로고
    • Evidence that the inositol phospholipids are necessary for exocytosis
    • Eberhard DA, Cooper CL, Low MG, Holz RW. Evidence that the inositol phospholipids are necessary for exocytosis. Biochem J 268: 15-25, 1990.
    • (1990) Biochem J , vol.268 , pp. 15-25
    • Eberhard, D.A.1    Cooper, C.L.2    Low, M.G.3    Holz, R.W.4
  • 44
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen LO, Perisic O, Cheung R, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 380: 595-602, 1996.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 45
    • 34848818827 scopus 로고    scopus 로고
    • The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function
    • Fairn GD, Curwin AJ, Stefan CJ, McMaster CR. The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function. Proc Natl Acad Sci USA 104: 15352-15357, 2007.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15352-15357
    • Fairn, G.D.1    Curwin, A.J.2    Stefan, C.J.3    McMaster, C.R.4
  • 48
    • 0035172107 scopus 로고    scopus 로고
    • Sad lipid phosphatase and stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology
    • Foti M, Audhya A, Emr SD. Sad lipid phosphatase and stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol Biol Cell 128: 2396-2411, 2001.
    • (2001) Mol Biol Cell , vol.128 , pp. 2396-2411
    • Foti, M.1    Audhya, A.2    Emr, S.D.3
  • 52
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • Fugmann T, Hausser A, Schoffler P, Schmid S, Pfizenmaier K, Olayioye MA. Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J Cell Biol 178: 15-22, 2007.
    • (2007) J Cell Biol , vol.178 , pp. 15-22
    • Fugmann, T.1    Hausser, A.2    Schoffler, P.3    Schmid, S.4    Pfizenmaier, K.5    Olayioye, M.A.6
  • 53
    • 0033598129 scopus 로고    scopus 로고
    • Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits
    • Gaidarov I, Keen JH. Phosphoinositide-AP-2 interactions required for targeting to plasma membrane clathrin-coated pits. J Cell Biol 146: 755-764, 1999.
    • (1999) J Cell Biol , vol.146 , pp. 755-764
    • Gaidarov, I.1    Keen, J.H.2
  • 55
    • 36348965431 scopus 로고    scopus 로고
    • Regulation of ion transport proteins by membrane phosphoinositides
    • Gamper N, Shapiro MS. Regulation of ion transport proteins by membrane phosphoinositides. Nat Rev Neurosci 8: 921-934, 2007.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 921-934
    • Gamper, N.1    Shapiro, M.S.2
  • 56
    • 0032487577 scopus 로고    scopus 로고
    • Fab1p is essential for Ptdlns(3)P 5kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • Gary JD, Wurmser AE, Bonangelino CJ, Weisman LS, Emr SD. Fab1p is essential for Ptdlns(3)P 5kinase activity and the maintenance of vacuolar size and membrane homeostasis. J Cell Biol 143: 65-79, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 62
    • 26544475380 scopus 로고
    • Myo-inositol phosphates from beef brain phosphoinostide
    • Grado C, Ballou CE. Myo-inositol phosphates from beef brain phosphoinostide. J Biol Chem 235: PC23-PC24, 1960.
    • (1960) J Biol Chem , vol.235
    • Grado, C.1    Ballou, C.E.2
  • 63
    • 59049103089 scopus 로고    scopus 로고
    • Ci-VSP is a depolarization- activated phosphatidylinositol4,5-bisphosphate and phosphatidylinositol-3,4, 5trisphosphate 5'-phosphatase
    • Halaszovich CR, Schreiber DN, Oliver D. Ci-VSP is a depolarization- activated phosphatidylinositol4,5-bisphosphate and phosphatidylinositol-3,4, 5trisphosphate 5'-phosphatase. J Biol Chem 284: 2106-2113, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 2106-2113
    • Halaszovich, C.R.1    Schreiber, D.N.2    Oliver, D.3
  • 65
    • 0033607537 scopus 로고    scopus 로고
    • Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae
    • Hama H, Schnieders EA, Thorner J, Takemoto JY, DeWald DB. Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae. J Biol Chem 274: 34294-34300, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 34294-34300
    • Hama, H.1    Schnieders, E.A.2    Thorner, J.3    Takemoto, J.Y.4    DeWald, D.B.5
  • 66
    • 33646227441 scopus 로고    scopus 로고
    • Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide
    • Hanada K. Discovery of the molecular machinery CERT for endoplasmic reticulum-to-Golgi trafficking of ceramide. Mol Cell Biochem 286: 23-31, 2006.
    • (2006) Mol Cell Biochem , vol.286 , pp. 23-31
    • Hanada, K.1
  • 68
    • 26944446652 scopus 로고    scopus 로고
    • Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase lllbeta at the Golgi complex
    • Hausser A, Storz P, Martens S, Link G, Toker A, Pfizenmaier K. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase lllbeta at the Golgi complex. Nat Cell Biol 7: 880-886, 2005.
    • (2005) Nat Cell Biol , vol.7 , pp. 880-886
    • Hausser, A.1    Storz, P.2    Martens, S.3    Link, G.4    Toker, A.5    Pfizenmaier, K.6
  • 71
    • 14044278863 scopus 로고    scopus 로고
    • Interaction of neuronal calcium sensor-1 and ADP-ribosylation factor 1 allows bidirectional control of phosphatidylinositol 4-kinase beta and trans-Golgi network-plasma membrane traffic
    • Haynes LP, Thomas GM, Burgoyne RD. Interaction of neuronal calcium sensor-1 and ADP-ribosylation factor 1 allows bidirectional control of phosphatidylinositol 4-kinase beta and trans-Golgi network-plasma membrane traffic. J Biol Chem 280: 6047-6054, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 6047-6054
    • Haynes, L.P.1    Thomas, G.M.2    Burgoyne, R.D.3
  • 72
    • 0033175467 scopus 로고    scopus 로고
    • Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol 4-OH-kinase
    • Hendricks KB, Wang BQ, Schnieders EA, Thorner J. Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol 4-OH-kinase. Nat Cell Biol 1:234-241, 1999.
    • (1999) Nat Cell Biol , vol.1 , pp. 234-241
    • Hendricks, K.B.1    Wang, B.Q.2    Schnieders, E.A.3    Thorner, J.4
  • 74
    • 0029831984 scopus 로고    scopus 로고
    • 2+ exchange and KATP potassium channels by PIP2
    • 2+ exchange and KATP potassium channels by PIP2. Science 273: 956-959, 1996.
    • (1996) Science , vol.273 , pp. 956-959
    • Hilgemann, D.W.1    Ball, R.2
  • 75
    • 0035808040 scopus 로고    scopus 로고
    • The complex and intriguing lives of PIP2 with ion channels and transporters
    • Hilgemann DW, Feng S, Nasuhoglu C. The complex and intriguing lives of PIP2 with ion channels and transporters. Sci STKE 2001 : RE19, 2001.
    • (2001) Sci STKE , vol.2001
    • Hilgemann, D.W.1    Feng, S.2    Nasuhoglu, C.3
  • 76
    • 84960994832 scopus 로고
    • Enzyme secretion and incorporation of P32 into phospholipides of pancreas slices
    • Hokin MR, Hokin LE. Enzyme secretion and incorporation of P32 into phospholipides of pancreas slices. J Biol Chem 203: 967-977, 1953.
    • (1953) J Biol Chem , vol.203 , pp. 967-977
    • Hokin, M.R.1    Hokin, L.E.2
  • 78
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma
    • Huang CL, Feng S, Hilgemann DW. Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma. Nature 391: 803-806, 1998.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 79
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Im YJ, Raychaudhuri S, Prinz WA, Hurley JH. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437: 154-158, 2005.
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 80
    • 33745228758 scopus 로고    scopus 로고
    • Nuclear inositide signalling: Expansion, structures and clarification
    • Irvine RF. Nuclear inositide signalling: expansion, structures and clarification. Biochim Biophys Acta 1761: 505-508, 2006.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 505-508
    • Irvine, R.F.1
  • 81
    • 48249119533 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion
    • James DJ, Khodthong C, Kowalchyk JA, Martin TF. Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion. J Cell Biol 182: 355-366, 2008.
    • (2008) J Cell Biol , vol.182 , pp. 355-366
    • James, D.J.1    Khodthong, C.2    Kowalchyk, J.A.3    Martin, T.F.4
  • 84
    • 85120095557 scopus 로고    scopus 로고
    • Kim AY, Tang Z, Liu Q, Patel KN, Maag D, Geng Y, Dong X. Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1. Cell 133: 475-485, 2008.
    • Kim AY, Tang Z, Liu Q, Patel KN, Maag D, Geng Y, Dong X. Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1. Cell 133: 475-485, 2008.
  • 85
    • 0031834338 scopus 로고    scopus 로고
    • Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3kinase and Akt
    • Kontos CD, Stauffer TP, Yang WP, York JD, Huang L, Blanar MA, Meyer T, Peters KG. Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3kinase and Akt. Mol Cell Biol 18: 4131-4140, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 4131-4140
    • Kontos, C.D.1    Stauffer, T.P.2    Yang, W.P.3    York, J.D.4    Huang, L.5    Blanar, M.A.6    Meyer, T.7    Peters, K.G.8
  • 87
    • 33847081630 scopus 로고    scopus 로고
    • Integration of phosphoinositide- and calmodulin-mediated regulation of TRPC6
    • Kwon Y, Hofmann T, Montell C. Integration of phosphoinositide- and calmodulin-mediated regulation of TRPC6. Mol Cell 25: 491-503, 2007.
    • (2007) Mol Cell , vol.25 , pp. 491-503
    • Kwon, Y.1    Hofmann, T.2    Montell, C.3
  • 90
    • 0028986620 scopus 로고
    • Protein kinase C epsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi Function
    • Lehel C, Olah Z, Jakab G, Anderson WB. Protein kinase C epsilon is localized to the Golgi via its zinc-finger domain and modulates Golgi Function. Proc Natl Acad Sci USA 92: 1406-1410, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1406-1410
    • Lehel, C.1    Olah, Z.2    Jakab, G.3    Anderson, W.B.4
  • 91
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon MA. Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9: 99-111, 2008.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 92
    • 8744219635 scopus 로고    scopus 로고
    • Pleckstrin homology domains: Not just for phosphoinositides
    • Lemmon MA. Pleckstrin homology domains: not just for phosphoinositides. Biochem Soc Trans 32: 707-711, 2004.
    • (2004) Biochem Soc Trans , vol.32 , pp. 707-711
    • Lemmon, M.A.1
  • 93
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • Levine TP, Munro S. Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol Biol Cell 6: 1633-1644, 2001.
    • (2001) Mol Biol Cell , vol.6 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 94
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both Ptdlns 4-kinase-dependent and -independent components
    • Levine TP, Munro S. Targeting of Golgi-specific pleckstrin homology domains involves both Ptdlns 4-kinase-dependent and -independent components. Curr Biol 12: 695-704, 2002.
    • (2002) Curr Biol , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 95
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin-homology domain of oxysterol-binding protein recognizes a determinant specific to Golgi membranes
    • Levine TP, Munro S. The pleckstrin-homology domain of oxysterol-binding protein recognizes a determinant specific to Golgi membranes. Curr Biol 8: 729-739, 1998.
    • (1998) Curr Biol , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2
  • 96
    • 33947243452 scopus 로고    scopus 로고
    • The molecular choreography of a storeoperated calcium channel
    • Lewis RS. The molecular choreography of a storeoperated calcium channel. Nature 446: 284-287, 2007.
    • (2007) Nature , vol.446 , pp. 284-287
    • Lewis, R.S.1
  • 97
    • 0036544518 scopus 로고    scopus 로고
    • Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex
    • Li X, Rivas MP, Fang M, Marchena J, Mehrotra B, Chaudhary A, Feng L, Prestwich GD, Bankaitis VA. Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. J Cell Biol 157: 63-77, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 63-77
    • Li, X.1    Rivas, M.P.2    Fang, M.3    Marchena, J.4    Mehrotra, B.5    Chaudhary, A.6    Feng, L.7    Prestwich, G.D.8    Bankaitis, V.A.9
  • 98
    • 14744294236 scopus 로고    scopus 로고
    • Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function
    • Litvak V, Dahan N, Ramachandran S, Sabanay H, Lev S. Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat Cell Biol 7: 225-234, 2005.
    • (2005) Nat Cell Biol , vol.7 , pp. 225-234
    • Litvak, V.1    Dahan, N.2    Ramachandran, S.3    Sabanay, H.4    Lev, S.5
  • 99
    • 18644381102 scopus 로고    scopus 로고
    • Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5bisphosphate
    • Liu B, Zhang C, Qin F. Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5bisphosphate. J Neurosci 25: 4835-4843, 2005.
    • (2005) J Neurosci , vol.25 , pp. 4835-4843
    • Liu, B.1    Zhang, C.2    Qin, F.3
  • 101
    • 34347399046 scopus 로고    scopus 로고
    • The alpha-tocopherol transfer protein
    • Manor D, Morley S. The alpha-tocopherol transfer protein. Vitam Horm 76: 45-65, 2007.
    • (2007) Vitam Horm , vol.76 , pp. 45-65
    • Manor, D.1    Morley, S.2
  • 107
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Meyer T, Oancea E. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 95: 307-318, 1998.
    • (1998) Cell , vol.95 , pp. 307-318
    • Meyer, T.1    Oancea, E.2
  • 109
    • 0016613531 scopus 로고
    • Inositol phospholipids and cell surface receptor function
    • Michell RH. Inositol phospholipids and cell surface receptor function. Biochim Biophys Acta 415: 81-147, 1975.
    • (1975) Biochim Biophys Acta , vol.415 , pp. 81-147
    • Michell, R.H.1
  • 110
    • 0020477276 scopus 로고
    • Is phosphotidylinositol really out of the calcium gate?
    • Michell RH. Is phosphotidylinositol really out of the calcium gate? Nature 296: 492-493, 1982.
    • (1982) Nature , vol.296 , pp. 492-493
    • Michell, R.H.1
  • 111
    • 0014193775 scopus 로고
    • Characteristics of rat liver phosphatidylinositol kinase and its presence in the plasma membrane
    • Michell RH, Harwood JL, Coleman R, Hawthorne JN. Characteristics of rat liver phosphatidylinositol kinase and its presence in the plasma membrane. Biochim Biophys Acta 144: 649-658, 1967.
    • (1967) Biochim Biophys Acta , vol.144 , pp. 649-658
    • Michell, R.H.1    Harwood, J.L.2    Coleman, R.3    Hawthorne, J.N.4
  • 112
    • 14944339213 scopus 로고    scopus 로고
    • Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the refeasable vesicle pool size in chromaffin cells
    • Milosevic I, Sorensen JB, Lang T, Krauss M, Nagy G, Haucke V, Jahn R, Neher E. Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the refeasable vesicle pool size in chromaffin cells. J Neurosci 25: 2557-2565, 2005.
    • (2005) J Neurosci , vol.25 , pp. 2557-2565
    • Milosevic, I.1    Sorensen, J.B.2    Lang, T.3    Krauss, M.4    Nagy, G.5    Haucke, V.6    Jahn, R.7    Neher, E.8
  • 113
    • 33644989853 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor
    • Minogue S, Waugh MG, De Matteis MA, Stephens DJ, Berditchevski F, Hsuan JJ. Phosphatidylinositol 4-kinase is required for endosomal trafficking and degradation of the EGF receptor. J Cell Sci 119: 571-581, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 571-581
    • Minogue, S.1    Waugh, M.G.2    De Matteis, M.A.3    Stephens, D.J.4    Berditchevski, F.5    Hsuan, J.J.6
  • 114
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata Y, Iwasaki H, Sasaki M, Inaba K, Okamura Y. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435: 1239-1243, 2005.
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 115
    • 34548725637 scopus 로고    scopus 로고
    • Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2
    • Murata Y, Okamura Y. Depolarization activates the phosphoinositide phosphatase Ci-VSP, as detected in Xenopus oocytes coexpressing sensors of PIP2. J Physiol 583: 875-889, 2007.
    • (2007) J Physiol , vol.583 , pp. 875-889
    • Murata, Y.1    Okamura, Y.2
  • 116
    • 0029892506 scopus 로고    scopus 로고
    • Cloning, expression and localization of 230 kDa phosphatidylinositol 4-kinase
    • Nakagawa T, Goto K, Kondo H. Cloning, expression and localization of 230 kDa phosphatidylinositol 4-kinase. J Biol Chem 271: 12088-12094, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 12088-12094
    • Nakagawa, T.1    Goto, K.2    Kondo, H.3
  • 118
    • 55549104701 scopus 로고    scopus 로고
    • Transient receptor potential channels meet phosphoinositides
    • Nilius B, Owsianik G, Voets T. Transient receptor potential channels meet phosphoinositides. EMBOJ 27: 2809-2816, 2008.
    • (2008) EMBOJ , vol.27 , pp. 2809-2816
    • Nilius, B.1    Owsianik, G.2    Voets, T.3
  • 119
    • 0034743127 scopus 로고    scopus 로고
    • 2 assembles in a mitotically regulated particle involved in pre-mRNA splicing. J Cell Sci 114: 2501-2511, 2001.
    • 2 assembles in a mitotically regulated particle involved in pre-mRNA splicing. J Cell Sci 114: 2501-2511, 2001.
  • 120
    • 0034633643 scopus 로고    scopus 로고
    • Intracellular delivery of phosphoinositides and inositol phosphates using polyamine carriers
    • Ozaki S, DeWald DB, Shope JC, Chen J, Prestwich GD. Intracellular delivery of phosphoinositides and inositol phosphates using polyamine carriers. Proc Natl Acad Sci USA 97: 11286-11291, 2000.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11286-11291
    • Ozaki, S.1    DeWald, D.B.2    Shope, J.C.3    Chen, J.4    Prestwich, G.D.5
  • 121
    • 0031026639 scopus 로고    scopus 로고
    • Characterization of p150, an adaptor protein for the human phosphatidylinositol (Ptolns) 3kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150/Ptdlns 3kinase complex
    • Panaretou C, Domin J, Cockcroft S, Waterfield MD. Characterization of p150, an adaptor protein for the human phosphatidylinositol (Ptolns) 3kinase. Substrate presentation by phosphatidylinositol transfer protein to the p150/Ptdlns 3kinase complex. J Biol Chem 111: 2477-2485, 1997.
    • (1997) J Biol Chem , vol.111 , pp. 2477-2485
    • Panaretou, C.1    Domin, J.2    Cockcroft, S.3    Waterfield, M.D.4
  • 123
    • 3342909622 scopus 로고    scopus 로고
    • Essential role for the myotubularin-related phosphatase Ymr1p and the synaptojanin-like phosphatases Sjl2p and Sj13p in regulation of phosphatidylinositol 3-phosphate in yeast
    • Parrish WR, Stefan CJ, Emr SD. Essential role for the myotubularin-related phosphatase Ymr1p and the synaptojanin-like phosphatases Sjl2p and Sj13p in regulation of phosphatidylinositol 3-phosphate in yeast. Mol Biol Cell 15: 3567-3579, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 3567-3579
    • Parrish, W.R.1    Stefan, C.J.2    Emr, S.D.3
  • 124
  • 125
    • 33744728346 scopus 로고    scopus 로고
    • Oxysterol-binding protein and VAMP-associated protein are required for sterol-dependent activation of the ceramide transport protein
    • Perry RJ, Ridgway ND. Oxysterol-binding protein and VAMP-associated protein are required for sterol-dependent activation of the ceramide transport protein. Mol Biol Cell 17: 2604-2616, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 126
    • 33744751509 scopus 로고    scopus 로고
    • Specific and nonspecific membranebinding determinants cooperate in targeting phosphatidylinositol transfer protein beta-isoform to the mammalian trans-Golgi network
    • Phillips SE, Ile KE, Boukhelifa M, Huijbregts RP, Bankaitis VA. Specific and nonspecific membranebinding determinants cooperate in targeting phosphatidylinositol transfer protein beta-isoform to the mammalian trans-Golgi network. Mol Biol Cell 17: 2498-2512, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 2498-2512
    • Phillips, S.E.1    Ile, K.E.2    Boukhelifa, M.3    Huijbregts, R.P.4    Bankaitis, V.A.5
  • 127
    • 0024415927 scopus 로고
    • Mass changes in inositol tetrakis- and pentakisphosphate isomers induced by chemotactic peptide stimulation in HL-60 cells
    • Pittet D, Schlegel W, Lew DP, Monod A, Mayr GW. Mass changes in inositol tetrakis- and pentakisphosphate isomers induced by chemotactic peptide stimulation in HL-60 cells. J Biol Chem 264: 18489-18493, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 18489-18493
    • Pittet, D.1    Schlegel, W.2    Lew, D.P.3    Monod, A.4    Mayr, G.W.5
  • 128
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard TD. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu Rev Biophys Biomol Struct 36: 451-477, 2007.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 129
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney JW Jr. A model for receptor-regulated calcium entry. Cell Calcium 1: 1-12, 1986.
    • (1986) Cell Calcium , vol.1 , pp. 1-12
    • Putney Jr., J.W.1
  • 130
    • 34347345599 scopus 로고    scopus 로고
    • Recent breakthroughs in the molecular mechanism of capacitative calcium entry (with thoughts on how we got here)
    • Putney JW Jr. Recent breakthroughs in the molecular mechanism of capacitative calcium entry (with thoughts on how we got here). Cell Calcium 42: 103-110, 2007.
    • (2007) Cell Calcium , vol.42 , pp. 103-110
    • Putney Jr., J.W.1
  • 131
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding proteinrelated proteins and phosphoinositides
    • Raychaudhuri S, Im YJ, Hurley JH, Prinz WA. Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding proteinrelated proteins and phosphoinositides. J Cell Biol 173: 107-119, 2006.
    • (2006) J Cell Biol , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prinz, W.A.4
  • 132
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi MJ, Pentyala SN. Structure, function, and control of phosphoinositide-specific phospholipase C. Phys Rev 80: 1291-1335, 2000.
    • (2000) Phys Rev , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 133
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee SG. Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem 70: 281-312, 2001.
    • (2001) Annu Rev Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 134
    • 67349183758 scopus 로고    scopus 로고
    • Phosphoinositide regulation of noncanonical transient receptor potential channels
    • Rohacs T. Phosphoinositide regulation of noncanonical transient receptor potential channels. Cell Calcium 45: 554-565, 2009.
    • (2009) Cell Calcium , vol.45 , pp. 554-565
    • Rohacs, T.1
  • 135
    • 17844373771 scopus 로고    scopus 로고
    • Rohacs T, Lopes CM, Michailidis I, Logothetis DE. PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain. Nat Neurosci 8: 626-634, 2005.
    • Rohacs T, Lopes CM, Michailidis I, Logothetis DE. PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain. Nat Neurosci 8: 626-634, 2005.
  • 136
    • 0037157830 scopus 로고    scopus 로고
    • A phosphatidylinositol (4,5)-bisphosphate binding site within mu2-adaptin regulates clathrin-mediated endocytosis
    • Rohde G, Wenzel D, Haucke V. A phosphatidylinositol (4,5)-bisphosphate binding site within mu2-adaptin regulates clathrin-mediated endocytosis. J Cell Biol 158: 209-214, 2002.
    • (2002) J Cell Biol , vol.158 , pp. 209-214
    • Rohde, G.1    Wenzel, D.2    Haucke, V.3
  • 137
    • 27744604253 scopus 로고    scopus 로고
    • Nonclassical PITPs activate PLD via the Stt4p Ptdlns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast
    • Routt SM, Ryan MM, Tyeryar K, Rizzieri KE, Mousley C, Roumanie O, Brennwald PJ, Bankaitis VA. Nonclassical PITPs activate PLD via the Stt4p Ptdlns-4-kinase and modulate function of late stages of exocytosis in vegetative yeast. Traffic 6: 1157-1172, 2005.
    • (2005) Traffic , vol.6 , pp. 1157-1172
    • Routt, S.M.1    Ryan, M.M.2    Tyeryar, K.3    Rizzieri, K.E.4    Mousley, C.5    Roumanie, O.6    Brennwald, P.J.7    Bankaitis, V.A.8
  • 138
    • 7244248722 scopus 로고    scopus 로고
    • Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p
    • Roy A, Levine TP. Multiple pools of phosphatidylinositol 4-phosphate detected using the pleckstrin homology domain of Osh2p. J Biol Chem 279: 44683-44689, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 44683-44689
    • Roy, A.1    Levine, T.P.2
  • 142
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, Emr SD. Phosphatidylinositol 3kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260: 88-91, 1993.
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 143
    • 34548120595 scopus 로고    scopus 로고
    • Roles for inositol polyphosphate kinases in the regulation of nuclear processes and developmental biology
    • Seeds AM, Frederick JP, Tsui MM, York JD. Roles for inositol polyphosphate kinases in the regulation of nuclear processes and developmental biology. Adv Enzyme Regul 47: 10-25, 2007.
    • (2007) Adv Enzyme Regul , vol.47 , pp. 10-25
    • Seeds, A.M.1    Frederick, J.P.2    Tsui, M.M.3    York, J.D.4
  • 144
    • 0034635513 scopus 로고    scopus 로고
    • Polarization of chemoattractant receptor signaling during neutrophil Chemotaxis
    • Servant G, Weiner OD, Herzmark P, Balla T, Sedat JW, Bourne HR. Polarization of chemoattractant receptor signaling during neutrophil Chemotaxis. Science 287: 1037-1040, 2000.
    • (2000) Science , vol.287 , pp. 1037-1040
    • Servant, G.1    Weiner, O.D.2    Herzmark, P.3    Balla, T.4    Sedat, J.W.5    Bourne, H.R.6
  • 145
    • 0005721829 scopus 로고    scopus 로고
    • Measurement of inositol phosphate turnover in intact cells and cell-free systems
    • Oxford, UK: Oxford Univ. Press
    • Shears SB. Measurement of inositol phosphate turnover in intact cells and cell-free systems. In: Signalling by Inositides. A Paractical Approach. Oxford, UK: Oxford Univ. Press, 1997, p. 33-53.
    • (1997) Signalling by Inositides. A Paractical Approach , pp. 33-53
    • Shears, S.B.1
  • 147
    • 43249117879 scopus 로고    scopus 로고
    • PlKfyve: Partners, significance, debates and paradoxes
    • Shisheva A. PlKfyve: partners, significance, debates and paradoxes. Cell Biol Int 32: 591-604, 2008.
    • (2008) Cell Biol Int , vol.32 , pp. 591-604
    • Shisheva, A.1
  • 148
    • 0032907207 scopus 로고    scopus 로고
    • 2+-binding FYVE finger-containing phosphoinositide kinase in insulin-sensitive cells
    • 2+-binding FYVE finger-containing phosphoinositide kinase in insulin-sensitive cells. Mol Cell Biol 19: 623-634, 1999.
    • (1999) Mol Cell Biol , vol.19 , pp. 623-634
    • Shisheva, A.1    Sbrissa, D.2    Ikonomov, O.3
  • 150
    • 0023918648 scopus 로고
    • Determination of inositol phosphates and other biologically important anions by ion chromatography
    • Smith RE, MacQuarrie RA. Determination of inositol phosphates and other biologically important anions by ion chromatography. Anal Biochem 170: 308-315, 1988.
    • (1988) Anal Biochem , vol.170 , pp. 308-315
    • Smith, R.E.1    MacQuarrie, R.A.2
  • 151
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane Ptdlns(4,5)P, concentration monitored in living cells
    • Stauffer TP, Ahn S, Meyer T. Receptor-induced transient reduction in plasma membrane Ptdlns(4,5)P, concentration monitored in living cells. Curr Biol 8: 343-346, 1998.
    • (1998) Curr Biol , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 153
    • 29144458344 scopus 로고    scopus 로고
    • Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus
    • Strahl T, Hama H, Dewald DB, Thorner J. Yeast phosphatidylinositol 4-kinase, Pik1, has essential roles at the Golgi and in the nucleus. J Cell Biol 171: 967-979, 2005.
    • (2005) J Cell Biol , vol.171 , pp. 967-979
    • Strahl, T.1    Hama, H.2    Dewald, D.B.3    Thorner, J.4
  • 154
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 306: 67-68, 1983.
    • (1983) Nature , vol.306 , pp. 67-68
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 155
    • 48249116482 scopus 로고    scopus 로고
    • PIP2 is a necessary cofactor for ion channel function: How and why?
    • Suh BC, Hille B. PIP2 is a necessary cofactor for ion channel function: how and why? Annu Rev Biophys 37: 175-195, 2008.
    • (2008) Annu Rev Biophys , vol.37 , pp. 175-195
    • Suh, B.C.1    Hille, B.2
  • 156
    • 33845310879 scopus 로고    scopus 로고
    • Rapid chemically induced changes of Ptdlns(4,5)P, gate KCNQ ion channels
    • Suh BC, Inoue T, Meyer T, Hille B. Rapid chemically induced changes of Ptdlns(4,5)P, gate KCNQ ion channels. Science 314: 1454-1457, 2006.
    • (2006) Science , vol.314 , pp. 1454-1457
    • Suh, B.C.1    Inoue, T.2    Meyer, T.3    Hille, B.4
  • 158
    • 0027185354 scopus 로고
    • An essential role of phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling
    • Thomas GMH, Cunningham E, Fensome A, Ball A, Totty NF, Truong O, Hsuan JJ, Cockcroft S. An essential role of phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling. Cell 74: 919-928, 1993.
    • (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
  • 159
    • 33846005514 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase lllbeta regulates the transport of ceramide between the endoplasmic reticulum and Golgi
    • Toth B, Balla A, Ma H, Knight ZA, Shokat KM, Balla T. Phosphatidylinositol 4-kinase lllbeta regulates the transport of ceramide between the endoplasmic reticulum and Golgi. J Biol Chem 281: 36369-36377, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 36369-36377
    • Toth, B.1    Balla, A.2    Ma, H.3    Knight, Z.A.4    Shokat, K.M.5    Balla, T.6
  • 161
    • 0242351932 scopus 로고    scopus 로고
    • Implication of phosphoinositide phosphatases in genetic diseases: The case of myotubularin
    • Tronchere H, Buj-Bello A, Mandel JL, Payrastre B. Implication of phosphoinositide phosphatases in genetic diseases: the case of myotubularin. Cell Mol Life Sci 10: 2084-2089, 2003.
    • (2003) Cell Mol Life Sci , vol.10 , pp. 2084-2089
    • Tronchere, H.1    Buj-Bello, A.2    Mandel, J.L.3    Payrastre, B.4
  • 162
    • 0032557556 scopus 로고    scopus 로고
    • A genetic screen for aminophospholipid transport mutants identifies the pnospnatidylinositol 4kinase, Stt4p, as an essential component in phosphatidylserine metabolism
    • Trotter PJ, Wu WI, Pedretti J, Yates R, Voelker DR. A genetic screen for aminophospholipid transport mutants identifies the pnospnatidylinositol 4kinase, Stt4p, as an essential component in phosphatidylserine metabolism. J Biol Chem 273: 13189-13196, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 13189-13196
    • Trotter, P.J.1    Wu, W.I.2    Pedretti, J.3    Yates, R.4    Voelker, D.R.5
  • 166
    • 33748333139 scopus 로고    scopus 로고
    • Live cell imaging of phosphoinositide dynamics with fluorescent protein domains
    • Varnai P, Balla T. Live cell imaging of phosphoinositide dynamics with fluorescent protein domains. Biochim Biophys Acta 1761: 957-967, 2006.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 957-967
    • Varnai, P.1    Balla, T.2
  • 167
    • 0032547744 scopus 로고    scopus 로고
    • 3H]inositol-labeled phosphoinositide pools
    • 3H]inositol-labeled phosphoinositide pools. J Cell Biol 143: 501-510, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 501-510
    • Várnai, P.1    Balla, T.2
  • 168
    • 0345561543 scopus 로고    scopus 로고
    • Phosphatidylinositol 3kinase-dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells
    • Varnai P, Rother KI, Balla T. Phosphatidylinositol 3kinase-dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells. J Biol Chem 274: 10983-10989, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 10983-10989
    • Varnai, P.1    Rother, K.I.2    Balla, T.3
  • 169
    • 33750730911 scopus 로고    scopus 로고
    • Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells
    • Varnai P, Thyagarajan B, Rohacs T, Balla T. Rapidly inducible changes in phosphatidylinositol 4,5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells. J Cell Biol 175: 377-382, 2006.
    • (2006) J Cell Biol , vol.175 , pp. 377-382
    • Varnai, P.1    Thyagarajan, B.2    Rohacs, T.3    Balla, T.4
  • 170
    • 35748956408 scopus 로고    scopus 로고
    • Visualization and manipulation of plasma membrane-endoplasmic reticulum contact sites indicates the presence of additional molecular components within the STIM1 -Orail Complex
    • Varnai P, Toth B, Toth DJ, Hunyady L, Balla T. Visualization and manipulation of plasma membrane-endoplasmic reticulum contact sites indicates the presence of additional molecular components within the STIM1 -Orail Complex. J Biol Chem 282: 29678-29690, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 29678-29690
    • Varnai, P.1    Toth, B.2    Toth, D.J.3    Hunyady, L.4    Balla, T.5
  • 172
    • 20844440571 scopus 로고    scopus 로고
    • Verbsky J, Lavine K, Majerus PW. Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2kinase gene, associated lethality, and tissue distribution of 2-kinase expression. Proc Natl Acad Sci USA 102: 8448-8453, 2005.
    • Verbsky J, Lavine K, Majerus PW. Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2kinase gene, associated lethality, and tissue distribution of 2-kinase expression. Proc Natl Acad Sci USA 102: 8448-8453, 2005.
  • 173
    • 33845487091 scopus 로고    scopus 로고
    • FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells
    • Vieira OV, Gaus K, Verkade P, Fullekrug J, Vaz WL, Simons K. FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells. Proc Natl Acad Sci USA 103: 18556-18561, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18556-18561
    • Vieira, O.V.1    Gaus, K.2    Verkade, P.3    Fullekrug, J.4    Vaz, W.L.5    Simons, K.6
  • 174
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Vieira OV, Verkade P, Simons K. FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J Cell Biol 170: 521-526, 2005.
    • (2005) J Cell Biol , vol.170 , pp. 521-526
    • Vieira, O.V.1    Verkade, P.2    Simons, K.3
  • 176
    • 0026722645 scopus 로고
    • 2+-regulated secretion in permeable neuroendocrine cells
    • 2+-regulated secretion in permeable neuroendocrine cells. Cell 70: 765-775, 1992.
    • (1992) Cell , vol.70 , pp. 765-775
    • Walent, J.H.1    Porter, B.W.2    Martin, T.F.3
  • 177
    • 34347382638 scopus 로고    scopus 로고
    • PI4P Promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal
    • Wang J, Sun HQ, Macia E, Kirchhausen T, Watson H, Bonifacino JS, Yin HL. PI4P Promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal. Mol Biol Cell 18: 2646-2655, 2007.
    • (2007) Mol Biol Cell , vol.18 , pp. 2646-2655
    • Wang, J.1    Sun, H.Q.2    Macia, E.3    Kirchhausen, T.4    Watson, H.5    Bonifacino, J.S.6    Yin, H.L.7
  • 180
    • 0036566427 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1
    • Watt SA, Kular G, Fleming IN, Downes CP, Lucocq JM. Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1. 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
  • 181
    • 2942623783 scopus 로고    scopus 로고
    • Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: Insights from vesicle recycling in nerve terminals
    • Wenk MR, De Camilli P. Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: insights from vesicle recycling in nerve terminals. Proc Natl Acad Sci USA 101: 8262-8269, 2004.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8262-8269
    • Wenk, M.R.1    De Camilli, P.2
  • 183
    • 0030989280 scopus 로고    scopus 로고
    • Subcellular localization of phosphatidylinositol 4-kinase isoforms
    • Wong K, Meyers R, Cantley LC. Subcellular localization of phosphatidylinositol 4-kinase isoforms. J Biol Chem 272: 13236-13241, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 13236-13241
    • Wong, K.1    Meyers, R.2    Cantley, L.C.3
  • 185
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin HL, Janmey PA. Phosphoinositide regulation of the actin cytoskeleton. Annu Rev Physiol 65: 761-789, 2003.
    • (2003) Annu Rev Physiol , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 186
    • 0033516604 scopus 로고    scopus 로고
    • A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
    • York JD, Odom AR, Murphy R, Ives EB, Wente SR. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285: 96-100, 1999.
    • (1999) Science , vol.285 , pp. 96-100
    • York, J.D.1    Odom, A.R.2    Murphy, R.3    Ives, E.B.4    Wente, S.R.5
  • 188
    • 58149161452 scopus 로고    scopus 로고
    • Ypp1/YGR198w plays an essential role in phosphoinositide signalling at the plasma membrane
    • Zhai C, Li K, Markaki V, Phelan JP, Bowers K, Cooke FT, Panaretou B. Ypp1/YGR198w plays an essential role in phosphoinositide signalling at the plasma membrane. Biochem J 415: 455-466, 2008.
    • (2008) Biochem J , vol.415 , pp. 455-466
    • Zhai, C.1    Li, K.2    Markaki, V.3    Phelan, J.P.4    Bowers, K.5    Cooke, F.T.6    Panaretou, B.7
  • 189
    • 0035955738 scopus 로고    scopus 로고
    • Interaction of neuronal calcium sensor-1 (NCS-1) with phosphatidylinositol 4-kinase beta stimulates lipid kinase activity and affects membrane trafficking in COS-7 cells
    • Zhao X, Varnai P, Tuymetova G, Balla A, Toth ZE, Oker-Blom C, Roder J, Jeromin A, Balla T. Interaction of neuronal calcium sensor-1 (NCS-1) with phosphatidylinositol 4-kinase beta stimulates lipid kinase activity and affects membrane trafficking in COS-7 cells. J Biol Chem 276: 40183-40189, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 40183-40189
    • Zhao, X.1    Varnai, P.2    Tuymetova, G.3    Balla, A.4    Toth, Z.E.5    Oker-Blom, C.6    Roder, J.7    Jeromin, A.8    Balla, T.9
  • 190
    • 62549151303 scopus 로고    scopus 로고
    • A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes
    • Zoncu R, Perera RM, Balkin DM, Pirruccello M, Toomre D, De Camilli P. A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Cell 136: 1110-1121, 2009.
    • (2009) Cell , vol.136 , pp. 1110-1121
    • Zoncu, R.1    Perera, R.M.2    Balkin, D.M.3    Pirruccello, M.4    Toomre, D.5    De Camilli, P.6


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