메뉴 건너뛰기




Volumn 52, Issue 3-4, 2012, Pages 259-269

Anionic lipids in Ca2+-triggered fusion

Author keywords

Cholesterol sulfate; Cortical vesicles; Docking; Exocytosis; Phosphatidylinositol; Phosphatidylserine; Priming

Indexed keywords

ANIONIC LIPID; CALCIUM ION; LIPID; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLSERINE; UNCLASSIFIED DRUG;

EID: 84865789432     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2012.03.006     Document Type: Article
Times cited : (18)

References (103)
  • 1
    • 0030586161 scopus 로고    scopus 로고
    • Non-bilayer lipids and biological fusion intermediates
    • Chernomordik L. Non-bilayer lipids and biological fusion intermediates. Chem. Phys. Lipids 1996, 81:203-213.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 203-213
    • Chernomordik, L.1
  • 2
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: crossing a chasm in two leaps
    • Chernomordik L.V., Kozlov M.M. Membrane hemifusion: crossing a chasm in two leaps. Cell 2005, 123:375-382.
    • (2005) Cell , vol.123 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 5
    • 79960559487 scopus 로고    scopus 로고
    • A new approach to the molecular analysis of docking, priming, and regulated membrane fusion
    • Ref Type: Generic
    • Rogasevskaia T.P., Coorssen J.R. A new approach to the molecular analysis of docking, priming, and regulated membrane fusion. J. Chem. Biol. 2011, 4(3):117-136. Ref Type: Generic.
    • (2011) J. Chem. Biol. , vol.4 , Issue.3 , pp. 117-136
    • Rogasevskaia, T.P.1    Coorssen, J.R.2
  • 6
    • 0030949722 scopus 로고    scopus 로고
    • The influence of cholesterol on phospholipid membrane curvature and bending elasticity
    • Chen Z., Rand R.P. The influence of cholesterol on phospholipid membrane curvature and bending elasticity. Biophys. J. 1997, 73:267-276.
    • (1997) Biophys. J. , vol.73 , pp. 267-276
    • Chen, Z.1    Rand, R.P.2
  • 7
    • 33746878419 scopus 로고    scopus 로고
    • Sphingomyelin-enriched microdomains define the efficiency of native Ca(2+)-triggered membrane fusion
    • Rogasevskaia T., Coorssen J.R. Sphingomyelin-enriched microdomains define the efficiency of native Ca(2+)-triggered membrane fusion. J. Cell Sci. 2006, 119:2688-2694.
    • (2006) J. Cell Sci. , vol.119 , pp. 2688-2694
    • Rogasevskaia, T.1    Coorssen, J.R.2
  • 8
    • 0025081987 scopus 로고
    • Effects of cholesterol on the structural transitions induced by diacylglycerol in phosphatidylcholine and phosphatidylethanolamine bilayer systems
    • Coorssen J.R., Rand R.P. Effects of cholesterol on the structural transitions induced by diacylglycerol in phosphatidylcholine and phosphatidylethanolamine bilayer systems. Biochem. Cell Biol. 1990, 68:65-69.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 65-69
    • Coorssen, J.R.1    Rand, R.P.2
  • 9
    • 0035423116 scopus 로고    scopus 로고
    • Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion
    • Kato M., Wickner W. Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J. 2001, 20:4035-4040.
    • (2001) EMBO J. , vol.20 , pp. 4035-4040
    • Kato, M.1    Wickner, W.2
  • 10
    • 70349763277 scopus 로고    scopus 로고
    • Cholesterol, regulated exocytosis, and the physiological fusion
    • Churchward M.A., Coorssen J.R. Cholesterol, regulated exocytosis, and the physiological fusion. Biochem. J. 2009, 423:1-14.
    • (2009) Biochem. J. , vol.423 , pp. 1-14
    • Churchward, M.A.1    Coorssen, J.R.2
  • 11
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • Lang T., Bruns D., Wenzel D., et al. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J. 2001, 20:2202-2213.
    • (2001) EMBO J. , vol.20 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3
  • 12
    • 21244500528 scopus 로고    scopus 로고
    • Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells
    • Salaun C., Gould G.W., Chamberlain L.H. Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells. J. Biol. Chem. 2005, 280:19449-19453.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19449-19453
    • Salaun, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 13
    • 65549087110 scopus 로고    scopus 로고
    • Fusion step-specific influence of cholesterol on SNARE-mediated membrane fusion
    • Chang J., Kim S.A., Lu X., Su Z., Kim S.K., Shin Y.K. Fusion step-specific influence of cholesterol on SNARE-mediated membrane fusion. Biophys. J. 2009, 96:1839-1846.
    • (2009) Biophys. J. , vol.96 , pp. 1839-1846
    • Chang, J.1    Kim, S.A.2    Lu, X.3    Su, Z.4    Kim, S.K.5    Shin, Y.K.6
  • 14
    • 0021779046 scopus 로고
    • Membrane fusion
    • Duzgunes N. Membrane fusion. Subcell. Biochem. 1985, 11:195-286.
    • (1985) Subcell. Biochem. , vol.11 , pp. 195-286
    • Duzgunes, N.1
  • 16
    • 79952922725 scopus 로고    scopus 로고
    • Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers
    • Boettcher J.M., vis-Harrison R.L., Clay M.C., et al. Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers. Biochemistry 2011, 50:2264-2273.
    • (2011) Biochemistry , vol.50 , pp. 2264-2273
    • Boettcher, J.M.1    vis-Harrison, R.L.2    Clay, M.C.3
  • 17
    • 78650336379 scopus 로고    scopus 로고
    • 2+ on the structures of anionic lipid bilayers and biological implication
    • 2+ on the structures of anionic lipid bilayers and biological implication. J. Phys. Chem. B 2010, 114:16978-16988.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16978-16988
    • Yang, H.1    Xu, Y.2    Gao, Z.3    Mao, Y.4    Du, Y.5    Jiang, H.6
  • 18
    • 60849122848 scopus 로고    scopus 로고
    • Calcium binding and head group dipole angle in phosphatidylserine-phosphatidylcholine bilayers
    • Vernier P.T., Ziegler M.J., Dimova R. Calcium binding and head group dipole angle in phosphatidylserine-phosphatidylcholine bilayers. Langmuir 2009, 25:1020-1027.
    • (2009) Langmuir , vol.25 , pp. 1020-1027
    • Vernier, P.T.1    Ziegler, M.J.2    Dimova, R.3
  • 20
    • 0022815250 scopus 로고
    • Morphological responses to calcium-induced interaction of phosphatidylserine-containing vesicles
    • Kachar B., Fuller N., Rand R.P. Morphological responses to calcium-induced interaction of phosphatidylserine-containing vesicles. Biophys. J. 1986, 50:779-788.
    • (1986) Biophys. J. , vol.50 , pp. 779-788
    • Kachar, B.1    Fuller, N.2    Rand, R.P.3
  • 21
    • 0028909698 scopus 로고
    • Structural effects of neutral lipids on divalent cation-induced interactions of phosphatidylserine-containing bilayers
    • Coorssen J.R., Rand R.P. Structural effects of neutral lipids on divalent cation-induced interactions of phosphatidylserine-containing bilayers. Biophys. J. 1995, 68:1009-1018.
    • (1995) Biophys. J. , vol.68 , pp. 1009-1018
    • Coorssen, J.R.1    Rand, R.P.2
  • 22
    • 0024592457 scopus 로고
    • Calcium ion binding between lipid bilayers: the four-component system of phosphatidylserine, phosphatidylcholine, calcium chloride, and water
    • Feigenson G.W. Calcium ion binding between lipid bilayers: the four-component system of phosphatidylserine, phosphatidylcholine, calcium chloride, and water. Biochemistry 1989, 28:1270-1278.
    • (1989) Biochemistry , vol.28 , pp. 1270-1278
    • Feigenson, G.W.1
  • 23
    • 0027470669 scopus 로고
    • Mechanism of activation of protein kinase C: roles of diolein and phosphatidylserine
    • Mosior M., Epand R.M. Mechanism of activation of protein kinase C: roles of diolein and phosphatidylserine. Biochemistry 1993, 32:66-75.
    • (1993) Biochemistry , vol.32 , pp. 66-75
    • Mosior, M.1    Epand, R.M.2
  • 24
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • Bai J., Tucker W.C., Chapman E.R. PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat. Struct. Mol. Biol. 2004, 11:36-44.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 25
    • 48249119533 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion
    • James D.J., Khodthong C., Kowalchyk J.A., Martin T.F. Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion. J. Cell Biol. 2008, 182:355-366.
    • (2008) J. Cell Biol. , vol.182 , pp. 355-366
    • James, D.J.1    Khodthong, C.2    Kowalchyk, J.A.3    Martin, T.F.4
  • 26
    • 0034816468 scopus 로고    scopus 로고
    • Anionic phospholipids are involved in membrane targeting of PI 3-kinase gamma
    • Kirsch C., Wetzker R., Klinger R. Anionic phospholipids are involved in membrane targeting of PI 3-kinase gamma. Biochem. Biophys. Res. Commun. 2001, 282:691-696.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 691-696
    • Kirsch, C.1    Wetzker, R.2    Klinger, R.3
  • 27
    • 0033584339 scopus 로고    scopus 로고
    • Synaptic function modulated by changes in the ratio of synaptotagmin I and IV
    • Littleton J.T., Serano T.L., Rubin G.M., Ganetzky B., Chapman E.R. Synaptic function modulated by changes in the ratio of synaptotagmin I and IV. Nature 1999, 400:757-760.
    • (1999) Nature , vol.400 , pp. 757-760
    • Littleton, J.T.1    Serano, T.L.2    Rubin, G.M.3    Ganetzky, B.4    Chapman, E.R.5
  • 28
    • 0032478796 scopus 로고    scopus 로고
    • Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis
    • Loyet K.M., Kowalchyk J.A., Chaudhary A., Chen J., Prestwich G.D., Martin T.F. Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis. J. Biol. Chem. 1998, 273:8337-8343.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8337-8343
    • Loyet, K.M.1    Kowalchyk, J.A.2    Chaudhary, A.3    Chen, J.4    Prestwich, G.D.5    Martin, T.F.6
  • 29
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • van K.W., Nilsson I., von H.G., de K.B. Anionic phospholipids are determinants of membrane protein topology. EMBO J. 1997, 16:4261-4266.
    • (1997) EMBO J. , vol.16 , pp. 4261-4266
    • van, K.W.1    Nilsson, I.2    von, H.G.3    de, K.B.4
  • 30
    • 33748300590 scopus 로고    scopus 로고
    • Phosphatidic acid- and phosphatidylserine-binding proteins
    • Stace C.L., Ktistakis N.T. Phosphatidic acid- and phosphatidylserine-binding proteins. Biochim. Biophys. Acta 2006, 1761:913-926.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 913-926
    • Stace, C.L.1    Ktistakis, N.T.2
  • 31
    • 77952944942 scopus 로고    scopus 로고
    • The distribution and function of phosphatidylserine in cellular membranes
    • Leventis P.A., Grinstein S. The distribution and function of phosphatidylserine in cellular membranes. Annu. Rev. Biophys. 2010, 39:407-427.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 407-427
    • Leventis, P.A.1    Grinstein, S.2
  • 32
    • 0029966690 scopus 로고    scopus 로고
    • Phospholipase activation and secretion: evidence that PLA2, PLC, and PLD are not essential to exocytosis
    • Coorssen J.R. Phospholipase activation and secretion: evidence that PLA2, PLC, and PLD are not essential to exocytosis. Am. J. Physiol. 1996, 270:C1153-C1163.
    • (1996) Am. J. Physiol. , vol.270
    • Coorssen, J.R.1
  • 34
    • 0028862292 scopus 로고
    • Docked granules, the exocytic burst, and the need for ATP hydrolysis in endocrine cells 1
    • Parsons T.D., Coorssen J.R., Horstmann H., Almers W. Docked granules, the exocytic burst, and the need for ATP hydrolysis in endocrine cells 1. Neuron 1995, 15:1085-1096.
    • (1995) Neuron , vol.15 , pp. 1085-1096
    • Parsons, T.D.1    Coorssen, J.R.2    Horstmann, H.3    Almers, W.4
  • 35
    • 21844444781 scopus 로고    scopus 로고
    • V-SNAREs control exocytosis of vesicles from priming to fusion
    • Borisovska M., Zhao Y., Tsytsyura Y., et al. v-SNAREs control exocytosis of vesicles from priming to fusion. EMBO J. 2005, 24:2114-2126.
    • (2005) EMBO J. , vol.24 , pp. 2114-2126
    • Borisovska, M.1    Zhao, Y.2    Tsytsyura, Y.3
  • 36
    • 33748923996 scopus 로고    scopus 로고
    • Vesicle pools, docking, priming, and release
    • Becherer U., Rettig J. Vesicle pools, docking, priming, and release. Cell Tissue Res. 2006, 326:393-407.
    • (2006) Cell Tissue Res. , vol.326 , pp. 393-407
    • Becherer, U.1    Rettig, J.2
  • 38
    • 0038526319 scopus 로고    scopus 로고
    • Regulated secretion: SNARE density, vesicle fusion and calcium dependence
    • Coorssen J.R., Blank P.S., Albertorio F., et al. Regulated secretion: SNARE density, vesicle fusion and calcium dependence. J. Cell Sci. 2003, 116:2087-2097.
    • (2003) J. Cell Sci. , vol.116 , pp. 2087-2097
    • Coorssen, J.R.1    Blank, P.S.2    Albertorio, F.3
  • 40
    • 0043162015 scopus 로고    scopus 로고
    • Revisiting the role of SNAREs in exocytosis and membrane fusion
    • Szule J.A., Coorssen J.R. Revisiting the role of SNAREs in exocytosis and membrane fusion. Biochim. Biophys. Acta 2003, 1641:121-135.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 121-135
    • Szule, J.A.1    Coorssen, J.R.2
  • 41
    • 0031942615 scopus 로고    scopus 로고
    • A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
    • Ungermann C., Nichols B.J., Pelham H.R., Wickner W. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J. Cell Biol. 1998, 140:61-69.
    • (1998) J. Cell Biol. , vol.140 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.3    Wickner, W.4
  • 42
    • 34248152672 scopus 로고    scopus 로고
    • Phospholipid mediated plasticity in exocytosis observed in PC12 cells
    • Uchiyama Y., Maxson M.M., Sawada T., Nakano A., Ewing A.G. Phospholipid mediated plasticity in exocytosis observed in PC12 cells. Brain Res. 2007, 1151:46-54.
    • (2007) Brain Res. , vol.1151 , pp. 46-54
    • Uchiyama, Y.1    Maxson, M.M.2    Sawada, T.3    Nakano, A.4    Ewing, A.G.5
  • 44
    • 0034121288 scopus 로고    scopus 로고
    • A stage-specific preparation to study the Ca(2+)-triggered fusion steps of exocytosis: rationale and perspectives
    • Zimmerberg J., Blank P.S., Kolosova I., Cho M.S., Tahara M., Coorssen J.R. A stage-specific preparation to study the Ca(2+)-triggered fusion steps of exocytosis: rationale and perspectives. Biochimie 2000, 82:303-314.
    • (2000) Biochimie , vol.82 , pp. 303-314
    • Zimmerberg, J.1    Blank, P.S.2    Kolosova, I.3    Cho, M.S.4    Tahara, M.5    Coorssen, J.R.6
  • 45
    • 49749084725 scopus 로고    scopus 로고
    • Vesicle docking in regulated exocytosis
    • Verhage M., Sorensen J.B. Vesicle docking in regulated exocytosis. Traffic 2008, 9:1414-1424.
    • (2008) Traffic , vol.9 , pp. 1414-1424
    • Verhage, M.1    Sorensen, J.B.2
  • 46
    • 0034130649 scopus 로고    scopus 로고
    • Priming in exocytosis: attaining fusion-competence after vesicle docking
    • Klenchin V.A., Martin T.F. Priming in exocytosis: attaining fusion-competence after vesicle docking. Biochimie 2000, 82:399-407.
    • (2000) Biochimie , vol.82 , pp. 399-407
    • Klenchin, V.A.1    Martin, T.F.2
  • 47
    • 0031774259 scopus 로고    scopus 로고
    • Submaximal responses in calcium-triggered exocytosis are explained by differences in the calcium sensitivity of individual secretory vesicles
    • Blank P.S., Cho M.S., Vogel S.S., et al. Submaximal responses in calcium-triggered exocytosis are explained by differences in the calcium sensitivity of individual secretory vesicles. J. Gen. Physiol. 1998, 112:559-567.
    • (1998) J. Gen. Physiol. , vol.112 , pp. 559-567
    • Blank, P.S.1    Cho, M.S.2    Vogel, S.S.3
  • 48
    • 22844432854 scopus 로고    scopus 로고
    • New reagents for phosphatidylserine recognition and detection of apoptosis
    • Hanshaw R.G., Smith B.D. New reagents for phosphatidylserine recognition and detection of apoptosis. Bioorg. Med. Chem. 2005, 13:5035-5042.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 5035-5042
    • Hanshaw, R.G.1    Smith, B.D.2
  • 49
    • 0010537002 scopus 로고
    • Neomycin inhibits the phosphatidylinositol monophosphate and phosphatidylinositol bisphosphate stimulation of plasma membrane ATPase activity
    • Chen Q., Boss W.F. Neomycin inhibits the phosphatidylinositol monophosphate and phosphatidylinositol bisphosphate stimulation of plasma membrane ATPase activity. Plant Physiol. 1991, 96:340-343.
    • (1991) Plant Physiol. , vol.96 , pp. 340-343
    • Chen, Q.1    Boss, W.F.2
  • 50
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E., Dyer W. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 1959, 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.1    Dyer, W.2
  • 51
    • 61349195290 scopus 로고    scopus 로고
    • Copper (II) sulfate charring for high sensitivity on-plate fluorescent detection of lipids and sterols: quantitative analyses of the composition of functional secretory vesicles
    • Churchward M.A., Brandman D.M., Rogasevskaia T., Coorssen J.R. Copper (II) sulfate charring for high sensitivity on-plate fluorescent detection of lipids and sterols: quantitative analyses of the composition of functional secretory vesicles. J. Chem. Biol. 2008, 1:79-87.
    • (2008) J. Chem. Biol. , vol.1 , pp. 79-87
    • Churchward, M.A.1    Brandman, D.M.2    Rogasevskaia, T.3    Coorssen, J.R.4
  • 53
    • 0025366069 scopus 로고
    • Interaction of calcium and cholesterol sulphate induces membrane destabilization and fusion: implications for the acrosome reaction
    • Cheetham J.J., Chen R.J., Epand R.M. Interaction of calcium and cholesterol sulphate induces membrane destabilization and fusion: implications for the acrosome reaction. Biochim. Biophys. Acta 1990, 1024:367-372.
    • (1990) Biochim. Biophys. Acta , vol.1024 , pp. 367-372
    • Cheetham, J.J.1    Chen, R.J.2    Epand, R.M.3
  • 54
    • 65149101397 scopus 로고    scopus 로고
    • Enhancement of the Ca(2+)-triggering steps of native membrane fusion via thiol-reactivity
    • Furber K.L., Brandman D.M., Coorssen J.R. Enhancement of the Ca(2+)-triggering steps of native membrane fusion via thiol-reactivity. J. Chem. Biol. 2009, 2:27-37.
    • (2009) J. Chem. Biol. , vol.2 , pp. 27-37
    • Furber, K.L.1    Brandman, D.M.2    Coorssen, J.R.3
  • 55
    • 29244475366 scopus 로고    scopus 로고
    • Actin is not an essential component in the mechanism of calcium-triggered vesicle fusion
    • Hibbert J.E., Butt R.H., Coorssen J.R. Actin is not an essential component in the mechanism of calcium-triggered vesicle fusion. Int. J. Biochem. Cell Biol. 2006, 38:461-471.
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 461-471
    • Hibbert, J.E.1    Butt, R.H.2    Coorssen, J.R.3
  • 56
    • 0042090267 scopus 로고    scopus 로고
    • Calcium-triggered membrane fusion proceeds independently of specific presynaptic proteins
    • Szule J.A., Jarvis S.E., Hibbert J.E., et al. Calcium-triggered membrane fusion proceeds independently of specific presynaptic proteins. J. Biol. Chem. 2003, 278:24251-24254.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24251-24254
    • Szule, J.A.1    Jarvis, S.E.2    Hibbert, J.E.3
  • 57
    • 0029943482 scopus 로고    scopus 로고
    • Poisson-distributed active fusion complexes underlie the control of the rate and extent of exocytosis by calcium
    • Vogel S.S., Blank P.S., Zimmerberg J. Poisson-distributed active fusion complexes underlie the control of the rate and extent of exocytosis by calcium. J. Cell Biol. 1996, 134:329-338.
    • (1996) J. Cell Biol. , vol.134 , pp. 329-338
    • Vogel, S.S.1    Blank, P.S.2    Zimmerberg, J.3
  • 58
    • 0016705406 scopus 로고
    • The isolation of intact cortical granules from sea urchin eggs: calcium ions trigger granule discharge
    • Vacquier V.D. The isolation of intact cortical granules from sea urchin eggs: calcium ions trigger granule discharge. Dev. Biol. 1975, 43:62-74.
    • (1975) Dev. Biol. , vol.43 , pp. 62-74
    • Vacquier, V.D.1
  • 59
    • 0032509210 scopus 로고    scopus 로고
    • Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion
    • Tahara M., Coorssen J.R., Timmers K., et al. Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion. J. Biol. Chem. 1998, 273:33667-33673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33667-33673
    • Tahara, M.1    Coorssen, J.R.2    Timmers, K.3
  • 61
    • 0021110010 scopus 로고
    • Calcium-dependent exocytosis in an in vitro secretory granule plasma membrane preparation from sea urchin eggs and the effects of some inhibitors of cytoskeletal function
    • Whitaker M.J., Baker P.F. Calcium-dependent exocytosis in an in vitro secretory granule plasma membrane preparation from sea urchin eggs and the effects of some inhibitors of cytoskeletal function. Proc. R. Soc. Lond. B: Biol. Sci. 1983, 218:397-413.
    • (1983) Proc. R. Soc. Lond. B: Biol. Sci. , vol.218 , pp. 397-413
    • Whitaker, M.J.1    Baker, P.F.2
  • 62
    • 34147109686 scopus 로고    scopus 로고
    • Sea urchin genome confirms kinship to humans and other vertebrates 148
    • Genetics Pennisi E. Sea urchin genome confirms kinship to humans and other vertebrates 148. Science 2006, 314:908-909.
    • (2006) Science , vol.314 , pp. 908-909
    • Genetics, P.E.1
  • 63
    • 0032562636 scopus 로고    scopus 로고
    • 2+-dependent manner. In vitro characteristics and possible significance
    • 2+-dependent manner. In vitro characteristics and possible significance. J. Biol. Chem. 1998, 273:10240-10248.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10240-10248
    • Chung, S.H.1    Song, W.J.2    Kim, K.3
  • 64
    • 34147117628 scopus 로고    scopus 로고
    • Phosphatidic acid domains in membranes: effect of divalent counterions
    • Faraudo J., Travesset A. Phosphatidic acid domains in membranes: effect of divalent counterions. Biophys. J. 2007, 92:2806-2818.
    • (2007) Biophys. J. , vol.92 , pp. 2806-2818
    • Faraudo, J.1    Travesset, A.2
  • 65
    • 0025728518 scopus 로고
    • Actin binding proteins-lipid interactions
    • Isenberg G. Actin binding proteins-lipid interactions. J. Muscle Res. Cell Motil. 1991, 12:136-144.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 136-144
    • Isenberg, G.1
  • 66
    • 33750508753 scopus 로고    scopus 로고
    • Ahead of the curve: mitochondrial fusion and phospholipase D
    • Jensen R.E., Sesaki H. Ahead of the curve: mitochondrial fusion and phospholipase D. Nat. Cell Biol. 2006, 8:1215-1217.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1215-1217
    • Jensen, R.E.1    Sesaki, H.2
  • 67
    • 61449152986 scopus 로고    scopus 로고
    • Phosphatidylinositol metabolism and membrane fusion
    • Poccia D., Larijani B. Phosphatidylinositol metabolism and membrane fusion. Biochem. J. 2009, 418:233-246.
    • (2009) Biochem. J. , vol.418 , pp. 233-246
    • Poccia, D.1    Larijani, B.2
  • 68
    • 1942520207 scopus 로고    scopus 로고
    • 2+-regulated membrane fusion by synaptotagmin and SNAREs
    • 2+-regulated membrane fusion by synaptotagmin and SNAREs. Science 2004, 304:435-438.
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 69
    • 66349122907 scopus 로고    scopus 로고
    • Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol
    • Murray D.H., Tamm L.K. Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol. Biochemistry 2009, 48:4617-4625.
    • (2009) Biochemistry , vol.48 , pp. 4617-4625
    • Murray, D.H.1    Tamm, L.K.2
  • 70
    • 33746478107 scopus 로고    scopus 로고
    • Phosphoinositide regulation of neuroexocytosis: adding to the complexity
    • Osborne S.L., Wen P.J., Meunier F.A. Phosphoinositide regulation of neuroexocytosis: adding to the complexity. J. Neurochem. 2006, 98:336-342.
    • (2006) J. Neurochem. , vol.98 , pp. 336-342
    • Osborne, S.L.1    Wen, P.J.2    Meunier, F.A.3
  • 71
    • 0030843265 scopus 로고    scopus 로고
    • Mechanism of alpha-cyclodextrin-induced hemolysis. 1. The two-step extraction of phosphatidylinositol from the membrane
    • Fauvelle F., Debouzy J.C., Crouzy S., Goschl M., Chapron Y. Mechanism of alpha-cyclodextrin-induced hemolysis. 1. The two-step extraction of phosphatidylinositol from the membrane. J. Pharm. Sci. 1997, 86:935-943.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 935-943
    • Fauvelle, F.1    Debouzy, J.C.2    Crouzy, S.3    Goschl, M.4    Chapron, Y.5
  • 72
    • 0038093145 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus
    • Ruiz-Arguello M.B., Goni F.M., Pereira F.B., Nieva J.L. Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus. J. Virol. 1998, 72:1775-1781.
    • (1998) J. Virol. , vol.72 , pp. 1775-1781
    • Ruiz-Arguello, M.B.1    Goni, F.M.2    Pereira, F.B.3    Nieva, J.L.4
  • 73
    • 0038303159 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic beta cells
    • Olsen H.L., Hoy M., Zhang W., et al. Phosphatidylinositol 4-kinase serves as a metabolic sensor and regulates priming of secretory granules in pancreatic beta cells. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:5187-5192.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5187-5192
    • Olsen, H.L.1    Hoy, M.2    Zhang, W.3
  • 74
    • 34547101964 scopus 로고    scopus 로고
    • Identification of secretory granule phosphatidylinositol 4,5-bisphosphate-interacting proteins using an affinity pulldown strategy
    • Osborne S.L., Wallis T.P., Jimenez J.L., Gorman J.J., Meunier F.A. Identification of secretory granule phosphatidylinositol 4,5-bisphosphate-interacting proteins using an affinity pulldown strategy. Mol. Cell. Proteomics 2007, 6:1158-1169.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1158-1169
    • Osborne, S.L.1    Wallis, T.P.2    Jimenez, J.L.3    Gorman, J.J.4    Meunier, F.A.5
  • 75
    • 0042490720 scopus 로고    scopus 로고
    • Synapsin I-associated phosphatidylinositol 3-kinase mediates synaptic vesicle delivery to the readily releasable pool 16
    • Cousin M.A., Malladi C.S., Tan T.C., Raymond C.R., Smillie K.J., Robinson P.J. Synapsin I-associated phosphatidylinositol 3-kinase mediates synaptic vesicle delivery to the readily releasable pool 16. J. Biol. Chem. 2003, 278:29065-29071.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29065-29071
    • Cousin, M.A.1    Malladi, C.S.2    Tan, T.C.3    Raymond, C.R.4    Smillie, K.J.5    Robinson, P.J.6
  • 76
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 2002, 296:1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 77
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G., De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature 2006, 443:651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 78
    • 34248209063 scopus 로고    scopus 로고
    • Phosphoinositides: regulators of membrane traffic and protein function
    • Krauss M., Haucke V. Phosphoinositides: regulators of membrane traffic and protein function. FEBS Lett. 2007, 581:2105-2111.
    • (2007) FEBS Lett. , vol.581 , pp. 2105-2111
    • Krauss, M.1    Haucke, V.2
  • 79
    • 36049025863 scopus 로고    scopus 로고
    • CAPS-1 and CAPS-2 are essential synaptic vesicle priming proteins
    • Jockusch W.J., Speidel D., Sigler A., et al. CAPS-1 and CAPS-2 are essential synaptic vesicle priming proteins. Cell 2007, 131:796-808.
    • (2007) Cell , vol.131 , pp. 796-808
    • Jockusch, W.J.1    Speidel, D.2    Sigler, A.3
  • 80
    • 77957861153 scopus 로고    scopus 로고
    • Spatial regulation of membrane fusion controlled by modification of phosphoinositides
    • Dumas F., Byrne R.D., Vincent B., Hobday T.M., Poccia D.L., Larijani B. Spatial regulation of membrane fusion controlled by modification of phosphoinositides. PLoS One 2010, 5(8):e12208.
    • (2010) PLoS One , vol.5 , Issue.8
    • Dumas, F.1    Byrne, R.D.2    Vincent, B.3    Hobday, T.M.4    Poccia, D.L.5    Larijani, B.6
  • 81
    • 33845345255 scopus 로고    scopus 로고
    • Polyunsaturated phosphatidylinositol and diacylglycerol substantially modify the fluidity and polymorphism of biomembranes: a solid-state deuterium NMR study
    • Larijani B., Dufourc E.J. Polyunsaturated phosphatidylinositol and diacylglycerol substantially modify the fluidity and polymorphism of biomembranes: a solid-state deuterium NMR study. Lipids 2006, 41:925-932.
    • (2006) Lipids , vol.41 , pp. 925-932
    • Larijani, B.1    Dufourc, E.J.2
  • 82
    • 84863065893 scopus 로고    scopus 로고
    • Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion
    • Wang Z., Liu H., Gu Y., Chapman E.R. Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion. J. Cell Biol. 2011, 195:1159-1170.
    • (2011) J. Cell Biol. , vol.195 , pp. 1159-1170
    • Wang, Z.1    Liu, H.2    Gu, Y.3    Chapman, E.R.4
  • 84
    • 0027079931 scopus 로고
    • Calcium-triggered fusion of exocytotic granules requires proteins in only one membrane
    • Vogel S.S., Chernomordik L.V., Zimmerberg J. Calcium-triggered fusion of exocytotic granules requires proteins in only one membrane. J. Biol. Chem. 1992, 267:25640-25643.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25640-25643
    • Vogel, S.S.1    Chernomordik, L.V.2    Zimmerberg, J.3
  • 85
    • 0032900153 scopus 로고    scopus 로고
    • Calcium-induced fusion of sea urchin egg secretory vesicles with planar phospholipid bilayer membranes
    • Chanturiya A., Whitaker M., Zimmerberg J. Calcium-induced fusion of sea urchin egg secretory vesicles with planar phospholipid bilayer membranes. Mol. Membr. Biol. 1999, 16:89-94.
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 89-94
    • Chanturiya, A.1    Whitaker, M.2    Zimmerberg, J.3
  • 88
    • 34147092000 scopus 로고    scopus 로고
    • Point-like protrusion as a prestalk intermediate in membrane fusion pathway 6
    • Efrat A., Chernomordik L.V., Kozlov M.M. Point-like protrusion as a prestalk intermediate in membrane fusion pathway 6. Biophys. J. 2007, 92:L61-L63.
    • (2007) Biophys. J. , vol.92
    • Efrat, A.1    Chernomordik, L.V.2    Kozlov, M.M.3
  • 90
    • 0346147032 scopus 로고    scopus 로고
    • Detection of apoptotic cells using a synthetic fluorescent sensor for membrane surfaces that contain phosphatidylserine
    • Koulov A.V., Stucker K.A., Lakshmi C., Robinson J.P., Smith B.D. Detection of apoptotic cells using a synthetic fluorescent sensor for membrane surfaces that contain phosphatidylserine. Cell Death Differ. 2003, 10:1357-1359.
    • (2003) Cell Death Differ. , vol.10 , pp. 1357-1359
    • Koulov, A.V.1    Stucker, K.A.2    Lakshmi, C.3    Robinson, J.P.4    Smith, B.D.5
  • 91
    • 80054082012 scopus 로고    scopus 로고
    • Phosphatidylserine directly and positively regulates fusion of myoblasts into myotubes
    • Jeong J., Conboy I.M. Phosphatidylserine directly and positively regulates fusion of myoblasts into myotubes. Biochem. Biophys. Res. Commun. 2011, 414:9-13.
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 9-13
    • Jeong, J.1    Conboy, I.M.2
  • 93
    • 0026788468 scopus 로고
    • Differential stimulation of protein kinase C activity by phorbol ester or calcium/phosphatidylserine in vitro and in intact synaptosomes
    • Robinson P.J. Differential stimulation of protein kinase C activity by phorbol ester or calcium/phosphatidylserine in vitro and in intact synaptosomes. J. Biol. Chem. 1992, 267:21637-21644.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21637-21644
    • Robinson, P.J.1
  • 94
    • 79960149724 scopus 로고    scopus 로고
    • Synaptotagmin 1 modulates lipid acyl chain order in lipid bilayers by demixing phosphatidylserine
    • Lai A.L., Tamm L.K., Ellena J.F., Cafiso D.S. Synaptotagmin 1 modulates lipid acyl chain order in lipid bilayers by demixing phosphatidylserine. J. Biol. Chem. 2011, 286:25291-25300.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25291-25300
    • Lai, A.L.1    Tamm, L.K.2    Ellena, J.F.3    Cafiso, D.S.4
  • 95
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • Fratti R.A., Jun Y., Merz A.J., Margolis N., Wickner W. Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles. J. Cell Biol. 2004, 167:1087-1098.
    • (2004) J. Cell Biol. , vol.167 , pp. 1087-1098
    • Fratti, R.A.1    Jun, Y.2    Merz, A.J.3    Margolis, N.4    Wickner, W.5
  • 97
    • 78249268540 scopus 로고    scopus 로고
    • Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane
    • Domanska M.K., Kiessling V., Tamm L.K. Docking and fast fusion of synaptobrevin vesicles depends on the lipid compositions of the vesicle and the acceptor SNARE complex-containing target membrane. Biophys. J. 2010, 99:2936-2946.
    • (2010) Biophys. J. , vol.99 , pp. 2936-2946
    • Domanska, M.K.1    Kiessling, V.2    Tamm, L.K.3
  • 98
    • 82455188329 scopus 로고    scopus 로고
    • Putting the pH into phosphatidic acid signaling
    • Shin J.J., Loewen C.J. Putting the pH into phosphatidic acid signaling. BMC Biol. 2011, 9:85.
    • (2011) BMC Biol. , vol.9 , pp. 85
    • Shin, J.J.1    Loewen, C.J.2
  • 99
    • 29344473783 scopus 로고    scopus 로고
    • What makes the bioactive lipids phosphatidic acid and lysophosphatidic acid so special?
    • Kooijman E.E., Carter K.M., van Laar E.G., Chupin V., Burger K.N., de K.B. What makes the bioactive lipids phosphatidic acid and lysophosphatidic acid so special?. Biochemistry 2005, 44:17007-17015.
    • (2005) Biochemistry , vol.44 , pp. 17007-17015
    • Kooijman, E.E.1    Carter, K.M.2    van Laar, E.G.3    Chupin, V.4    Burger, K.N.5    de, K.B.6
  • 100
    • 79957613290 scopus 로고    scopus 로고
    • A new role for the dynamin GTPase in the regulation of fusion pore expansion
    • Anantharam A., Bittner M.A., Aikman R.L., et al. A new role for the dynamin GTPase in the regulation of fusion pore expansion. Mol. Biol. Cell 2011, 22:1907-1918.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1907-1918
    • Anantharam, A.1    Bittner, M.A.2    Aikman, R.L.3
  • 101
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner T., Bennett M.K., Whiteheart S.W., Scheller R.H., Rothman J.E. A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 1993, 75:409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Sollner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 102
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: minimal machinery for membrane fusion
    • Weber T., Zemelman B.V., McNew J.A., et al. SNAREpins: minimal machinery for membrane fusion. Cell 1998, 92:759-772.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.