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Volumn 7, Issue 2, 2007, Pages 142-153

Protein and lipid signaling in membrane fusion: Nuclear envelope assembly

Author keywords

Diacylglycerol; Nuclear envelope; Phosphatidylinositol; PLC

Indexed keywords

MEMBRANE PHOSPHOLIPID; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHOLIPASE C GAMMA;

EID: 34248221198     PISSN: 16154053     EISSN: 16154061     Source Type: Journal    
DOI: 10.1002/sita.200600128     Document Type: Review
Times cited : (9)

References (78)
  • 1
    • 28844486078 scopus 로고    scopus 로고
    • Neuroscience. Synaptic membranes bend to the will of a neurotoxin
    • Zimmerberg, J., Chernomordik, L.V. (2005) Neuroscience. Synaptic membranes bend to the will of a neurotoxin. Science 310:1626-1627.
    • (2005) Science , vol.310 , pp. 1626-1627
    • Zimmerberg, J.1    Chernomordik, L.V.2
  • 2
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik, L.V., Kozlov, M.M. (2003) Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 72:175-207.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 3
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., Lang, T., Sudhof, T.C (2003) Membrane fusion. Cell 112: 519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 4
    • 0032549708 scopus 로고    scopus 로고
    • SNAREpins: Minimal machinery for membrane fusion
    • Weber, T., Zemelman, B.V., McNew, J.A., Westermann, B., et al. (1998) SNAREpins: minimal machinery for membrane fusion. Cell 92: 759-772.
    • (1998) Cell , vol.92 , pp. 759-772
    • Weber, T.1    Zemelman, B.V.2    McNew, J.A.3    Westermann, B.4
  • 5
    • 0035371723 scopus 로고    scopus 로고
    • How can proteolipids be central players in membrane fusion?
    • Zimmerberg, J. (2001) How can proteolipids be central players in membrane fusion? Trends Cell Biol. 11: 233-235.
    • (2001) Trends Cell Biol , vol.11 , pp. 233-235
    • Zimmerberg, J.1
  • 6
    • 33646019290 scopus 로고    scopus 로고
    • Membrane biophysics
    • Zimmerberg, J. (2006) Membrane biophysics. Curr. Biol. 16: R272-276.
    • (2006) Curr. Biol , vol.16
    • Zimmerberg, J.1
  • 7
    • 0025887748 scopus 로고
    • Organization of the sea urchin egg endoplasmic reticulum and its reorganization at fertilization
    • Terasaki, M., Jaffe, L.A. (1991) Organization of the sea urchin egg endoplasmic reticulum and its reorganization at fertilization. J. Cell Biol. 114: 929-940.
    • (1991) J. Cell Biol , vol.114 , pp. 929-940
    • Terasaki, M.1    Jaffe, L.A.2
  • 8
    • 0014353919 scopus 로고
    • The fine structure of pro-nuclear development and fusion in the sea urchin
    • Longo, F.J., Anderson, E. (1968) The fine structure of pro-nuclear development and fusion in the sea urchin, Arbacia punctulata. J. Cell Biol. 39: 339-368.
    • (1968) Arbacia punctulata. J. Cell Biol , vol.39 , pp. 339-368
    • Longo, F.J.1    Anderson, E.2
  • 9
    • 0017282818 scopus 로고
    • Derivation of the membrane comprising the male pronuclear envelope in inseminated sea urchin eggs
    • Longo, F.J. (1976) Derivation of the membrane comprising the male pronuclear envelope in inseminated sea urchin eggs. Dev. Biol. 49: 347-368.
    • (1976) Dev. Biol , vol.49 , pp. 347-368
    • Longo, F.J.1
  • 10
    • 30844455364 scopus 로고    scopus 로고
    • The nuclear envelope: Form and reformation
    • Prunuske, A.J., Ullman, K.S. (2006) The nuclear envelope: form and reformation. Curr. Opin. Cell Biol. 18: 108-116.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 108-116
    • Prunuske, A.J.1    Ullman, K.S.2
  • 11
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka, M.J., Masui, Y. (1983) Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220: 719-721.
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 12
    • 0022517260 scopus 로고
    • A cell free system to study reassembly of the nuclear envelope at the end of mitosis
    • Burke, B., Gerace, L. (1986) A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 44: 639-652.
    • (1986) Cell , vol.44 , pp. 639-652
    • Burke, B.1    Gerace, L.2
  • 13
    • 0028299148 scopus 로고
    • In vitro development of the sea urchin male pronucleus
    • Cameron, L.A., Poccia, D.L. (1994) In vitro development of the sea urchin male pronucleus. Dev. Biol. 162: 568-578.
    • (1994) Dev. Biol , vol.162 , pp. 568-578
    • Cameron, L.A.1    Poccia, D.L.2
  • 14
  • 15
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial, M., McBride, H. (2001) Rab proteins as membrane organizers. Nat. Rev. Mol Cell Biol. 2:107-117.
    • (2001) Nat. Rev. Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 16
    • 33751269381 scopus 로고    scopus 로고
    • Interactions between Rabs, tethers, SNAREs and their regulators in exocytosis
    • Novick, P., Medkova, M., Dong, G., Hutagalung, A., et al. (2006) Interactions between Rabs, tethers, SNAREs and their regulators in exocytosis. Biochem. Soc. Trans. 34: 683-686.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 683-686
    • Novick, P.1    Medkova, M.2    Dong, G.3    Hutagalung, A.4
  • 17
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • Grosshans, B.L., Ortiz, D., Novick, P. (2006) Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. U.S.A. 103: 11821-11827.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 18
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg, J., Siggia, E.D., Moreira, J.E., Smith, C.L., et al. (1997) Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138: 1193-1206.
    • (1997) J. Cell Biol , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4
  • 19
    • 0026071202 scopus 로고
    • A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs
    • Vigers, G.P.A., Lohka, M.J. (1991) A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs. J. Cell. Biol. 112: 545-556.
    • (1991) J. Cell. Biol , vol.112 , pp. 545-556
    • Vigers, G.P.A.1    Lohka, M.J.2
  • 20
    • 0032834360 scopus 로고    scopus 로고
    • In vitro nuclear assembly with affinity-purified nuclear envelope precursor vesicle fractions, PV1 and PV2
    • Sasagawa, S., Yamamoto, A., Ichimura, T., Omata, S., Horigome, T. (1999) In vitro nuclear assembly with affinity-purified nuclear envelope precursor vesicle fractions, PV1 and PV2. Eur. J. Cell Biol. 78: 593-600.
    • (1999) Eur. J. Cell Biol , vol.78 , pp. 593-600
    • Sasagawa, S.1    Yamamoto, A.2    Ichimura, T.3    Omata, S.4    Horigome, T.5
  • 21
    • 0033601757 scopus 로고    scopus 로고
    • Temporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types
    • Drummond, S., Ferrigno, P., Lyon, C, Murphy, J., et al. (1999) Temporal differences in the appearance of NEP-B78 and an LBR-like protein during Xenopus nuclear envelope reassembly reflect the ordered recruitment of functionally discrete vesicle types. J. Cell Biol. 144: 225-240.
    • (1999) J. Cell Biol , vol.144 , pp. 225-240
    • Drummond, S.1    Ferrigno, P.2    Lyon, C.3    Murphy, J.4
  • 22
    • 0036306726 scopus 로고    scopus 로고
    • The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly
    • Hetzer, M., Gruss, O.J., Mattaj, I.W. (2002) The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nat. Cell Biol. 4: E177-184.
    • (2002) Nat. Cell Biol , vol.4
    • Hetzer, M.1    Gruss, O.J.2    Mattaj, I.W.3
  • 24
    • 0026661397 scopus 로고
    • Packaging and unpackaging the sea urchin genome
    • Poccia, D.L., Green, G.R. (1992) Packaging and unpackaging the sea urchin genome. Trends Biochem. Sci. 17: 223-227.
    • (1992) Trends Biochem. Sci , vol.17 , pp. 223-227
    • Poccia, D.L.1    Green, G.R.2
  • 25
    • 0036019137 scopus 로고    scopus 로고
    • Two kinase activities are sufficient for sea urchin sperm chromatin decondensation in vitro
    • Stephens, S., Beyer, B., Balthazar-Stablein, U., Duncan, R., et al. (2002) Two kinase activities are sufficient for sea urchin sperm chromatin decondensation in vitro. Molec. Reprod. Dev. 62:496-503.
    • (2002) Molec. Reprod. Dev , vol.62 , pp. 496-503
    • Stephens, S.1    Beyer, B.2    Balthazar-Stablein, U.3    Duncan, R.4
  • 26
    • 0037229320 scopus 로고    scopus 로고
    • Nuclear envelope dynamics in oocytes: From germinal vesicle breakdown to mitosis
    • Lenart, P., Ellenberg, J. (2003) Nuclear envelope dynamics in oocytes: from germinal vesicle breakdown to mitosis. Curr. Opin. Cell Biol. 15: 88-95.
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 88-95
    • Lenart, P.1    Ellenberg, J.2
  • 27
    • 0031961741 scopus 로고    scopus 로고
    • Methods for studying in vitro assembly of male pronuclei using extracts from marine invertebrates: Sea urchins and surf clams
    • Collas, P., Poccia, D. (1998) Methods for studying in vitro assembly of male pronuclei using extracts from marine invertebrates: sea urchins and surf clams. Meth. Cell Biol. 53:417-452.
    • (1998) Meth. Cell Biol , vol.53 , pp. 417-452
    • Collas, P.1    Poccia, D.2
  • 29
    • 33750995860 scopus 로고    scopus 로고
    • The genome of the sea urchin Strongylocentrotus purpuratus
    • Sodergren, E., Weinstock, G.M., Davidson, E.H., Cameron, R.A., et al. (2006) The genome of the sea urchin Strongylocentrotus purpuratus. Science 314: 941-952.
    • (2006) Science , vol.314 , pp. 941-952
    • Sodergren, E.1    Weinstock, G.M.2    Davidson, E.H.3    Cameron, R.A.4
  • 30
    • 0029688692 scopus 로고    scopus 로고
    • Transforming sperm nuclei into male pronuclei in vivo and in vitro
    • Poccia, D., Collas, P. (1996) Transforming sperm nuclei into male pronuclei in vivo and in vitro. Curr. Top. Dev Biol 34: 25-88.
    • (1996) Curr. Top. Dev Biol , vol.34 , pp. 25-88
    • Poccia, D.1    Collas, P.2
  • 31
    • 0030885543 scopus 로고    scopus 로고
    • Nuclear envelope dynamics during male pronuclear development
    • Poccia, D., Collas, P. (1997) Nuclear envelope dynamics during male pronuclear development. Dev. Growth Differ. 39: 541-550.
    • (1997) Dev. Growth Differ , vol.39 , pp. 541-550
    • Poccia, D.1    Collas, P.2
  • 32
    • 0031919531 scopus 로고    scopus 로고
    • Remodeling the sperm nucleus into a male pronucleus at fertilization
    • Collas, P., Poccia, D. (1998) Remodeling the sperm nucleus into a male pronucleus at fertilization. Theriogenology 49: 67-81.
    • (1998) Theriogenology , vol.49 , pp. 67-81
    • Collas, P.1    Poccia, D.2
  • 33
    • 0033658702 scopus 로고    scopus 로고
    • Membrane fusion events during nuclear envelope assembly
    • Collas, P., Poccia, D. (2000) Membrane fusion events during nuclear envelope assembly. Subcell. Biochem. 34: 273-302.
    • (2000) Subcell. Biochem , vol.34 , pp. 273-302
    • Collas, P.1    Poccia, D.2
  • 34
    • 0027302306 scopus 로고
    • Two steps required for male pronucleus formation in the sea urchin egg
    • Cothren, C.C, Poccia, D.L. (1993) Two steps required for male pronucleus formation in the sea urchin egg. Exp. Cell Res. 205: 126-133.
    • (1993) Exp. Cell Res , vol.205 , pp. 126-133
    • Cothren, C.C.1    Poccia, D.L.2
  • 35
  • 36
    • 0029135338 scopus 로고
    • Formation of the sea urchin male pronucleus in vitro: Membrane-independent chromatin decondensation and nuclear-envelope dependent nuclear swelling
    • Collas, P., Poccia, D. (1995) Formation of the sea urchin male pronucleus in vitro: Membrane-independent chromatin decondensation and nuclear-envelope dependent nuclear swelling. Molec. Reprod. Dev. 42: 106-113.
    • (1995) Molec. Reprod. Dev , vol.42 , pp. 106-113
    • Collas, P.1    Poccia, D.2
  • 37
    • 0029055578 scopus 로고
    • Lipophilic organizing structures of sperm nuclei target membrane vesicle binding and are incorporated into the nuclear envelope
    • Collas, P., Poccia, D. (1995) Lipophilic organizing structures of sperm nuclei target membrane vesicle binding and are incorporated into the nuclear envelope. Dev. Biol. 169: 123-135.
    • (1995) Dev. Biol , vol.169 , pp. 123-135
    • Collas, P.1    Poccia, D.2
  • 38
    • 0033967894 scopus 로고    scopus 로고
    • Rearrangements of sea urchin egg cytoplasmic membrane domains at fertilization
    • Collas, P., Barona, T., Poccia, D.L. (2000) Rearrangements of sea urchin egg cytoplasmic membrane domains at fertilization. Eur. J. Cell Biol. 79: 10-16.
    • (2000) Eur. J. Cell Biol , vol.79 , pp. 10-16
    • Collas, P.1    Barona, T.2    Poccia, D.L.3
  • 39
    • 0014525362 scopus 로고
    • Sperm differentiation in the sea urchins Arbacia punctulata and Strongylocentrotus purpuratus
    • Longo, F.J., Anderson, E. (1969) Sperm differentiation in the sea urchins Arbacia punctulata and Strongylocentrotus purpuratus. J. Ultrastnicl. Res. 27: 486-499.
    • (1969) J. Ultrastnicl. Res , vol.27 , pp. 486-499
    • Longo, F.J.1    Anderson, E.2
  • 40
    • 2342501915 scopus 로고    scopus 로고
    • Chromatin organization during spermiogenesis in Octopus vulgaris. I: Morphological structures
    • Ribes, E., Gimenez-Bonafe, P., Martinez-Soler, F., Gonzalez, A., et al. (2004) Chromatin organization during spermiogenesis in Octopus vulgaris. I: Morphological structures. Mol. Reprod. Dev. 68: 223-231.
    • (2004) Mol. Reprod. Dev , vol.68 , pp. 223-231
    • Ribes, E.1    Gimenez-Bonafe, P.2    Martinez-Soler, F.3    Gonzalez, A.4
  • 42
    • 0029837908 scopus 로고    scopus 로고
    • Conserved binding recognition elements of sperm chromatin, sperm lipophilic structures and nuclear envelope precursor vesicles
    • Collas, P., Poccia, D. (1996) Conserved binding recognition elements of sperm chromatin, sperm lipophilic structures and nuclear envelope precursor vesicles. Eur. J. Cell Biol. 71: 22-32.
    • (1996) Eur. J. Cell Biol , vol.71 , pp. 22-32
    • Collas, P.1    Poccia, D.2
  • 43
    • 0029982203 scopus 로고    scopus 로고
    • Distinct egg cytoplasmic membrane vesicles differing in binding and fusion properties contribute to sea urchin male pronuclear envelopes formed in vitro
    • Collas, P., Poccia, D. (1996) Distinct egg cytoplasmic membrane vesicles differing in binding and fusion properties contribute to sea urchin male pronuclear envelopes formed in vitro. J. Cell Sci. 109: 1275-1283.
    • (1996) J. Cell Sci , vol.109 , pp. 1275-1283
    • Collas, P.1    Poccia, D.2
  • 44
    • 0030885543 scopus 로고    scopus 로고
    • Nuclear envelope dynamics during male pronuclear development
    • Poccia, D., Collas, P. (1997) Nuclear envelope dynamics during male pronuclear development. Devel. Growth Differ. 39: 541-550.
    • (1997) Devel. Growth Differ , vol.39 , pp. 541-550
    • Poccia, D.1    Collas, P.2
  • 45
    • 0030461544 scopus 로고    scopus 로고
    • Targeting of membranes to sea urchin sperm chromatin is mediated by an LBR-like integral membrane protein
    • Collas, P., Courvalin, J.-C, Poccia, D. (1996) Targeting of membranes to sea urchin sperm chromatin is mediated by an LBR-like integral membrane protein. J. Cell Biol. 135: 1715-1725.
    • (1996) J. Cell Biol , vol.135 , pp. 1715-1725
    • Collas, P.1    Courvalin, J.-C.2    Poccia, D.3
  • 47
    • 0029863628 scopus 로고    scopus 로고
    • Diacylglycerol and the promotion of lamellar-hexagonal and lamellar- isotropic phase transitions in lipids: Implications for membrane fusion
    • Basanez, G., Nieva, J.L., Rivas, E., Alonso, A., Goni, F.M. (1996) Diacylglycerol and the promotion of lamellar-hexagonal and lamellar- isotropic phase transitions in lipids: implications for membrane fusion. Biophys. J. 70: 2299-2306.
    • (1996) Biophys. J , vol.70 , pp. 2299-2306
    • Basanez, G.1    Nieva, J.L.2    Rivas, E.3    Alonso, A.4    Goni, F.M.5
  • 48
    • 0035366713 scopus 로고    scopus 로고
    • Role for phosphatidylinositol in nuclear envelope formation
    • Larijani, B., Barona, T.M., Poccia, D.L. (2001) Role for phosphatidylinositol in nuclear envelope formation. Biochem. J. 356: 495-501.
    • (2001) Biochem. J , vol.356 , pp. 495-501
    • Larijani, B.1    Barona, T.M.2    Poccia, D.L.3
  • 49
    • 17644409738 scopus 로고    scopus 로고
    • Nuclear envelope assembly is promoted by phosphoinositide-specific phospholipase C with selective recruitment of phosphatidylinositol-enriched membranes
    • Byrne, R.D., Barona, T.M., Gamier, M., Koster, G., et al. (2005) Nuclear envelope assembly is promoted by phosphoinositide-specific phospholipase C with selective recruitment of phosphatidylinositol-enriched membranes. Biochem. J. 387: 393-400.
    • (2005) Biochem. J , vol.387 , pp. 393-400
    • Byrne, R.D.1    Barona, T.M.2    Gamier, M.3    Koster, G.4
  • 50
    • 33845762823 scopus 로고    scopus 로고
    • Transmembrane proteins are not required for early stages of nuclear envelope assembly
    • Ramos, C, Rafikova, E.R., Melikov, K., Chernomordik, L.V. (2006) Transmembrane proteins are not required for early stages of nuclear envelope assembly. Biochem. J. 400: 393-400.
    • (2006) Biochem. J , vol.400 , pp. 393-400
    • Ramos, C.1    Rafikova, E.R.2    Melikov, K.3    Chernomordik, L.V.4
  • 51
    • 0036154247 scopus 로고    scopus 로고
    • Stalk model of membrane fusion: Solution of energy crisis
    • Kozlovsky, Y., Kozlov, M.M. (2002) Stalk model of membrane fusion: solution of energy crisis. Biophys. J. 82: 882-895.
    • (2002) Biophys. J , vol.82 , pp. 882-895
    • Kozlovsky, Y.1    Kozlov, M.M.2
  • 52
    • 29244466467 scopus 로고    scopus 로고
    • Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles
    • Barona, T., Byrne, R.D., Pettitt, T.R., Wakelam, M.J., et al. (2005) Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles. J. Biol. Chem. 280: 41171-41177.
    • (2005) J. Biol. Chem , vol.280 , pp. 41171-41177
    • Barona, T.1    Byrne, R.D.2    Pettitt, T.R.3    Wakelam, M.J.4
  • 53
    • 34248189825 scopus 로고    scopus 로고
    • PLCγ and phosphoinositides are highly enriched in membrane vesicles required for nuclear envelope assembly
    • in press
    • Byrne, R., Garnier, M., Han, K., Dowicki, M., et al. (2006) PLCγ and phosphoinositides are highly enriched in membrane vesicles required for nuclear envelope assembly. Cell. Signal., in press.
    • (2006) Cell. Signal
    • Byrne, R.1    Garnier, M.2    Han, K.3    Dowicki, M.4
  • 54
    • 33845345255 scopus 로고    scopus 로고
    • Polyunsaturated phosphatidylinositol and diacylglycerol substantially modify the fluidity and polymorphism of bio-membranes: A solid state deuterium NMR study
    • Larijani, B., Dufourc, E. (2006) Polyunsaturated phosphatidylinositol and diacylglycerol substantially modify the fluidity and polymorphism of bio-membranes: a solid state deuterium NMR study. Lipids 41: 925-932.
    • (2006) Lipids , vol.41 , pp. 925-932
    • Larijani, B.1    Dufourc, E.2
  • 55
    • 0020841230 scopus 로고
    • Sources of calcium in egg activation: A review and hypothesis
    • Jaffe, L.F. (1983) Sources of calcium in egg activation: a review and hypothesis. Dev. Biol. 99: 265-276.
    • (1983) Dev. Biol , vol.99 , pp. 265-276
    • Jaffe, L.F.1
  • 56
    • 1842665585 scopus 로고    scopus 로고
    • Identification of a starfish egg PLC-gamma that regulates Ca2+ release at fertilization
    • Runft, L.L., Carroll, D.J., Gillett, J., Giusti, A.F., et al. (2004) Identification of a starfish egg PLC-gamma that regulates Ca2+ release at fertilization. Dev. Biol. 269: 220-236.
    • (2004) Dev. Biol , vol.269 , pp. 220-236
    • Runft, L.L.1    Carroll, D.J.2    Gillett, J.3    Giusti, A.F.4
  • 57
    • 0025805394 scopus 로고
    • PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254
    • Kim, H.K., Kim, J.W., Zilberstein, A., Margolis, B., et al. (1991) PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254. Cell 65: 435-441.
    • (1991) Cell , vol.65 , pp. 435-441
    • Kim, H.K.1    Kim, J.W.2    Zilberstein, A.3    Margolis, B.4
  • 58
    • 34248143563 scopus 로고    scopus 로고
    • Lineage-specific expansions provide genomic complexity among sea urchin GTPases
    • Beane, W.S., Voronina, E., Wessel, G.M., McClay, D.R. (2006) Lineage-specific expansions provide genomic complexity among sea urchin GTPases. Dev. Biol. 300: 165-179.
    • (2006) Dev. Biol , vol.300 , pp. 165-179
    • Beane, W.S.1    Voronina, E.2    Wessel, G.M.3    McClay, D.R.4
  • 60
    • 33751547362 scopus 로고    scopus 로고
    • A functional genomic and proteomic perspective of sea urchin calcium signaling and egg activation
    • Roux, M.M., Townley, I.K., Raisch, M., Reade, A., et al. (2006) A functional genomic and proteomic perspective of sea urchin calcium signaling and egg activation. Dev. Biol. 300: 416-433.
    • (2006) Dev. Biol , vol.300 , pp. 416-433
    • Roux, M.M.1    Townley, I.K.2    Raisch, M.3    Reade, A.4
  • 61
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
    • Simonsen, A., Lippe, R., Christoforidis, S., Gaullier, J.M., et al. (1998) EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 394: 494-498.
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1    Lippe, R.2    Christoforidis, S.3    Gaullier, J.M.4
  • 62
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • Lindmo, K., Stenmark, H. (2006) Regulation of membrane traffic by phosphoinositide 3-kinases. J. Cell Sci. 119: 605-614.
    • (2006) J. Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 63
    • 0026071202 scopus 로고
    • A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs
    • Vigers, G.P., Lohka, M.J. (1991) A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs. J. Cell Biol. 112: 545-556.
    • (1991) J. Cell Biol , vol.112 , pp. 545-556
    • Vigers, G.P.1    Lohka, M.J.2
  • 64
    • 0027258499 scopus 로고
    • Nuclear assembly, structure, and function: The use of Xenopus in vitro systems
    • Almouzni, G., Wolffe, A.P. (1993) Nuclear assembly, structure, and function: The use of Xenopus in vitro systems. Exp. Cell Res. 205:1-15.
    • (1993) Exp. Cell Res , vol.205 , pp. 1-15
    • Almouzni, G.1    Wolffe, A.P.2
  • 65
    • 16644367358 scopus 로고    scopus 로고
    • The Xenopus cell cycle: An overview
    • Philpott, A., Yew, P.R. (2005) The Xenopus cell cycle: an overview. Methods Mol. Biol. 296: 95-112.
    • (2005) Methods Mol. Biol , vol.296 , pp. 95-112
    • Philpott, A.1    Yew, P.R.2
  • 66
    • 33745482249 scopus 로고    scopus 로고
    • Using Xenopus oocyte extracts to study signal transduction
    • Crane, R.F., Ruderman, J.V. (2006) Using Xenopus oocyte extracts to study signal transduction. Methods Mol. Biol. 322:435-443.
    • (2006) Methods Mol. Biol , vol.322 , pp. 435-443
    • Crane, R.F.1    Ruderman, J.V.2
  • 67
    • 0029688692 scopus 로고    scopus 로고
    • Transforming sperm nuclei into male pronuclei in vivo and in vitro
    • Poccia, D., Collas, P. (1996) Transforming sperm nuclei into male pronuclei in vivo and in vitro. Curr. Top. Devel. Biol. 34:25-88.
    • (1996) Curr. Top. Devel. Biol , vol.34 , pp. 25-88
    • Poccia, D.1    Collas, P.2
  • 68
    • 0026556684 scopus 로고
    • GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro
    • Boman, A.L., Delannoy, M.R., Wilson, K.L. (1992) GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro. J. Cell Biol. 115: 281-294.
    • (1992) J. Cell Biol , vol.115 , pp. 281-294
    • Boman, A.L.1    Delannoy, M.R.2    Wilson, K.L.3
  • 69
    • 0027175035 scopus 로고
    • Calcium mobilization is required for nuclear vesicle fusion in vitro: Implications for membrane traffic and IP3 receptor function
    • Sullivan, K.M.C, Busa, W.B., Wilson, K.L. (1993) Calcium mobilization is required for nuclear vesicle fusion in vitro: Implications for membrane traffic and IP3 receptor function. Cell 73: 1411-1422.
    • (1993) Cell , vol.73 , pp. 1411-1422
    • Sullivan, K.M.C.1    Busa, W.B.2    Wilson, K.L.3
  • 70
    • 0028170377 scopus 로고
    • A new role for IP3 receptors: Ca2+ release during nuclear vesicle fusion
    • Sullivan, K.M.C, Wilson, K.L. (1994) A new role for IP3 receptors: Ca2+ release during nuclear vesicle fusion. Cell Calcium 16: 314.
    • (1994) Cell Calcium , vol.16 , pp. 314
    • Sullivan, K.M.C.1    Wilson, K.L.2
  • 71
    • 0039518668 scopus 로고    scopus 로고
    • Structure and functional properties of diacylglycerols in membranes
    • Goni, F.M., Alonso, A. (1999) Structure and functional properties of diacylglycerols in membranes. Prog. Lipid Res. 38:1-48.
    • (1999) Prog. Lipid Res , vol.38 , pp. 1-48
    • Goni, F.M.1    Alonso, A.2
  • 72
    • 0035815365 scopus 로고    scopus 로고
    • Diacylglycerol effects on phosphatidylinositol-specific phospholipase C activity and vesicle fusion
    • Villar, A.V., Goni, F.M., Alonso, A. (2001) Diacylglycerol effects on phosphatidylinositol-specific phospholipase C activity and vesicle fusion. FEBS Lett. 494:117-120.
    • (2001) FEBS Lett , vol.494 , pp. 117-120
    • Villar, A.V.1    Goni, F.M.2    Alonso, A.3
  • 74
    • 33845762823 scopus 로고    scopus 로고
    • Transmembrane proteins are not required for early stages of nuclear envelope assembly
    • Ramos, C, Rafikova, E.R., Melikov, K., Chernomordik, L.V. (2006) Transmembrane proteins are not required for early stages of nuclear envelope assembly. Biochem. J. 400:393-400.
    • (2006) Biochem. J , vol.400 , pp. 393-400
    • Ramos, C.1    Rafikova, E.R.2    Melikov, K.3    Chernomordik, L.V.4
  • 75
    • 77957086662 scopus 로고
    • Myoblast fusion - a mechanistic analysis
    • Wakelam, M.J.O. (1988) Myoblast fusion - a mechanistic analysis. Curr. Top. Memb. Transport 82: 87-112.
    • (1988) Curr. Top. Memb. Transport , vol.82 , pp. 87-112
    • Wakelam, M.J.O.1
  • 76
    • 11144240474 scopus 로고    scopus 로고
    • Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion
    • Jun, Y., Fratti, R.A., Wickner, W. (2004) Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion. J. Biol. Chem. 279: 53186-53195.
    • (2004) J. Biol. Chem , vol.279 , pp. 53186-53195
    • Jun, Y.1    Fratti, R.A.2    Wickner, W.3
  • 77
    • 0018663294 scopus 로고
    • Diacylglycerol metabolism in mast cells: A potential role in membrane fusion and arachidonic acid release
    • Kennerly, D.A., Sullivan, T.J., Sylwester, P., Parker, C.W. (1979) Diacylglycerol metabolism in mast cells: a potential role in membrane fusion and arachidonic acid release. J. Exp. Med. 150: 1039-1044.
    • (1979) J. Exp. Med , vol.150 , pp. 1039-1044
    • Kennerly, D.A.1    Sullivan, T.J.2    Sylwester, P.3    Parker, C.W.4
  • 78
    • 0032494164 scopus 로고    scopus 로고
    • Dynamics of the genome during early Xenopus laevis development: Karyomeres as independent units of replication
    • Lemaitre, J.M., Geraud, G., Mechali, M. (1998) Dynamics of the genome during early Xenopus laevis development: karyomeres as independent units of replication. J. Cell Biol. 142:1159-1166.
    • (1998) J. Cell Biol , vol.142 , pp. 1159-1166
    • Lemaitre, J.M.1    Geraud, G.2    Mechali, M.3


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