메뉴 건너뛰기




Volumn 21, Issue 23, 2010, Pages 4173-4183

Microautophagy of the nucleus coincides with a vacuolar diffusion barrier at nuclear-vacuolar junctions

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DIENOYL COENZYME A REDUCTASE (NADPH); ADENOSINE TRIPHOSPHATASE; BINDING PROTEIN; FEN1P PROTEIN; LAG1P PROTEIN; OSH1P PROTEIN; TSC13P PROTEIN; UNCLASSIFIED DRUG;

EID: 78650154466     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E09-09-0782     Document Type: Article
Times cited : (70)

References (69)
  • 1
    • 0025743250 scopus 로고
    • Cloning and disruption of the yeast C-8 sterol isomerase gene
    • Ashman, W. H., Barbuch, R. J., Ulbright, C. E., Jarrett, H. W., and Bard, M. (1991). Cloning and disruption of the yeast C-8 sterol isomerase gene. Lipids 26, 628-632.
    • (1991) Lipids , vol.26 , pp. 628-632
    • Ashman, W.H.1    Barbuch, R.J.2    Ulbright, C.E.3    Jarrett, H.W.4    Bard, M.5
  • 2
    • 34948873616 scopus 로고    scopus 로고
    • Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium
    • Baars, T. L., Petri, S., Peters, C., and Mayer, A. (2007). Role of the V-ATPase in regulation of the vacuolar fission-fusion equilibrium. Mol. Biol. Cell 18, 3873-3882.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3873-3882
    • Baars, T.L.1    Petri, S.2    Peters, C.3    Mayer, A.4
  • 3
    • 0043174011 scopus 로고    scopus 로고
    • 2+-releasing channel
    • DOI 10.1083/jcb.200212004
    • Bayer, M. J., Reese, C., Buhler, S., Peters, C., and Mayer, A. (2003). Vacuole membrane fusion: V0 functions after trans-SNARE pairing and is coupled to the Ca2+-releasing channel. J. Cell Biol. 162, 211-222. (Pubitemid 36928835)
    • (2003) Journal of Cell Biology , vol.162 , Issue.2 , pp. 211-222
    • Bayer, M.J.1    Reese, C.2    Buhler, S.3    Peters, C.4    Mayer, A.5
  • 4
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • Beh, C. T., Cool, L., Phillips, J., and Rine, J. (2001). Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 157, 1117-1140. (Pubitemid 32225007)
    • (2001) Genetics , vol.157 , Issue.3 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 5
    • 4344641314 scopus 로고    scopus 로고
    • A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution
    • Beh, C. T., and Rine, J. (2004). A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution. J. Cell Sci. 117, 2983-2996.
    • (2004) J. Cell Sci. , vol.117 , pp. 2983-2996
    • Beh, C.T.1    Rine, J.2
  • 6
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • Bowman, B. J., and Bowman, E. J. (2002). Mutations in subunit C of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site. J. Biol. Chem. 277, 3965-3972.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 7
    • 0030962901 scopus 로고    scopus 로고
    • Novel Golgi to vacuole delivery pathway in yeast: Identification of a sorting determinant and required transport component
    • Cowles, C. R., Snyder, W. B., Burd, C. G., and Emr, S. D. (1997). Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component. EMBO J. 16, 2769-2782.
    • (1997) EMBO J. , vol.16 , pp. 2769-2782
    • Cowles, C.R.1    Snyder, W.B.2    Burd, C.G.3    Emr, S.D.4
  • 10
    • 67349158752 scopus 로고    scopus 로고
    • Molecular assemblies and membrane domains in multivesicular endosome dynamics
    • Falguieres, T., Luyet, P. P., and Gruenberg, J. (2009). Molecular assemblies and membrane domains in multivesicular endosome dynamics. Exp. Cell Res. 315, 1567-1573.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1567-1573
    • Falguieres, T.1    Luyet, P.P.2    Gruenberg, J.3
  • 11
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M. (2007). Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-929
    • Forgac, M.1
  • 12
    • 0035027807 scopus 로고    scopus 로고
    • Nuclear export of 60s ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p
    • Gadal, O., Strauss, D., Kessl, J., Trumpower, B., Tollervey, D., and Hurt, E. (2001). Nuclear export of 60s ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p. Mol. Cell. Biol. 21, 3405-3415.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3405-3415
    • Gadal, O.1    Strauss, D.2    Kessl, J.3    Trumpower, B.4    Tollervey, D.5    Hurt, E.6
  • 13
    • 33846240490 scopus 로고    scopus 로고
    • Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast
    • Grossmann, G., Opekarova, M., Malinsky, J., Weig-Meckl, I., and Tanner, W. (2007). Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast. EMBO J. 26, 1-8.
    • (2007) EMBO J. , vol.26 , pp. 1-8
    • Grossmann, G.1    Opekarova, M.2    Malinsky, J.3    Weig-Meckl, I.4    Tanner, W.5
  • 15
    • 3543052393 scopus 로고    scopus 로고
    • Pseudo real-time method for monitoring of the limiting anisotropy in membranes
    • Herman, P., Malinsky, J., Plasek, J., and Vecer, J. (2004). Pseudo real-time method for monitoring of the limiting anisotropy in membranes. J. Fluoresc. 14, 79-85.
    • (2004) J. Fluoresc. , vol.14 , pp. 79-85
    • Herman, P.1    Malinsky, J.2    Plasek, J.3    Vecer, J.4
  • 19
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: New fluorescent proteins, more markers and promoter substitution cassettes
    • DOI 10.1002/yea.1142
    • Janke, C., Magiera, M. M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A., Doenges, G., Schwob, E., Schiebel, E., and Knop, M. (2004). A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21, 947-962. (Pubitemid 39206863)
    • (2004) Yeast , vol.21 , Issue.11 , pp. 947-962
    • Janke, C.1    Magiera, M.M.2    Rathfelder, N.3    Taxis, C.4    Reber, S.5    Maekawa, H.6    Moreno-Borchart, A.7    Doenges, G.8    Schwob, E.9    Schiebel, E.10    Knop, M.11
  • 20
    • 0020338057 scopus 로고
    • PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae
    • Jones, E. W., Zubenko, G. S., and Parker, R. R. (1982). PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics 102, 665-677.
    • (1982) Genetics , vol.102 , pp. 665-677
    • Jones, E.W.1    Zubenko, G.S.2    Parker, R.R.3
  • 21
    • 0000692927 scopus 로고
    • Domain-induced budding of vesicles
    • Julicher, F., and Lipowsky, R. (1993). Domain-induced budding of vesicles. Phys Rev Lett 70, 2964-2967.
    • (1993) Phys Rev Lett , vol.70 , pp. 2964-2967
    • Julicher, F.1    Lipowsky, R.2
  • 23
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • Kane, P. M. (2006). The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol. Mol. Biol. Rev. 70, 177-191.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 24
    • 33947401472 scopus 로고    scopus 로고
    • Autophagosome-lysosome fusion depends on the pH in acidic compartments in CHO cells
    • Kawai, A., Uchiyama, H., Takano, S., Nakamura, N., and Ohkuma, S. (2007). Autophagosome-lysosome fusion depends on the pH in acidic compartments in CHO cells. Autophagy 3, 154-157. (Pubitemid 46449110)
    • (2007) Autophagy , vol.3 , Issue.2 , pp. 154-157
    • Kawai, A.1    Uchiyama, H.2    Takano, S.3    Nakamura, N.4    Ohkuma, S.5
  • 25
    • 0030893379 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae CYP61, sterol delta22-desaturase, and inhibition by azole antifungal agents
    • Kelly, S. L., Lamb, D. C., Baldwin, B. C., Corran, A. J., and Kelly, D. E. (1997). Characterization of Saccharomyces cerevisiae CYP61, sterol delta22-desaturase, and inhibition by azole antifungal agents. J. Biol. Chem. 272, 9986-9988.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9986-9988
    • Kelly, S.L.1    Lamb, D.C.2    Baldwin, B.C.3    Corran, A.J.4    Kelly, D.E.5
  • 26
    • 0034749756 scopus 로고    scopus 로고
    • Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae
    • Kohlwein, S. D., Eder, S., Oh, C. S., Martin, C. E., Gable, K., Bacikova, D., and Dunn, T. (2001). Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell. Biol. 21, 109-125.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 109-125
    • Kohlwein, S.D.1    Eder, S.2    Oh, C.S.3    Martin, C.E.4    Gable, K.5    Bacikova, D.6    Dunn, T.7
  • 27
    • 56249124005 scopus 로고    scopus 로고
    • Lipid rafts, cholesterol, and the brain
    • Korade, Z., and Kenworthy, A. K. (2008). Lipid rafts, cholesterol, and the brain. Neuropharmacology 55, 1265-1273.
    • (2008) Neuropharmacology , vol.55 , pp. 1265-1273
    • Korade, Z.1    Kenworthy, A.K.2
  • 29
    • 24344449583 scopus 로고    scopus 로고
    • Targeting of Tsc13p to nucleus-vacuole junctions: A role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles
    • Kvam, E., Gable, K., Dunn, T. M., and Goldfarb, D. S. (2005). Targeting of Tsc13p to nucleus-vacuole junctions: a role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol. Biol. Cell 16, 3987-3998.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3987-3998
    • Kvam, E.1    Gable, K.2    Dunn, T.M.3    Goldfarb, D.S.4
  • 30
    • 8744254603 scopus 로고    scopus 로고
    • Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae
    • Kvam, E., and Goldfarb, D. S. (2004). Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae. J. Cell Sci. 117, 4959-4968.
    • (2004) J. Cell Sci. , vol.117 , pp. 4959-4968
    • Kvam, E.1    Goldfarb, D.S.2
  • 31
    • 33745478714 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions in yeast: Anatomy of a membrane contact site
    • Kvam, E., and Goldfarb, D. S. (2006a). Nucleus-vacuole junctions in yeast: anatomy of a membrane contact site. Biochem. Soc. Trans. 34, 340-342.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 340-342
    • Kvam, E.1    Goldfarb, D.S.2
  • 32
    • 33749375121 scopus 로고    scopus 로고
    • Structure and function of nucleus-vacuole junctions: Outer-nuclear- membrane targeting of Nvj1p and a role in tryptophan uptake
    • DOI 10.1242/jcs.03093
    • Kvam, E., and Goldfarb, D. S. (2006b). Structure and function of nucleus-vacuole junctions: outer-nuclear-membrane targeting of Nvj1p and a role in tryptophan uptake. J. Cell Sci. 119, 3622-3633. (Pubitemid 44501866)
    • (2006) Journal of Cell Science , vol.119 , Issue.17 , pp. 3622-3633
    • Kvam, E.1    Goldfarb, D.S.2
  • 33
    • 33947375637 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in S. cerevisiae
    • Kvam, E., and Goldfarb, D. S. (2007). Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in. S. cerevisiae. Autophagy 3, 85-92. (Pubitemid 46449095)
    • (2007) Autophagy , vol.3 , Issue.2 , pp. 85-92
    • Kvam, E.1    Goldfarb, D.S.2
  • 34
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle
    • DOI 10.1016/j.cell.2005.07.025, PII S0092867405007567
    • Lee, M. C., Orci, L., Hamamoto, S., Futai, E., Ravazzola, M., and Schekman, R. (2005). Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPII vesicle. Cell 122, 605-617. (Pubitemid 41191158)
    • (2005) Cell , vol.122 , Issue.4 , pp. 605-617
    • Lee, M.C.S.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 35
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine, B., and Klionsky, D. J. (2004). Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell. 6, 463-477.
    • (2004) Dev. Cell. , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 36
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine, T. (2004). Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol. 14, 483-490.
    • (2004) Trends Cell Biol. , vol.14 , pp. 483-490
    • Levine, T.1
  • 37
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • Levine, T. P., and Munro, S. (2001). Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol. Biol. Cell 12, 1633-1644.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 38
    • 33745280126 scopus 로고    scopus 로고
    • The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans
    • Liegeois, S., Benedetto, A., Garnier, J. M., Schwab, Y., and Labouesse, M. (2006). The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-related proteins in Caenorhabditis elegans. J. Cell Biol. 173, 949-961.
    • (2006) J. Cell Biol. , vol.173 , pp. 949-961
    • Liegeois, S.1    Benedetto, A.2    Garnier, J.M.3    Schwab, Y.4    Labouesse, M.5
  • 39
    • 34250897699 scopus 로고    scopus 로고
    • Degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase is dependent on the vacuolar ATPase
    • Liu, J., Brown, C. R., and Chiang, H. L. (2005). Degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase is dependent on the vacuolar ATPase. Autophagy 1, 146-156.
    • (2005) Autophagy , vol.1 , pp. 146-156
    • Liu, J.1    Brown, C.R.2    Chiang, H.L.3
  • 40
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of protein compartmentation within the plasma membrane of living yeast cells
    • Malinska, K., Malinsky, J., Opekarova, M., and Tanner, W. (2003). Visualization of protein compartmentation within the plasma membrane of living yeast cells. Mol. Biol. Cell 14, 4427-4436.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4427-4436
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4
  • 41
    • 0028224791 scopus 로고
    • STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p
    • Manolson, M. F., Wu, B., Proteau, D., Taillon, B. E., Roberts, B. T., Hoyt, M. A., and Jones, E. W. (1994). STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p. J. Biol. Chem. 269, 14064-14074.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14064-14074
    • Manolson, M.F.1    Wu, B.2    Proteau, D.3    Taillon, B.E.4    Roberts, B.T.5    Hoyt, M.A.6    Jones, E.W.7
  • 42
    • 0034629140 scopus 로고    scopus 로고
    • Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme with reverse (CoA-independent) ceramide synthase activity
    • Mao, C., Xu, R., Bielawska, A., and Obeid, L. M. (2000). Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme with reverse (CoA-independent) ceramide synthase activity. J. Biol. Chem. 275, 6876-6884.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6876-6884
    • Mao, C.1    Xu, R.2    Bielawska, A.3    Obeid, L.M.4
  • 44
    • 0030724890 scopus 로고    scopus 로고
    • Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids
    • Mitchell, A. G., and Martin, C. E. (1997). Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. J. Biol. Chem. 272, 28281-28288.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28281-28288
    • Mitchell, A.G.1    Martin, C.E.2
  • 45
    • 0141964578 scopus 로고    scopus 로고
    • Modification of a ubiquitin-like protein Paz2 conducted micropexophagy through formation of a novel membrane structure
    • Mukaiyama, H., Baba, M., Osumi, M., Aoyagi, S., Kato, N., Ohsumi, Y., and Sakai, Y. (2004). Modification of a ubiquitin-like protein Paz2 conducted micropexophagy through formation of a novel membrane structure. Mol. Biol. Cell 15, 58-70.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 58-70
    • Mukaiyama, H.1    Baba, M.2    Osumi, M.3    Aoyagi, S.4    Kato, N.5    Ohsumi, Y.6    Sakai, Y.7
  • 46
    • 0037444478 scopus 로고    scopus 로고
    • Role of the Vtc proteins in V-ATPase stability and membrane trafficking
    • DOI 10.1242/jcs.00328
    • Muller, O., Neumann, H., Bayer, M. J., and Mayer, A. (2003). Role of the Vtc proteins in V-ATPase stability and membrane trafficking. J. Cell Sci. 116, 1107-1115. (Pubitemid 36395620)
    • (2003) Journal of Cell Science , vol.116 , Issue.6 , pp. 1107-1115
    • Muller, O.1    Neumann, H.2    Bayer, M.J.3    Mayer, A.4
  • 47
    • 0032741066 scopus 로고    scopus 로고
    • Specific sterols required for the internalization step of endocytosis in yeast
    • Munn, A. L., Heese-Peck, A., Stevenson, B. J., Pichler, H., and Riezman, H. (1999). Specific sterols required for the internalization step of endocytosis in yeast. Mol. Biol. Cell 10, 3943-3957.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3943-3957
    • Munn, A.L.1    Heese-Peck, A.2    Stevenson, B.J.3    Pichler, H.4    Riezman, H.5
  • 48
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases-nature's most versatile proton pumps
    • Nishi, T., and Forgac, M. (2002). The vacuolar (H+)-ATPases-nature's most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3, 94-103.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 49
    • 0030878240 scopus 로고    scopus 로고
    • ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation
    • Oh, C. S., Toke, D. A., Mandala, S., and Martin, C. E. (1997). ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J. Biol. Chem. 272, 17376-17384.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17376-17384
    • Oh, C.S.1    Toke, D.A.2    Mandala, S.3    Martin, C.E.4
  • 50
    • 0033944449 scopus 로고    scopus 로고
    • Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p
    • Pan, X., Roberts, P., Chen, Y., Kvam, E., Shulga, N., Huang, K., Lemmon, S., and Goldfarb, D. S. (2000). Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p. Mol. Biol. Cell 11, 2445-2457.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2445-2457
    • Pan, X.1    Roberts, P.2    Chen, Y.3    Kvam, E.4    Shulga, N.5    Huang, K.6    Lemmon, S.7    Goldfarb, D.S.8
  • 51
    • 43949088191 scopus 로고    scopus 로고
    • Live Imaging of Neuronal Degradation by Microglia Reveals a Role for v0-ATPase a1 in Phagosomal Fusion in Vivo
    • DOI 10.1016/j.cell.2008.04.037, PII S0092867408006119
    • Peri, F., and Nusslein-Volhard, C. (2008). Live imaging of neuronal degradation by microglia reveals a role for v0-ATPase a1 in phagosomal fusion in vivo. Cell 133, 916-927. (Pubitemid 351707689)
    • (2008) Cell , vol.133 , Issue.5 , pp. 916-927
    • Peri, F.1    Nusslein-Volhard, C.2
  • 52
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • DOI 10.1038/35054500
    • Peters, C., Bayer, M. J., Buhler, S., Andersen, J. S., Mann, M., and Mayer, A. (2001). Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409, 581-588. (Pubitemid 32154803)
    • (2001) Nature , vol.409 , Issue.6820 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 53
    • 7044260932 scopus 로고    scopus 로고
    • Where sterols are required for endocytosis
    • Pichler, H., and Riezman, H. (2004). Where sterols are required for endocytosis. Biochim. Biophys. Acta 1666, 51-61.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 51-61
    • Pichler, H.1    Riezman, H.2
  • 55
    • 0030910237 scopus 로고    scopus 로고
    • Identification of a Saccharomyces gene, LCB3, necessary for incorporation of exogenous long chain bases into sphingolipids
    • Qie, L., Nagiec, M. M., Baltisberger, J. A., Lester, R. L., and Dickson, R. C. (1997). Identification of a Saccharomyces gene, LCB3, necessary for incorporation of exogenous long chain bases into sphingolipids. J. Biol. Chem. 272, 16110-16117.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16110-16117
    • Qie, L.1    Nagiec, M.M.2    Baltisberger, J.A.3    Lester, R.L.4    Dickson, R.C.5
  • 56
    • 33845762823 scopus 로고    scopus 로고
    • Transmembrane proteins are not required for early stages of nuclear envelope assembly
    • Ramos, C., Rafikova, E. R., Melikov, K., and 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
  • 58
    • 59449088040 scopus 로고    scopus 로고
    • Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum
    • Ryan, M., Graham, L. A., and Stevens, T. H. (2008). Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum. Mol. Biol. Cell 19, 5131-5142.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5131-5142
    • Ryan, M.1    Graham, L.A.2    Stevens, T.H.3
  • 59
    • 0029182477 scopus 로고
    • Budding, fission and domain formation in mixed lipid vesicles induced by lateral phase separation and macromolecular condensation
    • Sackmann, E., and Feder, T. (1995). Budding, fission and domain formation in mixed lipid vesicles induced by lateral phase separation and macromolecular condensation. Mol. Membr. Biol. 12, 21-28.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 21-28
    • Sackmann, E.1    Feder, T.2
  • 61
    • 4444348028 scopus 로고    scopus 로고
    • Dynamic domain formation in membranes: Thickness-modulation-induced phase separation
    • Schaffer, E., and Thiele, U. (2004). Dynamic domain formation in membranes: thickness-modulation-induced phase separation. Eur. Phys. J. E Soft Matter 14, 169-175.
    • (2004) Eur. Phys. J. E Soft Matter , vol.14 , pp. 169-175
    • Schaffer, E.1    Thiele, U.2
  • 62
    • 0024564284 scopus 로고
    • Acidification of endosome subpopulations in wild-type Chinese hamster ovary cells and temperature-sensitive acidification-defective mutants
    • DOI 10.1083/jcb.108.4.1291
    • Schmid, S., Fuchs, R., Kielian, M., Helenius, A., and Mellman, I. (1989). Acidification of endosome subpopulations in wild-type Chinese hamster ovary cells and temperature-sensitive acidification-defective mutants. J. Cell Biol. 108, 1291-1300. (Pubitemid 19097038)
    • (1989) Journal of Cell Biology , vol.108 , Issue.4 , pp. 1291-1300
    • Schmid, S.1    Fuchs, R.2    Kielian, M.3    Helenius, A.4    Mellman, I.5
  • 63
    • 0017157457 scopus 로고
    • Nuclear pore absence from areas of close association between nucleus and vacuole in synchronous yeast cultures
    • Severs, N. J., Jordan, E. G., and Williamson, D. H. (1976). Nuclear pore absence from areas of close association between nucleus and vacuole in synchronous yeast cultures. J. Ultrastruct. Res. 54, 374-387.
    • (1976) J. Ultrastruct. Res. , vol.54 , pp. 374-387
    • Severs, N.J.1    Jordan, E.G.2    Williamson, D.H.3
  • 64
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons, K., and Ehehalt, R. (2002). Cholesterol, lipid rafts, and disease. J. Clin. Invest. 110, 597-603.
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 65
    • 33751511196 scopus 로고    scopus 로고
    • The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta-cells
    • Sun-Wada, G. H., Toyomura, T., Murata, Y., Yamamoto, A., Futai, M., and Wada, Y. (2006). The a3 isoform of V-ATPase regulates insulin secretion from pancreatic beta-cells. J. Cell. Sci. 119, 4531-4540.
    • (2006) J. Cell. Sci. , vol.119 , pp. 4531-4540
    • Sun-Wada, G.H.1    Toyomura, T.2    Murata, Y.3    Yamamoto, A.4    Futai, M.5    Wada, Y.6
  • 66
    • 33846116102 scopus 로고    scopus 로고
    • The vacuolar transporter chaperone (VTC) complex is required for microautophagy
    • Uttenweiler, A., Schwarz, H., Neumann, H., and Mayer, A. (2007). The vacuolar transporter chaperone (VTC) complex is required for microautophagy. Mol. Biol. Cell 18, 166-175.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 166-175
    • Uttenweiler, A.1    Schwarz, H.2    Neumann, H.3    Mayer, A.4
  • 67
    • 0032540894 scopus 로고    scopus 로고
    • Disruption of the Saccharomyces cerevisiae FAT1 gene decreases very long-chain fatty acyl-CoA synthetase activity and elevates intracellular very long-chain fatty acid concentrations
    • Watkins, P. A., Lu, J. F., Steinberg, S. J., Gould, S. J., Smith, K. D., and Braiterman, L. T. (1998). Disruption of the Saccharomyces cerevisiae FAT1 gene decreases very long-chain fatty acyl-CoA synthetase activity and elevates intracellular very long-chain fatty acid concentrations. J. Biol. Chem. 273, 18210-18219.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18210-18219
    • Watkins, P.A.1    Lu, J.F.2    Steinberg, S.J.3    Gould, S.J.4    Smith, K.D.5    Braiterman, L.T.6
  • 68
    • 2942623783 scopus 로고    scopus 로고
    • Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: Insights from vesicle recycling in nerve terminals
    • Wenk, M. R., and De Camilli, P. (2004). Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: insights from vesicle recycling in nerve terminals. Proc. Natl. Acad. Sci. USA 101, 8262-8269.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8262-8269
    • Wenk, M.R.1    De Camilli, P.2
  • 69
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto, A., Tagawa, Y., Yoshimori, T., Moriyama, Y., Masaki, R., and Tashiro, Y. (1998). Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 23, 33-42.
    • (1998) Cell Struct. Funct. , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.