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Volumn 3, Issue 2, 2007, Pages 85-92

Nucleus-vacuole junctions and piecemeal microautophagy of the nucleus in S. cerevisiae

Author keywords

Microautophagy; Nuclear envelope; Vacuole

Indexed keywords

FUNGAL PROTEIN; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; PERMEASE; PROTEIN NVJ1P; PROTEIN OSH1P; PROTEIN TSC13P; PROTEIN VAC8P; RAPAMYCIN; TARGET OF RAPAMYCIN KINASE; UNCLASSIFIED DRUG;

EID: 33947375637     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.3586     Document Type: Review
Times cited : (99)

References (76)
  • 1
    • 4344673498 scopus 로고    scopus 로고
    • Mechanisms of chaperone-mediated autophagy
    • Majeski AE, Dice JF. Mechanisms of chaperone-mediated autophagy. Int J Biochem Cell Biol 2004; 36:2435-44.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2435-2444
    • Majeski, A.E.1    Dice, J.F.2
  • 2
    • 0038309329 scopus 로고    scopus 로고
    • The molecular mechanism of autophagy
    • Wang CW, Klionsky DJ. The molecular mechanism of autophagy. Mol Med 2003; 9:65-76.
    • (2003) Mol Med , vol.9 , pp. 65-76
    • Wang, C.W.1    Klionsky, D.J.2
  • 3
    • 0031019152 scopus 로고    scopus 로고
    • Identification of novel vesicles in the cytosol to vacuole protein degradation pathway
    • Huang PH, Chiang HL. Identification of novel vesicles in the cytosol to vacuole protein degradation pathway. J Cell Biol 1997; 136:803-10.
    • (1997) J Cell Biol , vol.136 , pp. 803-810
    • Huang, P.H.1    Chiang, H.L.2
  • 5
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • Yorimitsu T, Klionsky DJ. Autophagy: Molecular machinery for self-eating. Cell Death Differ 2005; 12:1542-52.
    • (2005) Cell Death Differ , vol.12 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 6
    • 1642329712 scopus 로고    scopus 로고
    • Determination of four sequential stages during microautophagy in vitro
    • Kunz JB, Schwarz H, Mayer A. Determination of four sequential stages during microautophagy in vitro. J Biol Chem 2004; 279:9987-96.
    • (2004) J Biol Chem , vol.279 , pp. 9987-9996
    • Kunz, J.B.1    Schwarz, H.2    Mayer, A.3
  • 7
    • 0032482219 scopus 로고    scopus 로고
    • Peroxisome degradation by microautophagy in Pichia pastoris. Identification of specific steps and morphological intermediates
    • Sakai Y, Koller A, Rangell LK, Keller GA, Subramani S. Peroxisome degradation by microautophagy in Pichia pastoris. Identification of specific steps and morphological intermediates. J Cell Biol 1998; 141:625-36.
    • (1998) J Cell Biol , vol.141 , pp. 625-636
    • Sakai, Y.1    Koller, A.2    Rangell, L.K.3    Keller, G.A.4    Subramani, S.5
  • 8
    • 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, Sakai Y. Modification of a ubiquitin-like protein Paz2 conducted micropexophagy through formation of a novel membrane structure. Mol Biol Cell 2004; 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
  • 9
    • 0033747489 scopus 로고    scopus 로고
    • Autophagy in the epithelial cells of murine seminal vesicle in vitro. Formation of large sheets of nascent isolation membranes, sequestration of the nucleus and inhibition by wortmannin and 3-ethyladenine
    • Kovacs AL, Rez G, Palfia Z, Kovacs J. Autophagy in the epithelial cells of murine seminal vesicle in vitro. Formation of large sheets of nascent isolation membranes, sequestration of the nucleus and inhibition by wortmannin and 3-ethyladenine. Cell Tissue Res 2000; 302:253-61.
    • (2000) Cell Tissue Res , vol.302 , pp. 253-261
    • Kovacs, A.L.1    Rez, G.2    Palfia, Z.3    Kovacs, J.4
  • 10
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz GK, Rolls MM, Rapoport TA. Structural organization of the endoplasmic reticulum. EMBO Rep 2002; 3:944-50.
    • (2002) EMBO Rep , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 11
    • 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, Goldfarb DS. Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p. Mol Biol Cell 2000; 11:2445-57.
    • (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
  • 12
    • 0017157457 scopus 로고
    • Nuclear pore absence from areas of close association between nucleus and vacole in synchronous yeast cultures
    • Severs NJ, Jordan EG, Williamson DH. Nuclear pore absence from areas of close association between nucleus and vacole in synchronous yeast cultures. J Ultrastruct Res 1976; 54:374-87.
    • (1976) J Ultrastruct Res , vol.54 , pp. 374-387
    • Severs, N.J.1    Jordan, E.G.2    Williamson, D.H.3
  • 13
    • 0027161821 scopus 로고
    • DiOC6 staining reveals organelle structure and dynamics in living yeast cells
    • Koning AJ, Lum PY, Williams JM, Wright R. DiOC6 staining reveals organelle structure and dynamics in living yeast cells. Cell Motil Cytoskeleton 1993; 25:111-28.
    • (1993) Cell Motil Cytoskeleton , vol.25 , pp. 111-128
    • Koning, A.J.1    Lum, P.Y.2    Williams, J.M.3    Wright, R.4
  • 14
    • 8744254603 scopus 로고    scopus 로고
    • Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae
    • Kvam E, Goldfarb DS. Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae. J Cell Sci 2004; 117:4959-68.
    • (2004) J Cell Sci , vol.117 , pp. 4959-4968
    • Kvam, E.1    Goldfarb, D.S.2
  • 15
    • 33749375121 scopus 로고    scopus 로고
    • Structure and function of nucleus-vacuole junctions: Outer-nuclear-membrane targeting of Nvj1p and a role in tryptophan uptake
    • in press
    • Kvam E, Goldfarb DS. Structure and function of nucleus-vacuole junctions: Outer-nuclear-membrane targeting of Nvj1p and a role in tryptophan uptake. J Cell Sci 2006, (in press).
    • (2006) J Cell Sci
    • Kvam, E.1    Goldfarb, D.S.2
  • 16
    • 0142242210 scopus 로고    scopus 로고
    • Signal-anchor domains of proteins of the outer membrane of mitochondria: Structural and functional characteristics
    • Waizenegger T, Stan T, Neupert W, Rapaport D. Signal-anchor domains of proteins of the outer membrane of mitochondria: Structural and functional characteristics. J Biol Chem 2003; 278:42064-71.
    • (2003) J Biol Chem , vol.278 , pp. 42064-42071
    • Waizenegger, T.1    Stan, T.2    Neupert, W.3    Rapaport, D.4
  • 17
    • 32644479020 scopus 로고    scopus 로고
    • Here come the SUNs: A nucleocytoskeletal missing link
    • Worman HJ, Gundersen GG. Here come the SUNs: A nucleocytoskeletal missing link Trends Cell Biol 2006; 16:67-9.
    • (2006) Trends Cell Biol , vol.16 , pp. 67-69
    • Worman, H.J.1    Gundersen, G.G.2
  • 18
    • 30444450095 scopus 로고    scopus 로고
    • KASH 'n Karry: The KASH domain family of cargo-specific cytoskeletal adaptor proteins
    • Starr DA, Fischer JA. KASH 'n Karry: The KASH domain family of cargo-specific cytoskeletal adaptor proteins. Bioessays 2005; 27:1136-46.
    • (2005) Bioessays , vol.27 , pp. 1136-1146
    • Starr, D.A.1    Fischer, J.A.2
  • 19
    • 23944488301 scopus 로고    scopus 로고
    • Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPI1 vesicle
    • Lee MC, Orci L, Hamamoto S, Futai E, Ravazzola M, Schekman R, Sar1p N-terminal helix initiates membrane curvature and completes the fission of a COPI1 vesicle. Cell 2005; 122:605-17.
    • (2005) Cell , vol.122 , pp. 605-617
    • Lee, M.C.1    Orci, L.2    Hamamoto, S.3    Futai, E.4    Ravazzola, M.5    Schekman, R.6
  • 20
    • 0031669618 scopus 로고    scopus 로고
    • YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance
    • Pan X, Goldfarb DS. YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance. J Cell Sci 1998; 111:2137-47.
    • (1998) J Cell Sci , vol.111 , pp. 2137-2147
    • Pan, X.1    Goldfarb, D.S.2
  • 21
    • 0031739531 scopus 로고    scopus 로고
    • Yel013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin α, is associated with the yeast vacuole membrane
    • Fleckenstein D, Rohde M, Klionsky DJ, Rüdiger M. Yel013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin α, is associated with the yeast vacuole membrane. J Cell Sci 1998; 111:3109-18.
    • (1998) J Cell Sci , vol.111 , pp. 3109-3118
    • Fleckenstein, D.1    Rohde, M.2    Klionsky, D.J.3    Rüdiger, M.4
  • 22
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • Hatzfeld M. The armadillo family of structural proteins. Int Rev Cytol 1999; 186:179-224.
    • (1999) Int Rev Cytol , vol.186 , pp. 179-224
    • Hatzfeld, M.1
  • 23
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang YX, Catlett NL, Weisman LS. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J Cell Biol 1998; 140:1063-74.
    • (1998) J Cell Biol , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 25
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • Levine T. Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions. Trends Cell Biol 2004; 14:483-90.
    • (2004) Trends Cell Biol , vol.14 , pp. 483-490
    • Levine, T.1
  • 27
    • 33645754484 scopus 로고    scopus 로고
    • Organelles on the move: Insights from yeast vacuole inheritance
    • Weisman LS. Organelles on the move: Insights from yeast vacuole inheritance. Nat Rev Mol Cell Biol 2006; 7:243-52.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 243-252
    • Weisman, L.S.1
  • 28
    • 0346503885 scopus 로고    scopus 로고
    • The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the preautophagosomal structure
    • Reggioti F, Tucker KA, Stromhaug PE, Klionsky DJ. The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the preautophagosomal structure. Dev Cell 2004; 6:79-90.
    • (2004) Dev Cell , vol.6 , pp. 79-90
    • Reggioti, F.1    Tucker, K.A.2    Stromhaug, P.E.3    Klionsky, D.J.4
  • 30
    • 22044433038 scopus 로고    scopus 로고
    • Endoplasmic reticulum: One continuous network compartmentalized by extrinsic cues
    • Levine T, Rabouille C. Endoplasmic reticulum: One continuous network compartmentalized by extrinsic cues. Curr Opin Cell Biol 2005; 17:362-8.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 362-368
    • Levine, T.1    Rabouille, C.2
  • 31
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • Staehelin LA. The plant ER: A dynamic organelle composed of a large number of discrete functional domains. Plant J 1997; 11:1151-65.
    • (1997) Plant J , vol.11 , pp. 1151-1165
    • Staehelin, L.A.1
  • 32
    • 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 SD, Eder S, Oh CS, Martin CE, Gable K, Bacikova D, Dunn T. Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol Cell Biol 2001; 21:109-25.
    • (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
  • 33
    • 0038280115 scopus 로고    scopus 로고
    • Functional differentiation and selective inactivation of multiple Saccharomyces cerevisiae genes involved in very-long-chain fatty acid synthesis
    • Rossler H, Rieck C, Delong T, Hoja U, Schweizer E. Functional differentiation and selective inactivation of multiple Saccharomyces cerevisiae genes involved in very-long-chain fatty acid synthesis. Mol Genet Genomics 2003; 269:290-8.
    • (2003) Mol Genet Genomics , vol.269 , pp. 290-298
    • Rossler, H.1    Rieck, C.2    Delong, T.3    Hoja, U.4    Schweizer, E.5
  • 34
    • 0037470063 scopus 로고    scopus 로고
    • Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
    • Moon YA, Horton JD. Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade. J Biol Chem 2003; 278:7335-43.
    • (2003) J Biol Chem , vol.278 , pp. 7335-7343
    • Moon, Y.A.1    Horton, J.D.2
  • 35
    • 0031662853 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals
    • Dickson RC. Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals. Annu Rev Biochem 1998; 67:27-48.
    • (1998) Annu Rev Biochem , vol.67 , pp. 27-48
    • Dickson, R.C.1
  • 36
    • 23644451810 scopus 로고    scopus 로고
    • Silencing of NbECR encoding a putative enoyl-CoA reductase results in disorganized membrane structures and epidermal cell ablation in Nicotiana benthamiana
    • Park JA, Kim TW, Kim SK, Kim WT, Pai HS. Silencing of NbECR encoding a putative enoyl-CoA reductase results in disorganized membrane structures and epidermal cell ablation in Nicotiana benthamiana. FEBS Lett 2005; 579:4459-64.
    • (2005) FEBS Lett , vol.579 , pp. 4459-4464
    • Park, J.A.1    Kim, T.W.2    Kim, S.K.3    Kim, W.T.4    Pai, H.S.5
  • 37
    • 0030960623 scopus 로고    scopus 로고
    • Organelle structure, function, and inheritance in yeast: A role for fatty acid synthesis?
    • Schneiter R, Kohlwein SD. Organelle structure, function, and inheritance in yeast: A role for fatty acid synthesis? Cell 1997; 88:431-4.
    • (1997) Cell , vol.88 , pp. 431-434
    • Schneiter, R.1    Kohlwein, S.D.2
  • 38
    • 0029094333 scopus 로고
    • Interactions of a very long chain fatty acid with model membranes and serum albumin: Implications for the pathogenesis of adrenoleukodystrophy
    • Ho JK, Moser H, Kishimoto Y, Hamilton JA. Interactions of a very long chain fatty acid with model membranes and serum albumin: Implications for the pathogenesis of adrenoleukodystrophy. J Clin Invest 1995; 96:1455-63.
    • (1995) J Clin Invest , vol.96 , pp. 1455-1463
    • Ho, J.K.1    Moser, H.2    Kishimoto, Y.3    Hamilton, J.A.4
  • 39
    • 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 TP, Munro S. Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction. Mol Biol Cell 2001; 12:1633-44.
    • (2001) Mol Biol Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 40
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • Beh CT, Cool L, Phillips J, Rine J. Overlapping functions of the yeast oxysterol-binding protein homologues. Genetics 2001; 157:1117-40.
    • (2001) Genetics , vol.157 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 41
    • 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 CT, Rine J. A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution. J Cell Sci 2004; 117:2983-96.
    • (2004) J Cell Sci , vol.117 , pp. 2983-2996
    • Beh, C.T.1    Rine, J.2
  • 42
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Im YJ, Raychaudhuri S, Prinz WA, Hurley JH. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 2005; 437:154-8.
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 43
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • Loewen CJ, Roy A, Levine TP. A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP. EMBO J 2003; 22:2025-35.
    • (2003) EMBO J , vol.22 , pp. 2025-2035
    • Loewen, C.J.1    Roy, A.2    Levine, T.P.3
  • 44
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • Johansson M, Lehro M, Tanhaunpaa K, Covet TL, Olkkonen VM. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol Biol Cell 2005; 16:5480-92.
    • (2005) Mol Biol Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehro, M.2    Tanhaunpaa, K.3    Covet, T.L.4    Olkkonen, V.M.5
  • 45
    • 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 TM, Goldfarb DS. Targeting of Tsc13p to nucleus-vacuole junctions: A role for very-long-chain fatty acids in the biogenesis of microautophagic vesicles. Mol Biol Cell 2005; 16:3987-98.
    • (2005) Mol Biol Cell , vol.16 , pp. 3987-3998
    • Kvam, E.1    Gable, K.2    Dunn, T.M.3    Goldfarb, D.S.4
  • 48
    • 0031825456 scopus 로고    scopus 로고
    • A search in the genome of Saccharomyces cerevisiae for genes regulated via stress response elements
    • Moskvina E, Schuller C, Maurer CT, Mager WH, Ruis H. A search in the genome of Saccharomyces cerevisiae for genes regulated via stress response elements. Yeast 1998; 14:1041-50.
    • (1998) Yeast , vol.14 , pp. 1041-1050
    • Moskvina, E.1    Schuller, C.2    Maurer, C.T.3    Mager, W.H.4    Ruis, H.5
  • 49
    • 4444293342 scopus 로고    scopus 로고
    • Peroxisome turnover by micropexophagy: An autophagy-related process
    • Farre JC, Subramani S. Peroxisome turnover by micropexophagy: An autophagy-related process. Trends Cell Biol 2004; 14:515-23.
    • (2004) Trends Cell Biol , vol.14 , pp. 515-523
    • Farre, J.C.1    Subramani, S.2
  • 52
    • 0034735511 scopus 로고    scopus 로고
    • Cell-free reconstitution of microautophagic vacuole invagination and vesicle formation
    • Sattler T, Mayer A. Cell-free reconstitution of microautophagic vacuole invagination and vesicle formation. J Cell Biol 2000; 151:529-38.
    • (2000) J Cell Biol , vol.151 , pp. 529-538
    • Sattler, T.1    Mayer, A.2
  • 53
    • 21244448694 scopus 로고    scopus 로고
    • The TOR and EGO protein complexes orchestrate microautophagy in yeast
    • Dubouloz F, Deloche O, Wanke V, Cameroni E, De Virgilio C. The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol Cell 2005; 19:15-26.
    • (2005) Mol Cell , vol.19 , pp. 15-26
    • Dubouloz, F.1    Deloche, O.2    Wanke, V.3    Cameroni, E.4    De Virgilio, C.5
  • 54
    • 0029973561 scopus 로고    scopus 로고
    • A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex
    • Schneiter R, Hitomi M, Ivessa AS, Fasch EV, Kohlwein SD, Tartakoff AM. A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex. Mol Cell Biol 1996; 16:7161-72.
    • (1996) Mol Cell Biol , vol.16 , pp. 7161-7172
    • Schneiter, R.1    Hitomi, M.2    Ivessa, A.S.3    Fasch, E.V.4    Kohlwein, S.D.5    Tartakoff, A.M.6
  • 55
    • 11244258475 scopus 로고    scopus 로고
    • Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
    • Fratti RA, Jun Y, Merz AJ, 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; 167:1087-98.
    • (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
  • 58
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Wang YX, Kauffman EJ, Duex JE, Weisman LS. Fusion of docked membranes requires the armadillo repeat protein Vac8p. J Biol Chem 2001; 276:35133-40.
    • (2001) J Biol Chem , vol.276 , pp. 35133-35140
    • Wang, Y.X.1    Kauffman, E.J.2    Duex, J.E.3    Weisman, L.S.4
  • 59
    • 0036915634 scopus 로고    scopus 로고
    • A specific structural requirement for ergosterol in long-chain fatty acid synthesis mutants important for maintaining raft domains in yeast
    • Eisenkolb M, Zenzmaier C, Leitner E. Schneiter R. A specific structural requirement for ergosterol in long-chain fatty acid synthesis mutants important for maintaining raft domains in yeast. Mol Biol Cell 2002; 13:4414-28.
    • (2002) Mol Biol Cell , vol.13 , pp. 4414-4428
    • Eisenkolb, M.1    Zenzmaier, C.2    Leitner, E.3    Schneiter, R.4
  • 60
    • 0028351736 scopus 로고
    • Ribosome synthesis during the growth cycle of Saccharomyces cerevisiae
    • Ju Q, Warner JR. Ribosome synthesis during the growth cycle of Saccharomyces cerevisiae. Yeast 1994; 10:151-7.
    • (1994) Yeast , vol.10 , pp. 151-157
    • Ju, Q.1    Warner, J.R.2
  • 61
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang K, Kaufman RJ. Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb Exp Pharmacol 2006; 172:69-91.
    • (2006) Handb Exp Pharmacol , vol.172 , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 62
    • 0035834122 scopus 로고    scopus 로고
    • Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection
    • Nollen EA, Salomons FA, Brunsting JF, Want JJ, Sibon OC, Kampinga HH. Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protection Proc Natl Acad Sci USA 2001; 98:12038-43.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12038-12043
    • Nollen, E.A.1    Salomons, F.A.2    Brunsting, J.F.3    Want, J.J.4    Sibon, O.C.5    Kampinga, H.H.6
  • 63
    • 0027421919 scopus 로고
    • Ultrastructural changes in yeast following heat shock and recovery
    • Webster DL, Watson K. Ultrastructural changes in yeast following heat shock and recovery. Yeast 1993; 9:1165-75.
    • (1993) Yeast , vol.9 , pp. 1165-1175
    • Webster, D.L.1    Watson, K.2
  • 65
    • 33745386112 scopus 로고    scopus 로고
    • Yeast nuclear envelope subdomains with distinct abilities to resist membrane expansion
    • Campbell JL, Lorenz A, Witkin KL, Hays T, Loidl J, Cohen-Fix O. Yeast nuclear envelope subdomains with distinct abilities to resist membrane expansion. Mol Biol Cell 2006; 17:1768-78.
    • (2006) Mol Biol Cell , vol.17 , pp. 1768-1778
    • Campbell, J.L.1    Lorenz, A.2    Witkin, K.L.3    Hays, T.4    Loidl, J.5    Cohen-Fix, O.6
  • 66
    • 32044465506 scopus 로고    scopus 로고
    • TOR signalling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. TOR signalling in growth and metabolism. Cell 2006; 124:471-84.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 67
    • 0033588918 scopus 로고    scopus 로고
    • Starvation induces vacuolar targeting and degradation of the tyrptophan permease in yeast
    • Beck T, Schmidt A, Hall MN. Starvation induces vacuolar targeting and degradation of the tyrptophan permease in yeast. J Cell Biol 1999; 146:1227-38.
    • (1999) J Cell Biol , vol.146 , pp. 1227-1238
    • Beck, T.1    Schmidt, A.2    Hall, M.N.3
  • 68
    • 0032403058 scopus 로고    scopus 로고
    • The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease
    • Schmidt A, Beck T, Koller A, Kunz J, Hall MN. The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease. EMBO J 1998; 17:6924-31.
    • (1998) EMBO J , vol.17 , pp. 6924-6931
    • Schmidt, A.1    Beck, T.2    Koller, A.3    Kunz, J.4    Hall, M.N.5
  • 69
    • 0038491550 scopus 로고    scopus 로고
    • Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane
    • Umehayashi K, Nakano A. Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane. J Cell Biol 2003; 161:1117-31.
    • (2003) J Cell Biol , vol.161 , pp. 1117-1131
    • Umehayashi, K.1    Nakano, A.2
  • 70
    • 33645216185 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins are required for the transport of detergent-resistant microdomain-associated membrane proteins Tat2p and Fur4p
    • Okamoto M, Yoko-O T, Umemura M, Nakayama K, Jigami Y. Glycosylphosphatidylinositol-anchored proteins are required for the transport of detergent-resistant microdomain-associated membrane proteins Tat2p and Fur4p. J Biol Chem 2006; 281:4013-23.
    • (2006) J Biol Chem , vol.281 , pp. 4013-4023
    • Okamoto, M.1    Yoko-O, T.2    Umemura, M.3    Nakayama, K.4    Jigami, Y.5
  • 71
    • 0028213802 scopus 로고
    • A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein
    • Jiang B, Brown JL, Sheraton J, Fortin N, Bussey N. A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein. Yeast 1994; 10:341-53.
    • (1994) Yeast , vol.10 , pp. 341-353
    • Jiang, B.1    Brown, J.L.2    Sheraton, J.3    Fortin, N.4    Bussey, N.5
  • 73
    • 33745745910 scopus 로고    scopus 로고
    • A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast
    • Gao M, Kaiser CA. A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast. Nat Cell Biol 2006; 8:657-67.
    • (2006) Nat Cell Biol , vol.8 , pp. 657-667
    • Gao, M.1    Kaiser, C.A.2
  • 74
    • 0018760796 scopus 로고
    • Luteinizing hormone-accelerated redistribution of lysosome-like organelles preceding dissolution of the nuclear envelope in rat oocytes maturing in vitro
    • Ezzell RM, Szego CM. Luteinizing hormone-accelerated redistribution of lysosome-like organelles preceding dissolution of the nuclear envelope in rat oocytes maturing in vitro. J Cell Biol 1979; 82:264-77.
    • (1979) J Cell Biol , vol.82 , pp. 264-277
    • Ezzell, R.M.1    Szego, C.M.2
  • 75
    • 0035069454 scopus 로고    scopus 로고
    • Lysosomal enzymes in the macronucleus of Tetrahymena during its apoptosis-like degragation
    • Lu E, Wolfe J. Lysosomal enzymes in the macronucleus of Tetrahymena during its apoptosis-like degragation. Cell Death Differ 2001; 8:289-97.
    • (2001) Cell Death Differ , vol.8 , pp. 289-297
    • Lu, E.1    Wolfe, J.2
  • 76
    • 33645951059 scopus 로고    scopus 로고
    • Death harmony played by nucleus and mitochondria: Nuclear apoptosis during conjugation of Tetrahymena
    • Endoh H, Kobayashi T. Death harmony played by nucleus and mitochondria: Nuclear apoptosis during conjugation of Tetrahymena. Autophagy 2006; 2:129-31.
    • (2006) Autophagy , vol.2 , pp. 129-131
    • Endoh, H.1    Kobayashi, T.2


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