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Volumn 4, Issue 5, 1997, Pages 351-356

Polyphosphoinositide synthesis and platelet shape change

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FIBRINOGEN RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL KINASE; PLECKSTRIN; POLYPHOSPHOINOSITIDE; PROTEIN KINASE C;

EID: 0030799317     PISSN: 10656251     EISSN: None     Source Type: Journal    
DOI: 10.1097/00062752-199704050-00009     Document Type: Review
Times cited : (11)

References (45)
  • 1
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig J, Bokoch G, Carpenter C, Janmey P, Taylor L, Toker A, Stossel T: Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 1995, 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.1    Bokoch, G.2    Carpenter, C.3    Janmey, P.4    Taylor, L.5    Toker, A.6    Stossel, T.7
  • 2
    • 0026075254 scopus 로고
    • "Thrombin" receptor-directed ligand accounts for activation by thrombin of platelet phospholipase C and accumulation of 3-phosphorylated phosphoinositides
    • Huang R, Sorisky A, Church W, Simons E, Rittenhouse S: "Thrombin" receptor-directed ligand accounts for activation by thrombin of platelet phospholipase C and accumulation of 3-phosphorylated phosphoinositides. J Biol Chem 1991, 266:18435-18438.
    • (1991) J Biol Chem , vol.266 , pp. 18435-18438
    • Huang, R.1    Sorisky, A.2    Church, W.3    Simons, E.4    Rittenhouse, S.5
  • 3
    • 0030474160 scopus 로고    scopus 로고
    • D3 phosphoinositides and outside-in integrin signaling by GPIIb/IIIa mediate platelet actin assembly and filopodial extension Induced by phorbol 12-myristate 13-acetate
    • Hartwig J, Kung S, Kovacsovics T, Janmey P, Cantley L, Stossel T, Toker A: D3 phosphoinositides and outside-in integrin signaling by GPIIb/IIIa mediate platelet actin assembly and filopodial extension Induced by phorbol 12-myristate 13-acetate. J Biol Chem 1996, 271:32986-32993. Explores the mechanism of filopodial growth in platelets. Activation of GPIIb-IIIa by protein kinase C or with activating IgGs is shown to affect filopodia formation. Actin assembly and nucleation activity are characterized. Filopodia formation, as well as actin assembly and nucleation, require the production of PI 3,4-biphosphate.
    • (1996) J Biol Chem , vol.271 , pp. 32986-32993
    • Hartwig, J.1    Kung, S.2    Kovacsovics, T.3    Janmey, P.4    Cantley, L.5    Stossel, T.6    Toker, A.7
  • 4
    • 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 1994, 56:169-191.
    • (1994) Annu Rev Physiol , vol.56 , pp. 169-191
    • Janmey, P.1
  • 5
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow K, Witke W, Kwiatkowski D, Hartwig J: Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J Cell Biol 1996, 134:389-399.
    • (1996) J Cell Biol , vol.134 , pp. 389-399
    • Barkalow, K.1    Witke, W.2    Kwiatkowski, D.3    Hartwig, J.4
  • 6
    • 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 (4,5) levels in human platelets are controlled by translocation of Ptdlns 4-P 5-kinase C to the cytoskeleton. EMBO 1996, 15:6516-6524. Phosphatidylinositol 4-monophosphate 5 kinase is shown to translocate to the cytoskeleton in a GPIIb-IIIa-dependent fashion. Translocation correlates with an increase in the amount of PI 4,5-biphosphate in the cytoskeleton.
    • (1996) EMBO , vol.15 , pp. 6516-6524
    • Hinchliffe, K.1    Irvine, R.2    Divecha, N.3
  • 7
    • 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, Yazaki Y: Massive actin polymerization Induced by phosphatidylinositol-4 phosphate 5-kinase in vivo. J Biol Chem 1997, 272:7578-7581. Ectopic expression of PI 4-monophosphate 5 kinase in Cos cells causes a dramatic rearrangement of cell shape and the decoration of the cell surface with actin-rich spikes. Co-expression of negative dominant rho did not alter the ability of the 5-kinase to change the morphology of cells.
    • (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
  • 8
    • 0029050557 scopus 로고
    • Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets, but reverses platelet aggregation
    • Kovacsovics T, Bachelot C, Toker A, Vlahos C, Duckworth B, Cantley L, Hartwig J: Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets, but reverses platelet aggregation. J Biol Chem 1995, 270:11358-11366.
    • (1995) J Biol Chem , vol.270 , pp. 11358-11366
    • Kovacsovics, T.1    Bachelot, C.2    Toker, A.3    Vlahos, C.4    Duckworth, B.5    Cantley, L.6    Hartwig, J.7
  • 9
    • 0029964243 scopus 로고    scopus 로고
    • 3 integrin
    • 3 integrin. J Biol Chem 1996, 271:6265-6272. The relative contribution of p85/PI-3 kinase and PI-3 kinase gamma to the generation of position D containing polyphosphoinositide after activation with phorbol esters or through the thrombin receptor is determined.
    • (1996) J Biol Chem , vol.271 , pp. 6265-6272
    • Zhang, J.1    Zhang, J.2    Shattil, S.3    Cunningham, M.4    Rittenhouse, S.5
  • 10
    • 0026354977 scopus 로고
    • Involvement of platelet glycoprotein IIb-IIIa (alphaIIb-beta3 Integrin) in thrombin-induced synthesis of phosphatidylinositol 3′,4′-bisphosphate
    • Sultan C, Plantavid M, Bachelot C, Grondin P, Breton M, Mauco G, Lévy-Toledano S, Caen J, Chap H: Involvement of platelet glycoprotein IIb-IIIa (alphaIIb-beta3 Integrin) In thrombin-induced synthesis of phosphatidylinositol 3′,4′-bisphosphate. J Biol Chem 1991, 266:23554-23557.
    • (1991) J Biol Chem , vol.266 , pp. 23554-23557
    • Sultan, C.1    Plantavid, M.2    Bachelot, C.3    Grondin, P.4    Breton, M.5    Mauco, G.6    Lévy-Toledano, S.7    Caen, J.8    Chap, H.9
  • 11
    • 0028951464 scopus 로고
    • Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85alpha with actin filaments and focal adhesion kinase
    • Guinebault C, Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H: Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85alpha with actin filaments and focal adhesion kinase. J Cell Biol 1995, 129:831-842.
    • (1995) J Cell Biol , vol.129 , pp. 831-842
    • Guinebault, C.1    Payrastre, B.2    Racaud-Sultan, C.3    Mazarguil, H.4    Breton, M.5    Mauco, G.6    Plantavid, M.7    Chap, H.8
  • 13
    • 0028788181 scopus 로고
    • Phosphorylation of the platelet p47 phosphoprotein Is mediated by the lipid products of phosphoinositide 3-kinase
    • Toker A, Bachelot C, Chen S-C, Falck J, Hartwig J, Cantley L, Kovacsovics T: Phosphorylation of the platelet p47 phosphoprotein Is mediated by the lipid products of phosphoinositide 3-kinase. J Biol Chem 1995, 270:29525-29531.
    • (1995) J Biol Chem , vol.270 , pp. 29525-29531
    • Toker, A.1    Bachelot, C.2    Chen, S.-C.3    Falck, J.4    Hartwig, J.5    Cantley, L.6    Kovacsovics, T.7
  • 14
    • 0029084949 scopus 로고
    • Phosphatidylinositol (3,4,5)-trisphosphate stimulates phosphorylation of pleckstrin in human platelets
    • Zhang J, Falck J, Reddy K, Abrams C, Zhao W, Rittenhouse S: Phosphatidylinositol (3,4,5)-trisphosphate stimulates phosphorylation of pleckstrin in human platelets. J Biol Chem 1995, 270:22807-22810.
    • (1995) J Biol Chem , vol.270 , pp. 22807-22810
    • Zhang, J.1    Falck, J.2    Reddy, K.3    Abrams, C.4    Zhao, W.5    Rittenhouse, S.6
  • 15
    • 0030023759 scopus 로고    scopus 로고
    • Abnormal inside-out signal transduction-dependent activation of glycoprotein IIb-IIIa in a patient with Impaired pleckstrin phosphorylation
    • Gabbeta J, Yang X, Sun L, McLane M, Niewiarowski S, Rao A: Abnormal inside-out signal transduction-dependent activation of glycoprotein IIb-IIIa In a patient with Impaired pleckstrin phosphorylation. Blood 1996, 87:1368-1376. Links pleckstrin to the function of GPIIb-IIIa. The aggregation reaction of platelets from a 16-year-old patient with lifelong bleeding problems is studied. Patients display abnormal aggregation, decreased conversion of GPIIb-IIIa to its active form, and disminished phosphorylation of pleckstrin after cell activaton.
    • (1996) Blood , vol.87 , pp. 1368-1376
    • Gabbeta, J.1    Yang, X.2    Sun, L.3    McLane, M.4    Niewiarowski, S.5    Rao, A.6
  • 16
    • 0027374497 scopus 로고
    • Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein rho
    • Zhang J, King W, Dillon S, Hall A, Feig L, Rittenhouse S: Activation of platelet phosphatidylinositide 3-kinase requires the small GTP-binding protein rho. J Biol Chem 1993, 268:22251-22254.
    • (1993) J Biol Chem , vol.268 , pp. 22251-22254
    • Zhang, J.1    King, W.2    Dillon, S.3    Hall, A.4    Feig, L.5    Rittenhouse, S.6
  • 17
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias K, Cantley L, Carpenter C: Rho family GTPases bind to phosphoinositide kinases. J Biol Chem 1995, 270:17656-17659.
    • (1995) J Biol Chem , vol.270 , pp. 17656-17659
    • Tolias, K.1    Cantley, L.2    Carpenter, C.3
  • 18
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase Rho with the 68-kDa Phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren X-D, Bokoch G, Traynor-Kaplan A, Jenkins G, Anderson R, Schwartz M: Physical association of the small GTPase Rho with the 68-kDa Phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol Biol Cell 1996, 7:435-442. Phosphatidylinositol 4-monophosphate 5 kinase is shown to bind specifically to a rho-affinity matrix. Binding is independent of GTP charging of rho.
    • (1996) Mol Biol Cell , vol.7 , pp. 435-442
    • Ren, X.-D.1    Bokoch, G.2    Traynor-Kaplan, A.3    Jenkins, G.4    Anderson, R.5    Schwartz, M.6
  • 19
    • 0028036684 scopus 로고
    • The small GTP-binding protein rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong L, Traynor-Kaplan A, Bokoch G, Schwartz M: The small GTP-binding protein rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 1994, 79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.1    Traynor-Kaplan, A.2    Bokoch, G.3    Schwartz, M.4
  • 20
    • 0029157584 scopus 로고
    • Identification, purification and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)
    • Reinhard M, Tripier D, Walter U: Identification, purification and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc Natl Acad Sci U S A 1995, 92:7956-7960.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 7956-7960
    • Reinhard, M.1    Tripier, D.2    Walter, U.3
  • 21
    • 0030577348 scopus 로고    scopus 로고
    • VASP interaction with vinculin: A recurring theme of interactions with proline-rich motifs
    • Reinhard M, Rudiger M, Jockusch B, Walter U: VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. FEBS Letters 1996, 399:103-107. Vinculin-VASP binding is demonstrated in vitro. The VASP binding site for vinculin is defined using peptide competition and is shown to be the actin-binding motif-1 polyproline region.
    • (1996) FEBS Letters , vol.399 , pp. 103-107
    • Reinhard, M.1    Rudiger, M.2    Jockusch, B.3    Walter, U.4
  • 22
    • 0029761645 scopus 로고    scopus 로고
    • The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the prolinerich domain in vinculin
    • Brindle N, Holt M, Davies J, Price C, Critchley D: The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the prolinerich domain In vinculin. Biochem J 1996, 318:753-757. The first demonstration that VASP binds the predicted FPPPP motif in vinculin.
    • (1996) Biochem J , vol.318 , pp. 753-757
    • Brindle, N.1    Holt, M.2    Davies, J.3    Price, C.4    Critchley, D.5
  • 23
    • 0031584867 scopus 로고    scopus 로고
    • ABM-1 and ABM-2 homology sequences: Consensus docking sites for actin-based motility defined by oligoproline regions in Listeria Acta surface protein and human VASP
    • Punch D, Southwick F: ABM-1 and ABM-2 homology sequences: consensus docking sites for actin-based motility defined by oligoproline regions in Listeria Acta surface protein and human VASP. Biochem Biophys Res Comm 1997, 231:686-691.
    • (1997) Biochem Biophys Res Comm , vol.231 , pp. 686-691
    • Punch, D.1    Southwick, F.2
  • 25
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is Implicated in actin polymerization
    • Symons M, Derry J, 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 1996, 84:723-734. This is one of three papers published in 1996 that demonstrate that WASP interacts with Cdc42 and Rac in a GTP-dependent manner.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 26
    • 0028961293 scopus 로고
    • Rac, rho, and cdc42 GTPase regulate the assembly of multi-molecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes C, Hall A: Rac, rho, and cdc42 GTPase regulate the assembly of multi-molecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.1    Hall, A.2
  • 27
    • 0027937223 scopus 로고
    • Identification of a novel gene mutated in Wiskott-Aldrich syndrome
    • Deny J, Ochs H, Francke U: Identification of a novel gene mutated In Wiskott-Aldrich syndrome. Cell 1994, 78:635-644.
    • (1994) Cell , vol.78 , pp. 635-644
    • Deny, J.1    Ochs, H.2    Francke, U.3
  • 28
    • 0029680639 scopus 로고    scopus 로고
    • The two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome
    • Aspenstrom P, Lindberg U, Hall A: The two GTPases, Cdc42 and Rac, bind directly to a protein implicated In the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr Biol 1996, 6:70-75. This is one of three papers published in 1996 that demonstrate that WASP interact with a Cdc42 and Rac in a GTP-dependent manner.
    • (1996) Curr Biol , vol.6 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 29
    • 0029953158 scopus 로고    scopus 로고
    • Direct Interaction of the Wiskott-Aldrich syndrome protein with the GTPase, Cdc42
    • Kolluri R, Fuchs Tolias K, Carpenter C, Rosen F, Kirchhausen T: Direct Interaction of the Wiskott-Aldrich syndrome protein with the GTPase, Cdc42. Proc Natl Acad Sci U S A 1996, 93:5615-5618. This is one of three papers published in 1996 that demonstrate that WASP interacts with Cdc42 and Rac in a GTP-dependent manner.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5615-5618
    • Kolluri, R.1    Fuchs Tolias, K.2    Carpenter, C.3    Rosen, F.4    Kirchhausen, T.5
  • 30
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing 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-depolymerizing protein, regulates the cortical cytoskeletal rearrangement In a PIP2-dependent manner downstream of tyrosine kinases. EMBO J 1996, 15:5326-5335. Cloning and characterization of the ubiquitous N-WASP. Overexpression in Clos cells results in the formation of actin-based microspikes at the cell surface. An N-WASP truncate having both the verprolin and cofilin domains is shown to depolymerize actin filaments in vitro. Binding of PI 4,5-biphosphate to the pleckstrin homology domain is demonstrated.
    • (1996) EMBO J , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 31
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan J, Hajduk P, Yoon H, Fesik S: Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 1994, 371:168-170.
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.1    Hajduk, P.2    Yoon, H.3    Fesik, S.4
  • 32
    • 0031015986 scopus 로고    scopus 로고
    • A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through Its pleckstrin homology domain
    • Klippel A, Kavanaugh WM, Pot D, Williams LT: A specific product of phosphatidylinositol 3-kinase directly activates the protein kinase Akt through Its pleckstrin homology domain. Mol Cell Biol 1997, 17:338-344.
    • (1997) Mol Cell Biol , vol.17 , pp. 338-344
    • Klippel, A.1    Kavanaugh, W.M.2    Pot, D.3    Williams, L.T.4
  • 33
    • 0028891875 scopus 로고
    • Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase-differential effects on g(beta-gamma) and phosphatidylinositol 4,5-bisphosphate binding
    • Touhara K, Koch W, Hawes B, Lefkowitz R: Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase-differential effects on g(beta-gamma) and phosphatidylinositol 4,5-bisphosphate binding. J Biol Chem 1995, 270:17000-17005.
    • (1995) J Biol Chem , vol.270 , pp. 17000-17005
    • Touhara, K.1    Koch, W.2    Hawes, B.3    Lefkowitz, R.4
  • 34
    • 0029157058 scopus 로고
    • Pleckstrin homology domains: A fact file
    • Saraste M, Hyvonen M: Pleckstrin homology domains: a fact file. Curr Opin Struct Biol 1995, 5:403-408.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 403-408
    • Saraste, M.1    Hyvonen, M.2
  • 36
    • 0027276925 scopus 로고
    • Pleckstrin domain homology
    • Haslam R, Koide H, Hammings B: Pleckstrin domain homology. Nature 1993, 363:309-310.
    • (1993) Nature , vol.363 , pp. 309-310
    • Haslam, R.1    Koide, H.2    Hammings, B.3
  • 37
    • 0019298511 scopus 로고
    • Phospholipid turnover as a possible transmembrane signal for protein phosphorylation during human platelet activation by thrombin
    • Kawahara Y, Takai Y, Minakuchi R, Sano K, Nishizuka Y: Phospholipid turnover as a possible transmembrane signal for protein phosphorylation during human platelet activation by thrombin. Biochem Biophys Res Commun 1980, 97:309-317.
    • (1980) Biochem Biophys Res Commun , vol.97 , pp. 309-317
    • Kawahara, Y.1    Takai, Y.2    Minakuchi, R.3    Sano, K.4    Nishizuka, Y.5
  • 38
    • 0018741860 scopus 로고
    • Effects of collagen, ionophore A23187 and prostaglandin E1 on the phosphorylation of specific proteins in blood platelets
    • Haslam R, Lynham J, Fox J: Effects of collagen, ionophore A23187 and prostaglandin E1 on the phosphorylation of specific proteins in blood platelets. Biochem J 1979, 178:397-406.
    • (1979) Biochem J , vol.178 , pp. 397-406
    • Haslam, R.1    Lynham, J.2    Fox, J.3
  • 39
    • 0028865255 scopus 로고
    • Protein kinase C regulates pleckstrin by phosphorylation of sites adjacent to the N-terminal pleckstrin homology domain
    • Abrams C, Zhao W, Belmonte E, Brass L: Protein kinase C regulates pleckstrin by phosphorylation of sites adjacent to the N-terminal pleckstrin homology domain. J Biol Chem 1995, 270:23317-23321.
    • (1995) J Biol Chem , vol.270 , pp. 23317-23321
    • Abrams, C.1    Zhao, W.2    Belmonte, E.3    Brass, L.4
  • 40
    • 0029055503 scopus 로고
    • Pleckstrin inhibits phosphoinositide hydrolysis Initiated by g-protein-coupled and growth factor receptors-a role for pleckstrins pH domains
    • Abrams C, Wu H, Zhao W, Belmonte E, White D, Brass L: Pleckstrin inhibits phosphoinositide hydrolysis Initiated by g-protein-coupled and growth factor receptors-a role for pleckstrins pH domains. J Biol Chem 1995, 270:14485-14492.
    • (1995) J Biol Chem , vol.270 , pp. 14485-14492
    • Abrams, C.1    Wu, H.2    Zhao, W.3    Belmonte, E.4    White, D.5    Brass, L.6
  • 41
    • 0029661976 scopus 로고    scopus 로고
    • Phosphopleckstrin inhibits G beta gamma-activable platelet phosphatidylinositol-4,5-bisphosphate 3-kinase
    • Abrams C, Zhang J, Downes C, Tang X, Zhao W, Rittenhouse S: Phosphopleckstrin inhibits G beta gamma-activable platelet phosphatidylinositol-4,5-bisphosphate 3-kinase. J Biol Chem 1996, 271:25192-25197.
    • (1996) J Biol Chem , vol.271 , pp. 25192-25197
    • Abrams, C.1    Zhang, J.2    Downes, C.3    Tang, X.4    Zhao, W.5    Rittenhouse, S.6
  • 42
    • 0029039613 scopus 로고
    • Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requeres coordinate interaction of Gbeta 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 requeres coordinate interaction of Gbeta gamma subunits and lipid. J Biol Chem 1995, 270:11707-11710.
    • (1995) J Biol Chem , vol.270 , pp. 11707-11710
    • Pitcher, J.A.1    Touhara, K.2    Payne, E.S.3    Lefkowitz, R.J.4
  • 43
    • 0026014052 scopus 로고
    • Protein kinase C and cAMP regulate reversible exposure of fibrinogen binding sites on the glycoprotein IIbIIIa complex of human platelets
    • Willegen GV, Ackerman J-W: Protein kinase C and cAMP regulate reversible exposure of fibrinogen binding sites on the glycoprotein IIbIIIa complex of human platelets. Biochem J 1991, 273:115.
    • (1991) Biochem J , vol.273 , pp. 115
    • Willegen, G.V.1    Ackerman, J.-W.2
  • 44
    • 0031018359 scopus 로고    scopus 로고
    • Phosphorylation of platelet pleckstrin activates inositol polyphosphate 5-phosphatase I
    • Auethavekiatt V, Abrams C, Majerus P: Phosphorylation of platelet pleckstrin activates inositol polyphosphate 5-phosphatase I. J Biol Chem 1997, 272:1786-1790.
    • (1997) J Biol Chem , vol.272 , pp. 1786-1790
    • Auethavekiatt, V.1    Abrams, C.2    Majerus, P.3
  • 45
    • 0030998128 scopus 로고    scopus 로고
    • Pleckstrin associates with plasma membrane and induces the formation of membrane projections: Requirements for phosphorylation and the NH2-terminal PH domain
    • Ma A, Brass L, Abrams C: Pleckstrin associates with plasma membrane and induces the formation of membrane projections: requirements for phosphorylation and the NH2-terminal PH domain. J Cell Biol 1997, 136:1071-1080. Ectopic expression in Cos cells reveals that pleckstrin associates with membranes and membrane projections. Truncation experiments demonstrate that these effects require phosphorylation of pleckstrin and the N-T pleckstrin homology domain of the protein.
    • (1997) J Cell Biol , vol.136 , pp. 1071-1080
    • Ma, A.1    Brass, L.2    Abrams, C.3


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