메뉴 건너뛰기




Volumn 73, Issue 3, 1997, Pages 1440-1447

The structure of divalent cation-induced aggregates of PIP2 and their alteration by gelsolin and tau

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; BINDING PROTEIN; DIACYLGLYCEROL; DIVALENT CATION; GELSOLIN; INOSITOL TRISPHOSPHATE; PROFILIN; TAU PROTEIN; TRIPHOSPHOINOSITIDE;

EID: 0030855302     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78176-1     Document Type: Article
Times cited : (76)

References (39)
  • 2
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt, R., J. Leger, and G. Lee. 1995. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 131:1327-1340.
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Leger, J.2    Lee, G.3
  • 3
    • 0029790963 scopus 로고    scopus 로고
    • Synthesis of photoactivatable 1,2-o-diacyl-sn-glycerol derivatives of 1-1-phosphatidyl-d-myoinositol 4,5-bisphosphate (ptdinsp(2)) and 3,4,5-trisphosphate (ptdinsp(3))
    • Chen, J., A. A. Profit, and G. D. Prestwich. 1996. Synthesis of photoactivatable 1,2-o-diacyl-sn-glycerol derivatives of 1-1-phosphatidyl-d-myoinositol 4,5-bisphosphate (ptdinsp(2)) and 3,4,5-trisphosphate (ptdinsp(3)). J. Org. Chem. 61:6305-6312.
    • (1996) J. Org. Chem. , vol.61 , pp. 6305-6312
    • Chen, J.1    Profit, A.A.2    Prestwich, G.D.3
  • 4
    • 0027209418 scopus 로고
    • Inositides and the nucleus and inositides in the nucleus
    • Divecha, N., H. Banfic, and R. F. Irvine. 1993. Inositides and the nucleus and inositides in the nucleus. Cell. 74:405-407.
    • (1993) Cell , vol.74 , pp. 405-407
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 5
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha, N., and R. F. Irvine. 1995. Phospholipid signaling. Cell. 80: 269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 6
    • 0027965072 scopus 로고
    • X-ray structure of isoforms of the actin binding protein profilin that differ in their affinity for polyphosphoinositides
    • Federov, A. A., K. A. Magnus, M. H. Graupe, E. E. Lattman, T. D. Pollard, and S. C. Almo. 1994. X-ray structure of isoforms of the actin binding protein profilin that differ in their affinity for polyphosphoinositides. Proc. Natl. Acad. Sci. U.S.A. 91:8636-8640.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8636-8640
    • Federov, A.A.1    Magnus, K.A.2    Graupe, M.H.3    Lattman, E.E.4    Pollard, T.D.5    Almo, S.C.6
  • 7
    • 0024433060 scopus 로고
    • Microtubule formation and neunte growth in cerebellar macroneurons which develop in vitro: Evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau
    • Ferreira, A., J. Busciglio, and A. Caceres. 1989. Microtubule formation and neunte growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau. Brain Res. Dev. Brain Res. 49: 215-228.
    • (1989) Brain Res. Dev. Brain Res. , vol.49 , pp. 215-228
    • Ferreira, A.1    Busciglio, J.2    Caceres, A.3
  • 8
    • 37049076711 scopus 로고
    • From discoid micelles to spherical vesicles - The concept of edge activity
    • Fromherz, P., C. Rocker, and D. Ruppel. 1986. From discoid micelles to spherical vesicles - the concept of edge activity. Farad Disc. Chem. Soc. 81:39-48.
    • (1986) Farad Disc. Chem. Soc. , vol.81 , pp. 39-48
    • Fromherz, P.1    Rocker, C.2    Ruppel, D.3
  • 9
    • 12044259093 scopus 로고
    • Fluid and solid fibers made of lipid molecular bilayers
    • Fuhrhop, J.-H., and W. Helfrich. 1993. Fluid and solid fibers made of lipid molecular bilayers. Chem. Rev. 93:1565-1582.
    • (1993) Chem. Rev. , vol.93 , pp. 1565-1582
    • Fuhrhop, J.-H.1    Helfrich, W.2
  • 10
    • 0014011091 scopus 로고
    • Phospholipid-metal complexes. Interaction of triphosphoinositide- and phosphatidylserine-metal complexes with ethylenediamine, polyaminoacids, and protein
    • Fullington, J. G., and H. S. Hendrickson. 1966. Phospholipid-metal complexes. Interaction of triphosphoinositide-and phosphatidylserine-metal complexes with ethylenediamine, polyaminoacids, and protein. J. Biol. Chem. 241:4098-4100.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4098-4100
    • Fullington, J.G.1    Hendrickson, H.S.2
  • 12
    • 0025308055 scopus 로고
    • The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C
    • Goldschmidt-Clermont, P. J., L. M. Machesky, J. J. Baldassare, and T. D. Pollard. 1990. The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science. 247:1575-1578.
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1    Machesky, L.M.2    Baldassare, J.J.3    Pollard, T.D.4
  • 13
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., G. M. Bokoch, C. L. Carpenter, P. A. Janmey, L. A. Taylor, A. Toker, and T. P. Stossel. 1995. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 14
    • 0013795179 scopus 로고
    • Stabilities of metal complexes of phospholipids: Ca(II), Mg(II), and Ni(II) complexes of phosphatidylserine and triphosphoinositide
    • Hendrickson, H. S., and J. G. Fullington. 1965. Stabilities of metal complexes of phospholipids: Ca(II), Mg(II), and Ni(II) complexes of phosphatidylserine and triphosphoinositide. Biochem. 4:1599-1605.
    • (1965) Biochem. , vol.4 , pp. 1599-1605
    • Hendrickson, H.S.1    Fullington, J.G.2
  • 16
    • 0001169160 scopus 로고    scopus 로고
    • Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid
    • Hwang, S., D.-Y. Jhon, Y. Bae, J. Kim, and S. Rhee. 1996. Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid. J. Biol. Chem. 271:18342-18349.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18342-18349
    • Hwang, S.1    Jhon, D.-Y.2    Bae, Y.3    Kim, J.4    Rhee, S.5
  • 17
    • 0017377723 scopus 로고
    • Morphology of lipid micelles containing lysolecithin
    • Inoue, K., K. Suzuki, and S. Nojima. 1977. Morphology of lipid micelles containing lysolecithin. J. Biochem. 81:1097-1106.
    • (1977) J. Biochem. , vol.81 , pp. 1097-1106
    • Inoue, K.1    Suzuki, K.2    Nojima, S.3
  • 18
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P. 1994. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Ann. Rev. Physiol. 56:169-191.
    • (1994) Ann. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.1
  • 19
    • 0025878284 scopus 로고
    • Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide
    • Janmey, P. A. 1991. Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide. Methods Enzymol. 196:92-99.
    • (1991) Methods Enzymol. , vol.196 , pp. 92-99
    • Janmey, P.A.1
  • 20
    • 0023199043 scopus 로고
    • Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin
    • Janmey, P. A., K. Iida, H. L. Yin, and T. P. Stossel. 1987. Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J. Biol. Chem. 262:12228-12236.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12228-12236
    • Janmey, P.A.1    Iida, K.2    Yin, H.L.3    Stossel, T.P.4
  • 21
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • Janmey, P. A., J. Lamb, P. G. Allen, and P. T. Matsudaira. 1992. Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267:11818-11823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 22
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey, P. A., and T. P. Stossel. 1987. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature. 325:362-364.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 23
    • 0024567044 scopus 로고
    • Gelsolin-polyphosphoinositide interaction. Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group
    • Janmey, P. A., and T. P. Stossel. 1989. Gelsolin-polyphosphoinositide interaction. Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group. J. Biol. Chem. 264:4825-4831.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4825-4831
    • Janmey, P.A.1    Stossel, T.P.2
  • 24
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller, R., and L. C. Cantley. 1994. Phosphatidylinositol 3-kinase. Bioessays. 16:565-576.
    • (1994) Bioessays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 26
    • 0024109687 scopus 로고
    • Epitopes that span the tau molecule are shared with paired helical filaments
    • Kosik, K. S., L. D. Orecchio, L. Binder, J. Q. Trojanowski, V. M. Lee, and G. Lee. 1988. Epitopes that span the tau molecule are shared with paired helical filaments. Neuron. 1:817-825.
    • (1988) Neuron , vol.1 , pp. 817-825
    • Kosik, K.S.1    Orecchio, L.D.2    Binder, L.3    Trojanowski, J.Q.4    Lee, V.M.5    Lee, G.6
  • 27
    • 0018402422 scopus 로고
    • Practical aspects of immune electron microscopy
    • Lake, J. A. 1979. Practical aspects of immune electron microscopy. Methods Enzymol. 61:250-257.
    • (1979) Methods Enzymol. , vol.61 , pp. 250-257
    • Lake, J.A.1
  • 28
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • Lassing, I., and U. Lindberg. 1985. Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature. 314:472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 29
    • 0024518870 scopus 로고
    • Characterization and purification of membrane-associated phosphatidylinositol-4-phosphate kinase from human red blood cells
    • Ling, L. E., J. T. Schulz, and L. C. Cantley. 1989. Characterization and purification of membrane-associated phosphatidylinositol-4-phosphate kinase from human red blood cells. J. Biol. Chem. 264:5080-5088.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5080-5088
    • Ling, L.E.1    Schulz, J.T.2    Cantley, L.C.3
  • 30
    • 0016820946 scopus 로고
    • Cochleate lipid cylinders: Formation by fusion of unilamellar lipid vesicles
    • Papahadjopoulos, D., W. J. Vail, K. Jacobson, and G. Poste. 1975. Cochleate lipid cylinders: formation by fusion of unilamellar lipid vesicles. Biochim. Biophys. Acta. 394:483-491.
    • (1975) Biochim. Biophys. Acta , vol.394 , pp. 483-491
    • Papahadjopoulos, D.1    Vail, W.J.2    Jacobson, K.3    Poste, G.4
  • 31
    • 0001484549 scopus 로고    scopus 로고
    • Touching all the bases - Synthesis of inositol polyphosphate and phosphoinositide affinity probes from glucose
    • Prestwich, G. D. 1996. Touching all the bases - synthesis of inositol polyphosphate and phosphoinositide affinity probes from glucose. Acc. Chem. Res. 29:503-513.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 503-513
    • Prestwich, G.D.1
  • 32
    • 0022343675 scopus 로고
    • Mass changes in myoinositol trisphosphate in human platelets stimulated by thrombin. Inhibitory effects of phorbol ester
    • Rittenhouse, S. E., and J. P. Sasson. 1985. Mass changes in myoinositol trisphosphate in human platelets stimulated by thrombin. Inhibitory effects of phorbol ester. J. Biol. Chem. 260:8657-8660.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8657-8660
    • Rittenhouse, S.E.1    Sasson, J.P.2
  • 33
    • 0023152555 scopus 로고
    • Calcium-induced fusion of didodecylphosphate vesicles: The lamellar to hexagonal II (HII) phase transition
    • Rupert, L. A. M., J. F. L. v. Breemen, E. F. J. v. Bruggen, J. B. F. N. Engberts, and D. Hoekstra. 1987. Calcium-induced fusion of didodecylphosphate vesicles: the lamellar to hexagonal II (HII) phase transition. J. Membr. Biol. 95:255-263.
    • (1987) J. Membr. Biol. , vol.95 , pp. 255-263
    • Rupert, L.A.M.1    Breemen, J.F.L.V.2    Bruggen, E.F.J.V.3    Engberts, J.B.F.N.4    Hoekstra, D.5
  • 34
    • 0019469654 scopus 로고
    • Structure of molecular aggregates of 1-(3-sn-phosphatidyl)-L-myo-inositol 3,4-bis(phosphate) in water
    • Sugiura, Y. 1981. Structure of molecular aggregates of 1-(3-sn-phosphatidyl)-L-myo-inositol 3,4-bis(phosphate) in water. Biochim. Biophys. Acta. 641:148-159.
    • (1981) Biochim. Biophys. Acta , vol.641 , pp. 148-159
    • Sugiura, Y.1
  • 35
    • 0028233811 scopus 로고
    • The difference in the binding of phosphatidylinositol distinguishes MAP2 from MAP2c and tau
    • Surridge, C. D., and R. G. Burns. 1994. The difference in the binding of phosphatidylinositol distinguishes MAP2 from MAP2c and tau. Biochem. 33:8051-8057.
    • (1994) Biochem. , vol.33 , pp. 8051-8057
    • Surridge, C.D.1    Burns, R.G.2
  • 36
    • 0029993245 scopus 로고    scopus 로고
    • Tau as a nucleolar protein in human nonneural cells in vitro and in vivo
    • Thurston, V., R. Zinkowski, and L. Binder. 1996. Tau as a nucleolar protein in human nonneural cells in vitro and in vivo. Chromosoma. 105:20-30.
    • (1996) Chromosoma , vol.105 , pp. 20-30
    • Thurston, V.1    Zinkowski, R.2    Binder, L.3
  • 37
    • 0027469909 scopus 로고
    • A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau
    • Wang, Y., P. A. Loomis, R. P. Zinkowski, and L. I. Binder. 1993. A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau. J. Cell Biol. 121:257-267.
    • (1993) J. Cell Biol. , vol.121 , pp. 257-267
    • Wang, Y.1    Loomis, P.A.2    Zinkowski, R.P.3    Binder, L.I.4
  • 39
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin
    • Yu, F. X., H. Q. Sun, P. A. Janmey, and H. L. Yin. 1992. Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267:14616-14621.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.X.1    Sun, H.Q.2    Janmey, P.A.3    Yin, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.