메뉴 건너뛰기




Volumn 125, Issue 7, 2012, Pages 1683-1692

SNAREs, HOPS and regulatory lipids control the dynamics of vacuolar actin during homotypic fusion in S. Cerevisiae

Author keywords

Actin dynamics; Fusion; HOPS; Phosphoinositide; Phospholipase C; SNARE

Indexed keywords

ACTIN; HOPS PROTEIN; HYBRID PROTEIN; JASPAMIDE; LATRUNCULIN B; LIPID; MONOMER; PHOSPHOLIPASE C; REGULATORY LIPID; SNARE PROTEIN; UNCLASSIFIED DRUG; YPT7P PROTEIN;

EID: 84863097996     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.091900     Document Type: Article
Times cited : (17)

References (59)
  • 1
    • 70350418724 scopus 로고    scopus 로고
    • Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
    • Albiges-Rizo, C., Destaing, O., Fourcade, B., Planus, E. and Block, M. R. (2009). Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions. J. Cell Sci. 122, 3037-3049.
    • (2009) J. Cell Sci. , vol.122 , pp. 3037-3049
    • Albiges-Rizo, C.1    Destaing, O.2    Fourcade, B.3    Planus, E.4    Block, M.R.5
  • 2
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst, M., Odorizzi, G., Estepa, E. J. and Emr, S. D. (2000). Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 1, 248-258.
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 3
    • 0036544561 scopus 로고    scopus 로고
    • A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion
    • Boeddinghaus, C., Merz, A. J., Laage, R. and Ungermann, C. (2002). A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion. J. Cell Biol. 157, 79-89.
    • (2002) J. Cell Biol. , vol.157 , pp. 79-89
    • Boeddinghaus, C.1    Merz, A.J.2    Laage, R.3    Ungermann, C.4
  • 4
    • 78649649128 scopus 로고    scopus 로고
    • Class I and class III phosphoinositide 3-kinases are required for actin polymerization that propels phagosomes
    • Bohdanowicz, M., Cosio, G., Backer, J. M. and Grinstein, S. (2010). Class I and class III phosphoinositide 3-kinases are required for actin polymerization that propels phagosomes. J. Cell Biol. 191, 999-1012.
    • (2010) J. Cell Biol. , vol.191 , pp. 999-1012
    • Bohdanowicz, M.1    Cosio, G.2    Backer, J.M.3    Grinstein, S.4
  • 5
    • 0034681423 scopus 로고    scopus 로고
    • Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations
    • Bubb, M. R., Spector, I., Beyer, B. B. and Fosen, K. M. (2000). Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations. J. Biol. Chem. 275, 5163-5170.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 6
    • 37549035926 scopus 로고    scopus 로고
    • Clustering of membrane raft proteins by the actin cytoskeleton
    • Chichili, G. R. and Rodgers, W. (2007). Clustering of membrane raft proteins by the actin cytoskeleton. J. Biol. Chem. 282, 36682-36691.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36682-36691
    • Chichili, G.R.1    Rodgers, W.2
  • 7
    • 77951991606 scopus 로고    scopus 로고
    • T cell signal regulation by the actin cytoskeleton
    • Chichili, G. R., Westmuckett, A. D. and Rodgers, W. (2010). T cell signal regulation by the actin cytoskeleton. J. Biol. Chem. 285, 14737-14746.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14737-14746
    • Chichili, G.R.1    Westmuckett, A.D.2    Rodgers, W.3
  • 9
    • 0037135973 scopus 로고    scopus 로고
    • Vacuole-bound actin regulates homotypic membrane fusion
    • Eitzen, G., Wang, L., Thorngren, N. and Wickner, W. (2002). Vacuole-bound actin regulates homotypic membrane fusion. J. Cell Biol. 158, 669-679.
    • (2002) J. Cell Biol. , vol.158 , pp. 669-679
    • Eitzen, G.1    Wang, L.2    Thorngren, N.3    Wickner, W.4
  • 10
    • 34250327976 scopus 로고    scopus 로고
    • Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p
    • Fratti, R. A. andWickner, W. (2007). Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p. J. Biol. Chem. 282, 13133-13138.
    • (2007) J. Biol. Chem. , vol.282 , pp. 13133-13138
    • Fratti, R.A.1    Wickner, W.2
  • 11
    • 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. and Wickner, W. (2004). Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles. J. Cell Biol. 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
  • 12
    • 34447524098 scopus 로고    scopus 로고
    • Stringent 3Q: [1R] composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification
    • Fratti, R. A., Collins, K. M., Hickey, C. M. and Wickner, W. (2007). Stringent 3Q: [1R] composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. J. Biol. Chem. 282, 14861-14867.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14861-14867
    • Fratti, R.A.1    Collins, K.M.2    Hickey, C.M.3    Wickner, W.4
  • 14
    • 0038652046 scopus 로고    scopus 로고
    • Compression forces generated by actin comet tails on lipid vesicles
    • Giardini, P. A., Fletcher, D. A. and Theriot, J. A. (2003). Compression forces generated by actin comet tails on lipid vesicles. Proc. Natl. Acad. Sci. USA 100, 6493-6498.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6493-6498
    • Giardini, P.A.1    Fletcher, D.A.2    Theriot, J.A.3
  • 16
    • 0036276195 scopus 로고    scopus 로고
    • Purification of yeast actin and actin-associated proteins
    • Goode, B. L. (2002). Purification of yeast actin and actin-associated proteins. Methods Enzymol. 351, 433-441.
    • (2002) Methods Enzymol , vol.351 , pp. 433-441
    • Goode, B.L.1
  • 17
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF)
    • Haas, A. and Wickner, W. (1996). Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF). EMBO J. 15, 3296-3305.
    • (1996) EMBO J , vol.15 , pp. 3296-3305
    • Haas, A.1    Wickner, W.2
  • 18
    • 0028333056 scopus 로고
    • G-protein ligands inhibit in vitro reactions of vacuole inheritance
    • Haas, A., Conradt, B. and Wickner, W. (1994). G-protein ligands inhibit in vitro reactions of vacuole inheritance. J. Cell Biol. 126, 87-97.
    • (1994) J. Cell Biol. , vol.126 , pp. 87-97
    • Haas, A.1    Conradt, B.2    Wickner, W.3
  • 19
    • 0028788311 scopus 로고
    • The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance
    • Haas, A., Scheglmann, D., Lazar, T., Gallwitz, D. and Wickner, W. (1995). The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance. EMBO J. 14, 5258-5270.
    • (1995) EMBO J , vol.14 , pp. 5258-5270
    • Haas, A.1    Scheglmann, D.2    Lazar, T.3    Gallwitz, D.4    Wickner, W.5
  • 20
    • 70350418738 scopus 로고    scopus 로고
    • Cholesterol regulates glucose-stimulated insulin secretion through phosphatidylinositol 4,5-bisphosphate
    • Hao, M. and Bogan, J. S. (2009). Cholesterol regulates glucose-stimulated insulin secretion through phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 284, 29489-29498.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29489-29498
    • Hao, M.1    Bogan, J.S.2
  • 21
    • 0023806352 scopus 로고
    • The organization and regulation of the macrophage actin skeleton
    • Hartwig, J. H. and Yin, H. L. (1988). The organization and regulation of the macrophage actin skeleton. Cell Motil. Cytoskeleton. 10, 117-125.
    • (1988) Cell Motil. Cytoskeleton. , vol.10 , pp. 117-125
    • Hartwig, J.H.1    Yin, H.L.2
  • 23
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. and Sudhof, T. C. (1999). Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 24
    • 0034687153 scopus 로고    scopus 로고
    • The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain
    • Johnson, J. E., Giorgione, J. and Newton, A. C. (2000). The C1 and C2 domains of protein kinase C are independent membrane targeting modules, with specificity for phosphatidylserine conferred by the C1 domain. Biochemistry 39, 11360-11369.
    • (2000) Biochemistry , vol.39 , pp. 11360-11369
    • Johnson, J.E.1    Giorgione, J.2    Newton, A.C.3
  • 25
    • 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. and 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
  • 27
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik, J., Boyle, S., Fooksman, D., Margolis, L., Sheetz, M. P. and Edidin, M. (2003). Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin. Proc. Natl. Acad. Sci. USA 100, 13964-13969.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 28
    • 70350005334 scopus 로고    scopus 로고
    • Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages
    • Liebl, D. and Griffiths, G. (2009). Transient assembly of F-actin by phagosomes delays phagosome fusion with lysosomes in cargo-overloaded macrophages. J. Cell Sci. 122, 2935-2945.
    • (2009) J. Cell Sci. , vol.122 , pp. 2935-2945
    • Liebl, D.1    Griffiths, G.2
  • 29
    • 0035853477 scopus 로고    scopus 로고
    • A synaptojanin-homologous region of Salmonella typhimurium SigD is essential for inositol phosphatase activity and Akt activation
    • Marcus, S. L., Wenk, M. R., Steele-Mortimer, O. and Finlay, B. B. (2001). A synaptojanin-homologous region of Salmonella typhimurium SigD is essential for inositol phosphatase activity and Akt activation. FEBS Lett. 494, 201-207.
    • (2001) FEBS Lett , vol.494 , pp. 201-207
    • Marcus, S.L.1    Wenk, M.R.2    Steele-Mortimer, O.3    Finlay, B.B.4
  • 30
    • 0031040763 scopus 로고    scopus 로고
    • Docking of yeast vacuoles is catalyzed by the Raslike GTPase Ypt7p after symmetric priming by Sec18p (NSF)
    • Mayer, A. and Wickner, W. (1997). Docking of yeast vacuoles is catalyzed by the Raslike GTPase Ypt7p after symmetric priming by Sec18p (NSF). J. Cell Biol. 136, 307-317.
    • (1997) J. Cell Biol. , vol.136 , pp. 307-317
    • Mayer, A.1    Wickner, W.2
  • 31
    • 0029980441 scopus 로고    scopus 로고
    • Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W. and Haas, A. (1996). Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 32
    • 0034019904 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion
    • Mayer, A., Scheglmann, D., Dove, S., Glatz, A., Wickner, W. and Haas, A. (2000). Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion. Mol. Biol. Cell 11, 807-817.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 807-817
    • Mayer, A.1    Scheglmann, D.2    Dove, S.3    Glatz, A.4    Wickner, W.5    Haas, A.6
  • 33
    • 1642539980 scopus 로고    scopus 로고
    • 2+ efflux from the yeast vacuole lumen
    • 2+ efflux from the yeast vacuole lumen. J. Cell Biol. 164, 195-206.
    • (2004) J. Cell Biol. , vol.164 , pp. 195-206
    • Merz, A.J.1    Wickner, W.T.2
  • 34
    • 4143122322 scopus 로고    scopus 로고
    • Resolution of organelle docking and fusion kinetics in a cell-free assay
    • Merz, A. J. and Wickner, W. T. (2004b). Resolution of organelle docking and fusion kinetics in a cell-free assay. Proc. Natl. Acad. Sci. USA 101, 11548-11553.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11548-11553
    • Merz, A.J.1    Wickner, W.T.2
  • 35
    • 69949156933 scopus 로고    scopus 로고
    • The shape of motile cells
    • Mogilner, A. and Keren, K. (2009). The shape of motile cells. Curr. Biol. 19, R762-R771.
    • (2009) Curr. Biol. , vol.19
    • Mogilner, A.1    Keren, K.2
  • 36
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton, W. M., Ayscough, K. R. and McLaughlin, P. J. (2000). Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat. Cell Biol. 2, 376-378.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 37
  • 38
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • Pollard, T. D. (2010). Mechanics of cytokinesis in eukaryotes. Curr. Opin. Cell Biol. 22, 50-56.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 50-56
    • Pollard, T.D.1
  • 39
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard, T. D. and Cooper, J. A. (2009). Actin, a central player in cell shape and movement. Science. 326, 1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 40
    • 29144520288 scopus 로고    scopus 로고
    • Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion
    • Reese, C. and Mayer, A. (2005). Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusion. J. Cell Biol. 171, 981-990.
    • (2005) J. Cell Biol. , vol.171 , pp. 981-990
    • Reese, C.1    Mayer, A.2
  • 41
    • 22944485726 scopus 로고    scopus 로고
    • Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion
    • Reese, C., Heise, F. and Mayer, A. (2005). Trans-SNARE pairing can precede a hemifusion intermediate in intracellular membrane fusion. Nature 436, 410-414.
    • (2005) Nature , vol.436 , pp. 410-414
    • Reese, C.1    Heise, F.2    Mayer, A.3
  • 42
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate
    • Rohatgi, R., Ho, H. Y. and Kirschner, M. W. (2000). Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 150, 1299-1310.
    • (2000) J. Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 43
    • 0033607806 scopus 로고    scopus 로고
    • The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module
    • Rosenthal, J. A., Chen, H., Slepnev, V. I., Pellegrini, L., Salcini, A. E., Di Fiore, P. P. and De Camilli, P. (1999). The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module. J. Biol. Chem. 274, 33959-33965.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33959-33965
    • Rosenthal, J.A.1    Chen, H.2    Slepnev, V.I.3    Pellegrini, L.4    Salcini, A.E.5    Di Fiore, P.P.6    De Camilli, P.7
  • 45
    • 0034662876 scopus 로고    scopus 로고
    • A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
    • Seals, D. F., Eitzen, G., Margolis, N., Wickner, W. T. and Price, A. (2000). A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion. Proc. Natl. Acad. Sci. USA 97, 9402-9407.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9402-9407
    • Seals, D.F.1    Eitzen, G.2    Margolis, N.3    Wickner, W.T.4    Price, A.5
  • 47
    • 38349076023 scopus 로고    scopus 로고
    • Expression of PI(4,5)P2-binding proteins lowers the PI(4,5)P2level and inhibits FcgammaRIIAmediated cell spreading and phagocytosis
    • Szymanska, E., Sobota, A., Czurylo, E. and Kwiatkowska, K. (2008). Expression of PI(4,5)P2-binding proteins lowers the PI(4,5)P2level and inhibits FcgammaRIIAmediated cell spreading and phagocytosis. Eur. J. Immunol. 38, 260-272.
    • (2008) Eur. J. Immunol. , vol.38 , pp. 260-272
    • Szymanska, E.1    Sobota, A.2    Czurylo, E.3    Kwiatkowska, K.4
  • 48
    • 0034244437 scopus 로고    scopus 로고
    • Inaugural article: myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate
    • Taylor, G. S., Maehama, T. and Dixon, J. E. (2000). Inaugural article: myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate. Proc. Natl. Acad. Sci. USA. 97, 8910-8915.
    • (2000) Proc. Natl. Acad. Sci. USA. , vol.97 , pp. 8910-8915
    • Taylor, G.S.1    Maehama, T.2    Dixon, J.E.3
  • 49
    • 34547784117 scopus 로고    scopus 로고
    • A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2. channels
    • Tamkun, M. M., O'Connell, K. M. and Rolig, A. S. (2007). A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels. J. Cell Sci. 120, 2413-2423.
    • (2007) J. Cell Sci. , vol.120 , pp. 2413-2423
    • Tamkun, M.M.1    O'Connell, K.M.2    Rolig, A.S.3
  • 50
    • 0032526955 scopus 로고    scopus 로고
    • Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion
    • Ungermann, C. and Wickner, W. (1998). Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. EMBO J. 17, 3269-3276.
    • (1998) EMBO J , vol.17 , pp. 3269-3276
    • Ungermann, C.1    Wickner, W.2
  • 51
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann, C., Sato, K. and Wickner, W. (1998). Defining the functions of trans-SNARE pairs. Nature 396, 543-548.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 53
    • 0034255122 scopus 로고    scopus 로고
    • Exploitation of host cells by enteropathogenic Escherichia coli
    • Vallance, B. A. and Finlay, B. B. (2000). Exploitation of host cells by enteropathogenic Escherichia coli. Proc. Natl. Acad. Sci. USA 97, 8799-8806.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8799-8806
    • Vallance, B.A.1    Finlay, B.B.2
  • 55
    • 0034725579 scopus 로고    scopus 로고
    • The docking of primed vacuoles can be reversibly arrested by excess Sec17p (alpha-SNAP)
    • Wang, L., Ungermann, C. and Wickner, W. (2000). The docking of primed vacuoles can be reversibly arrested by excess Sec17p (alpha-SNAP). J. Biol. Chem. 275, 22862-22867.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22862-22867
    • Wang, L.1    Ungermann, C.2    Wickner, W.3
  • 56
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • Wang, L., Seeley, E. S., Wickner, W. and Merz, A. J. (2002). Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 108, 357-369.
    • (2002) Cell , vol.108 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4
  • 57
    • 0037415612 scopus 로고    scopus 로고
    • Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion
    • Wang, L., Merz, A. J., Collins, K. M. and Wickner, W. (2003). Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J. Cell Biol. [160,] 365-374.
    • (2003) J. Cell Biol. , vol.160 , pp. 365-374
    • Wang, L.1    Merz, A.J.2    Collins, K.M.3    Wickner, W.4
  • 58
    • 77957020175 scopus 로고    scopus 로고
    • Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles
    • Wickner, W. (2010). Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles. Annu. Rev. Cell Dev. Biol. 26, 115-136.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 115-136
    • Wickner, W.1
  • 59
    • 34447531896 scopus 로고    scopus 로고
    • Inactivation of the phosphoinositide phosphatases Sac1p and Inp54p leads to accumulation of phosphatidylinositol 4,5-bisphosphate on vacuole membranes and vacuolar fusion defects
    • Wiradjaja, F., Ooms, L. M., Tahirovic, S., Kuhne, E., Devenish, R. J., Munn, A. L., Piper, R. C., Mayinger, P. and Mitchell, C. A. (2007). Inactivation of the phosphoinositide phosphatases Sac1p and Inp54p leads to accumulation of phosphatidylinositol 4,5-bisphosphate on vacuole membranes and vacuolar fusion defects. J. Biol. Chem. 282, 16295-16307.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16295-16307
    • Wiradjaja, F.1    Ooms, L.M.2    Tahirovic, S.3    Kuhne, E.4    Devenish, R.J.5    Munn, A.L.6    Piper, R.C.7    Mayinger, P.8    Mitchell, C.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.