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Volumn 10, Issue 2, 1998, Pages 254-261

The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PHOSPHOLIPID; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE;

EID: 0032053708     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80148-8     Document Type: Article
Times cited : (250)

References (63)
  • 2
    • 16944365378 scopus 로고    scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinases are distinct members of this novel lipid kinase family
    • Loijens JC, Anderson RA. Type I phosphatidylinositol 4-phosphate 5-kinases are distinct members of this novel lipid kinase family. J Biol Chem. 271:1996;32937-32943.
    • (1996) J Biol Chem , vol.271 , pp. 32937-32943
    • Loijens, J.C.1    Anderson, R.A.2
  • 3
    • 0028218165 scopus 로고
    • Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae
    • Yoshida S, Ohya Y, Nakano A, Anraku Y. Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae. Mol Gen Genet. 242:1994;631-640.
    • (1994) Mol Gen Genet , vol.242 , pp. 631-640
    • Yoshida, S.1    Ohya, Y.2    Nakano, A.3    Anraku, Y.4
  • 4
  • 7
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker A, Cantley LC. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:1997;673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 8
    • 0030944761 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate defines a novel PI 3-kinase pathway in resting mouse fibroblasts
    • 2, exists. Pulse labeling experiments in fibroblasts suggest that the majority of this lipid is generated by phosphorylation of Ptdlns 3-P at the D5 position, presumably by a PI 5-K. See also [9].
    • 2, exists. Pulse labeling experiments in fibroblasts suggest that the majority of this lipid is generated by phosphorylation of Ptdlns 3-P at the D5 position, presumably by a PI 5-K. See also [9].
    • (1997) Biochem J , vol.323 , pp. 597-601
    • Whiteford, C.C.1    Brearley, C.A.2    Ulug, E.T.3
  • 9
    • 0030669546 scopus 로고    scopus 로고
    • Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis
    • 2 in yeasts, plant and mammalian cells suggests that it may play an important role in functions such as vesicular sorting.
    • 2 in yeasts, plant and mammalian cells suggests that it may play an important role in functions such as vesicular sorting.
    • (1997) Nature , 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
  • 10
    • 0028812255 scopus 로고
    • The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases
    • Boronenkov IV, Anderson RA. The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases. J Biol Chem. 270:1995;2881-2884.
    • (1995) J Biol Chem , vol.270 , pp. 2881-2884
    • Boronenkov, I.V.1    Anderson, R.A.2
  • 14
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee SG, Bae YS. Regulation of phosphoinositide-specific phospholipase C isozymes. J Biol Chem. 272:1997;15045-15048.
    • (1997) J Biol Chem , vol.272 , pp. 15045-15048
    • Rhee, S.G.1    Bae, Y.S.2
  • 15
    • 0001169160 scopus 로고    scopus 로고
    • Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid
    • Hwang SC, Jhon DY, Bae YS, Kim JH, Rhee SG. Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid. J Biol Chem. 271:1996;18342-18349.
    • (1996) J Biol Chem , vol.271 , pp. 18342-18349
    • Hwang, S.C.1    Jhon, D.Y.2    Bae, Y.S.3    Kim, J.H.4    Rhee, S.G.5
  • 16
    • 0027310309 scopus 로고
    • Proteolytic fragments of phosphoinositide-specific phospholipase C-delta 1. Catalytic and membrane binding properties
    • Cifuentes ME, Honkanen L, Rebecchi MJ. Proteolytic fragments of phosphoinositide-specific phospholipase C-delta 1. Catalytic and membrane binding properties. J Biol Chem. 268:1993;11586-11593.
    • (1993) J Biol Chem , vol.268 , pp. 11586-11593
    • Cifuentes, M.E.1    Honkanen, L.2    Rebecchi, M.J.3
  • 17
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol triphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Structure of the high affinity complex of inositol triphosphate with a phospholipase C pleckstrin homology domain. Cell. 83:1995;1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 18
    • 0029795505 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-delta1 enhances enzyme activity
    • Lomasney JW, Cheng HF, Wang LP, Kuan Y, Liu S, Fesik SW, King K. Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-delta1 enhances enzyme activity. J Biol Chem. 271:1996;25316-25326.
    • (1996) J Biol Chem , vol.271 , pp. 25316-25326
    • Lomasney, J.W.1    Cheng, H.F.2    Wang, L.P.3    Kuan, Y.4    Liu, S.5    Fesik, S.W.6    King, K.7
  • 22
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey P. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu Rev Physiol. 56:1994;169-191.
    • (1994) Annu Rev Physiol , vol.56 , pp. 169-191
    • Janmey, P.1
  • 23
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig JH, Bokoch GM, Carpenter CL, Janmey PA, Taylor LA, Toker A, Stossel TP. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:1995;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
  • 24
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias KF, Cantley LC, Carpenter CL. Rho family GTPases bind to phosphoinositide kinases. J Biol Chem. 270:1995;17656-17659.
    • (1995) J Biol Chem , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 25
    • 0031882760 scopus 로고    scopus 로고
    • Characterization of a rac-1 and RhoGDI-associated lipid kinase signaling complex
    • Tolias KF, Couvillon AD, Cantley LC, Carpenter CL. Characterization of a rac-1 and RhoGDI-associated lipid kinase signaling complex. Mol Cell Biol. 18:1997;762-770.
    • (1997) Mol Cell Biol , vol.18 , pp. 762-770
    • Tolias, K.F.1    Couvillon, A.D.2    Cantley, L.C.3    Carpenter, C.L.4
  • 26
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong LD, Traynor KA, Bokoch GM, Schwartz MA. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell. 79:1994;507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor, K.A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 27
    • 0031004866 scopus 로고    scopus 로고
    • Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo
    • of special interest. Expression of the type I PI 5-K in COS-7 cells leads to a dramatic increase in actin polymerization. Co-expression studies with dominant negative Rho suggest that the PI 5-K activity is downstream of this GTPase, as previously reported [26].
    • Shibasaki Y, Ishihara H, Kizuki N, Asano T, Oka Y, Yazaki Y. Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo. of special interest J Biol Chem. 272:1997;7578-7581 Expression of the type I PI 5-K in COS-7 cells leads to a dramatic increase in actin polymerization. Co-expression studies with dominant negative Rho suggest that the PI 5-K activity is downstream of this GTPase, as previously reported [26].
    • (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
  • 28
    • 0030981640 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments
    • 2 phosphatase activity is not inhibited by actin-binding proteins such as profilin, indicating that synaptojanin hydrolyzes lipid bound to these proteins.
    • 2 phosphatase activity is not inhibited by actin-binding proteins such as profilin, indicating that synaptojanin hydrolyzes lipid bound to these proteins.
    • (1997) Mol Cell Biol , vol.17 , pp. 3841-3849
    • Sakisaka, T.1    Itoh, T.2    Miura, K.3    Takenawa, T.4
  • 29
    • 0029827247 scopus 로고    scopus 로고
    • 2 (4,5) levels in human platelets are controlled by translocation of Ptdlns 4-P 5-kinase C to the cytoskeleton
    • 2 associated with the cytoskeleton.
    • 2 associated with the cytoskeleton.
    • (1996) EMBO J , vol.15 , pp. 6516-6524
    • Hinchliffe, K.A.1    Irvine, R.F.2    Divecha, N.3
  • 30
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol. 135:1996;37-51.
    • (1996) J Cell Biol , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 31
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai Y. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J Biol Chem. 272:1997;23371-23375.
    • (1997) J Biol Chem , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Takai, Y.7
  • 32
    • 0030872949 scopus 로고    scopus 로고
    • Rho- And rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • of special interest. A cytosol reconstitution assay is used to identify an activity responsible for actin filament assembly through activation of the GTPase Rho and Rac. Purification studies indicate that this activity is moesin, a member of the ERM family of proteins. In combination with [30,31,33], these studies indicate that ERM proteins act as effectors of small GTPases to reorganize the actin filament network.
    • Mackay DJ, Esch F, Furthmayr H, Hall A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. of special interest J Cell Biol. 138:1997;927-938 A cytosol reconstitution assay is used to identify an activity responsible for actin filament assembly through activation of the GTPase Rho and Rac. Purification studies indicate that this activity is moesin, a member of the ERM family of proteins. In combination with [30,31,33], these studies indicate that ERM proteins act as effectors of small GTPases to reorganize the actin filament network.
    • (1997) J Cell Biol , vol.138 , pp. 927-938
    • MacKay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 33
    • 0031240066 scopus 로고    scopus 로고
    • Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts
    • of special interest. Transformation of fibroblasts leads to increase ezrin expression and increased phosphorylation of ezrin associated with the actin cytoskeleton (particularly at the leading edge of the cell). A link between ezrin function and localization with oncogenic transformation is suggested.
    • Lamb RF, Ozanne BW, Roy C, McGarry L, Stipp C, Mangeat P, Jay DG. Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts. of special interest Curr Biol. 7:1997;682-688 Transformation of fibroblasts leads to increase ezrin expression and increased phosphorylation of ezrin associated with the actin cytoskeleton (particularly at the leading edge of the cell). A link between ezrin function and localization with oncogenic transformation is suggested.
    • (1997) Curr Biol , vol.7 , pp. 682-688
    • Lamb, R.F.1    Ozanne, B.W.2    Roy, C.3    McGarry, L.4    Stipp, C.5    Mangeat, P.6    Jay, D.G.7
  • 34
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M, Derry JM, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell. 84:1996;723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 35
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerization protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki H, Miura K, Takenawa T. N-WASP, a novel actin-depolymerization protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15:1996;5326-5335.
    • (1996) EMBO J , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 36
    • 0030998128 scopus 로고    scopus 로고
    • Pleckstrin associates with plasma membranes and induces the formation of membrane projections: Requirements for phosphorylation and the NH2-terminal PH domain
    • Ma AD, Brass LF, Abrams CS. Pleckstrin associates with plasma membranes and induces the formation of membrane projections: requirements for phosphorylation and the NH2-terminal PH domain. J Cell Biol. 136:1997;1071-1079.
    • (1997) J Cell Biol , vol.136 , pp. 1071-1079
    • Ma, A.D.1    Brass, L.F.2    Abrams, C.S.3
  • 37
    • 0029087181 scopus 로고
    • Structural characterization of the interaction between a pleckstrin homology domain and phosphatidylinositol 4,5-bisphosphate
    • Harlan JE, Yoon HS, Hajduk PJ, Fesik SW. Structural characterization of the interaction between a pleckstrin homology domain and phosphatidylinositol 4,5-bisphosphate. Biochemistry. 34:1995;9859-9864.
    • (1995) Biochemistry , vol.34 , pp. 9859-9864
    • Harlan, J.E.1    Yoon, H.S.2    Hajduk, P.J.3    Fesik, S.W.4
  • 38
    • 10244224044 scopus 로고    scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains
    • Glaser M, Wanaski S, Buser CA, Boguslavsky V, Rashidzada W, Morris A, Rebecchi M, Scarlata SF, Runnels LW, Prestwich GD, et al. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains. J Biol Chem. 271:1996;26187-26193.
    • (1996) J Biol Chem , vol.271 , pp. 26187-26193
    • Glaser, M.1    Wanaski, S.2    Buser, C.A.3    Boguslavsky, V.4    Rashidzada, W.5    Morris, A.6    Rebecchi, M.7    Scarlata, S.F.8    Runnels, L.W.9    Prestwich, G.D.10
  • 39
    • 0027965240 scopus 로고
    • Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D
    • Liscovitch M, Chalifa V, Pertile P, Chen CS, Cantley LC. Novel function of phosphatidylinositol 4,5-bisphosphate as a cofactor for brain membrane phospholipase D. J Biol Chem. 269:1994;21403-21406.
    • (1994) J Biol Chem , vol.269 , pp. 21403-21406
    • Liscovitch, M.1    Chalifa, V.2    Pertile, P.3    Chen, C.S.4    Cantley, L.C.5
  • 40
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown HA, Gutowski S, Moomaw CR, Slaughter C, Sternweis PC. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell. 75:1993;1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 41
    • 0028278346 scopus 로고
    • GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids
    • Randazzo PA, Kahn RA. GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids. J Biol Chem. 269:1994;10758-10763.
    • (1994) J Biol Chem , vol.269 , pp. 10758-10763
    • Randazzo, P.A.1    Kahn, R.A.2
  • 42
    • 0030944208 scopus 로고    scopus 로고
    • Functional interaction of ADP-ribosylation factor 1 with phosphatidylinositol 4,5-bisphosphate
    • 2:ARF1 complex directs the interaction with GAP. A model is proposed in which ARF1 may sense the lipid environment leading to interactions with specific proteins, and directing membrane traffic.
    • 2:ARF1 complex directs the interaction with GAP. A model is proposed in which ARF1 may sense the lipid environment leading to interactions with specific proteins, and directing membrane traffic.
    • (1997) J Biol Chem , vol.272 , pp. 7688-7692
    • Randazzo, P.A.1
  • 43
    • 0029844904 scopus 로고    scopus 로고
    • A human exchange factor for ARF contains Sec7 and PH domains
    • 2. Subsequent studies [46] show that lipid binding may serve to localize the protein, without directly affecting its exchange activity.
    • 2. Subsequent studies [46] show that lipid binding may serve to localize the protein, without directly affecting its exchange activity.
    • (1996) Nature , vol.384 , pp. 481-484
    • Chardin, P.1    Paris, S.2    Antonny, B.3    Robineau, S.4    Beraud-Dufour, S.5    Jackson, C.L.6    Chabre, M.7
  • 44
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund JK, Guilherme A, Holik JJ, Virbasius JV, Chawla A, Czech MP. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science. 275:1997;1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 45
    • 0030602819 scopus 로고    scopus 로고
    • Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
    • Kolanus W, Nagel W, Schiller B, Zeitlmann L, Godar S, Stockinger H, Seed B. Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell. 86:1996;233-242.
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3    Zeitlmann, L.4    Godar, S.5    Stockinger, H.6    Seed, B.7
  • 46
    • 1842416568 scopus 로고    scopus 로고
    • Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno
    • Paris S, Beraud-Dufour S, Robineau S, Bigay J, Antonny B, Chabre M, Chardin P. Role of protein-phospholipid interactions in the activation of ARF1 by the guanine nucleotide exchange factor Arno. J Biol Chem. 272:1997;22221-22226.
    • (1997) J Biol Chem , vol.272 , pp. 22221-22226
    • Paris, S.1    Beraud-Dufour, S.2    Robineau, S.3    Bigay, J.4    Antonny, B.5    Chabre, M.6    Chardin, P.7
  • 48
    • 0030156660 scopus 로고    scopus 로고
    • ARF and PITP restore GTP gamma S-stimulated protein secretion from cytosol-depleted HL60 cells by promoting PIP2 synthesis
    • Fensome A, Cunningham E, Prosser S, Tan SK, Swigart P, Thomas G, Hsuan J, Cockcroft S. ARF and PITP restore GTP gamma S-stimulated protein secretion from cytosol-depleted HL60 cells by promoting PIP2 synthesis. Curr Biol. 6:1996;730-738.
    • (1996) Curr Biol , vol.6 , pp. 730-738
    • Fensome, A.1    Cunningham, E.2    Prosser, S.3    Tan, S.K.4    Swigart, P.5    Thomas, G.6    Hsuan, J.7    Cockcroft, S.8
  • 49
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis VA, Aitken JR, Cleves AE, Dowhan W. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature. 347:1990;561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 50
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature. 371:1994;168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 51
    • 0030040967 scopus 로고    scopus 로고
    • The pleckstrin homology domain: An intriguing multifunctional protein module
    • Shaw G. The pleckstrin homology domain: an intriguing multifunctional protein module. Bioessays. 18:1996;35-46.
    • (1996) Bioessays , vol.18 , pp. 35-46
    • Shaw, G.1
  • 52
    • 15144349594 scopus 로고    scopus 로고
    • High affinity binding of the pleckstrin homology domain of mSos1 to phosphatidylinositol (4,5)-bisphosphate
    • Kubiseski TJ, Chook YM, Parris WE, Rozakis-Adcock M, Pawson T. High affinity binding of the pleckstrin homology domain of mSos1 to phosphatidylinositol (4,5)-bisphosphate. J Biol Chem. 272:1997;1799-1804.
    • (1997) J Biol Chem , vol.272 , pp. 1799-1804
    • Kubiseski, T.J.1    Chook, Y.M.2    Parris, W.E.3    Rozakis-Adcock, M.4    Pawson, T.5
  • 53
    • 0031002348 scopus 로고    scopus 로고
    • The role of the PH domain in the signal-dependent membrane targeting of Sos
    • 2-binding to the SOS PH domain appears to be dispensable for localization, as mutants deficient in lipid binding still localize at the membrane.
    • 2-binding to the SOS PH domain appears to be dispensable for localization, as mutants deficient in lipid binding still localize at the membrane.
    • (1997) EMBO J , vol.16 , pp. 1351-1359
    • Chen, R.H.1    Corbalan-Garcia, S.2    Bar-Sagi, D.3
  • 54
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the pH domain of dynamin: Implications for stimulation of GTPase activity
    • Zheng J, Cahill SM, Lemmon MA, Fushman D, Schlessinger J, Cowburn D. Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity. J Mol Biol. 255:1996;14-21.
    • (1996) J Mol Biol , vol.255 , pp. 14-21
    • Zheng, J.1    Cahill, S.M.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6
  • 55
    • 0001351392 scopus 로고    scopus 로고
    • Regulation of dynamin I GTPase activity by G protein betagamma subunits and phosphatidylinositol 4,5-bisphosphate
    • Lin HC, Gilman AG. Regulation of dynamin I GTPase activity by G protein betagamma subunits and phosphatidylinositol 4,5-bisphosphate. J Biol Chem. 271:1996;27979-27982.
    • (1996) J Biol Chem , vol.271 , pp. 27979-27982
    • Lin, H.C.1    Gilman, A.G.2
  • 56
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid
    • Pitcher JA, Touhara K, Payne ES, Lefkowitz RJ. Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid. J Biol Chem. 270:1995;11707-11710.
    • (1995) J Biol Chem , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 57
    • 0029788099 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase GRK2 is a phospholipid-dependent enzyme that can be conditionally activated by G protein betagamma subunits
    • DebBurman SK, Ptasienski J, Benovic JL, Hosey MM. G protein-coupled receptor kinase GRK2 is a phospholipid-dependent enzyme that can be conditionally activated by G protein betagamma subunits. J Biol Chem. 271:1996;22552-22562.
    • (1996) J Biol Chem , vol.271 , pp. 22552-22562
    • Debburman, S.K.1    Ptasienski, J.2    Benovic, J.L.3    Hosey, M.M.4
  • 58
    • 0030995811 scopus 로고    scopus 로고
    • Interactions between protein kinase C and pleckstrin homology domains. Inhibition by phosphatidylinositol 4,5-bisphosphate and phorbol 12-myristate 13-acetate
    • Yao L, Suzuki H, Ozawa K, Deng J, Lehel C, Fukamachi H, Anderson WB, Kawakami Y, Kawakami T. Interactions between protein kinase C and pleckstrin homology domains. Inhibition by phosphatidylinositol 4,5-bisphosphate and phorbol 12-myristate 13-acetate. J Biol Chem. 272:1997;13033-13039.
    • (1997) J Biol Chem , vol.272 , pp. 13033-13039
    • Yao, L.1    Suzuki, H.2    Ozawa, K.3    Deng, J.4    Lehel, C.5    Fukamachi, H.6    Anderson, W.B.7    Kawakami, Y.8    Kawakami, T.9
  • 59
    • 0026752622 scopus 로고
    • Identification of a phosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin
    • Yu F-X, Sun H-Q, Jamney PA, Yin HL. Identification of a phosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J Biol Chem. 267:1992;14616-14621.
    • (1992) J Biol Chem , vol.267 , pp. 14616-14621
    • Yu F-X1    Sun H-Q2    Jamney, P.A.3    Yin, H.L.4
  • 60
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • Janmey PA, Lamb J, Allen PG, Matsudaira PT. Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J Biol Chem. 267:1992;11815-11823.
    • (1992) J Biol Chem , vol.267 , pp. 11815-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 61
    • 0030878997 scopus 로고    scopus 로고
    • Gelsolin binding to phosphatidylinositol 4,5-bisphosphate is modulated by calcium and pH
    • Lin KM, Wenegieme E, Lu PJ, Chen CS, Yin HL. Gelsolin binding to phosphatidylinositol 4,5-bisphosphate is modulated by calcium and pH. J Biol Chem. 272:1997;20443-20450.
    • (1997) J Biol Chem , vol.272 , pp. 20443-20450
    • Lin, K.M.1    Wenegieme, E.2    Lu, P.J.3    Chen, C.S.4    Yin, H.L.5
  • 62
    • 0029097309 scopus 로고
    • Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin
    • Sohn RH, Chen J, Koblan KS, Bray PF, Goldschmidt-Clermont PJ. Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin. J Biol Chem. 270:1995;21114-21120.
    • (1995) J Biol Chem , vol.270 , pp. 21114-21120
    • Sohn, R.H.1    Chen, J.2    Koblan, K.S.3    Bray, P.F.4    Goldschmidt-Clermont, P.J.5
  • 63
    • 0031024690 scopus 로고    scopus 로고
    • The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences
    • Lambrechts A, Verschelde JL, Jonckheere V, Goethals M, Vandekerckhove J, Ampe C. The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences. EMBO J. 16:1997;484-494.
    • (1997) EMBO J , vol.16 , pp. 484-494
    • Lambrechts, A.1    Verschelde, J.L.2    Jonckheere, V.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6


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