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Volumn 37, Issue , 2003, Pages 435-460

Yeast Vacuole Inheritance and Dynamics

Author keywords

Actin based transport; Myosin V; Osmotic stress; Phosphatidylinositol 3,5 bisphosphate; Protein acylation

Indexed keywords

BISPHOSPHONIC ACID DERIVATIVE; FUNGAL PROTEIN; GENE PRODUCT; ISOPROTEIN; MYOSIN V; PHOSPHATASE; RECEPTOR;

EID: 0347416707     PISSN: 00664197     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.genet.37.050203.103207     Document Type: Review
Times cited : (109)

References (138)
  • 1
    • 0036118329 scopus 로고    scopus 로고
    • The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains
    • Ahn A, Gibbons DL, Kielian M. 2002. The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains. J. Virol. 76:3267-75
    • (2002) J. Virol. , vol.76 , pp. 3267-3275
    • Ahn, A.1    Gibbons, D.L.2    Kielian, M.3
  • 2
    • 0022753540 scopus 로고
    • PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors
    • Ammerer G, Hunter CP, Rothman JH, Saari GC, Valls LA, Stevens TH. 1986. PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell. Biol. 6:2490-99
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2490-2499
    • Ammerer, G.1    Hunter, C.P.2    Rothman, J.H.3    Saari, G.C.4    Valls, L.A.5    Stevens, T.H.6
  • 3
    • 0000272957 scopus 로고
    • Isolation of yeast mutants defective in protein targeting to the vacuole
    • Bankaitis VA, Johnson LM, Emr SD. 1986. Isolation of yeast mutants defective in protein targeting to the vacuole. Proc. Natl. Acad. Sci. USA 83:9075-79
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9075-9079
    • Bankaitis, V.A.1    Johnson, L.M.2    Emr, S.D.3
  • 4
    • 0024095176 scopus 로고
    • Organelle assembly in yeast: Characterization of yeast mutants defective in vacuolar biogenesis and protein sorting
    • Banta LM, Robinson JS, Klionsky DJ, Emr SD. 1988. Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting. J. Cell Biol. 108:1369-83
    • (1988) J. Cell Biol. , vol.108 , pp. 1369-1383
    • Banta, L.M.1    Robinson, J.S.2    Klionsky, D.J.3    Emr, S.D.4
  • 5
    • 0034735942 scopus 로고    scopus 로고
    • The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast
    • Beach DL, Thibodeaux J, Maddox P, Yeh E, Bloom K. 2000. The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast. Curr. Biol. 10:1497-506
    • (2000) Curr. Biol. , vol.10 , pp. 1497-1506
    • Beach, D.L.1    Thibodeaux, J.2    Maddox, P.3    Yeh, E.4    Bloom, K.5
  • 6
    • 0034966332 scopus 로고    scopus 로고
    • Mitochondrial inheritance in budding yeast
    • Boldogh IR, Yang HC, Pon LA. 2001. Mitochondrial inheritance in budding yeast. Traffic 2:368-74
    • (2001) Traffic , vol.2 , pp. 368-374
    • Boldogh, I.R.1    Yang, H.C.2    Pon, L.A.3
  • 7
    • 0030692711 scopus 로고    scopus 로고
    • Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology
    • Bonangelino C, Catlett N, Weisman LS. 1997. Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology. Mol. Cell Biol. 17:6847-58
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6847-6858
    • Bonangelino, C.1    Catlett, N.2    Weisman, L.S.3
  • 8
    • 0037128929 scopus 로고    scopus 로고
    • Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p
    • Bonangelino CJ, Nau JJ, Duex JE, Brinkman M, Wurmser AE, et al. 2002. Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p. J. Cell Biol. 156:1015-28
    • (2002) J. Cell Biol. , vol.156 , pp. 1015-1028
    • Bonangelino, C.J.1    Nau, J.J.2    Duex, J.E.3    Brinkman, M.4    Wurmser, A.E.5
  • 9
    • 0031854866 scopus 로고    scopus 로고
    • Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment
    • Bryant NJ, Piper RC, Weisman LS, Stevens TH. 1998. Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment. J. Cell Biol. 142:651-63
    • (1998) J. Cell Biol. , vol.142 , pp. 651-663
    • Bryant, N.J.1    Piper, R.C.2    Weisman, L.S.3    Stevens, T.H.4
  • 10
    • 0034618049 scopus 로고    scopus 로고
    • Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes
    • Catlett N, Duex J, Tang F, Weisman L. 2000. Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes. J. Cell Biol. 150:513-25
    • (2000) J. Cell Biol. , vol.150 , pp. 513-525
    • Catlett, N.1    Duex, J.2    Tang, F.3    Weisman, L.4
  • 11
    • 0033934232 scopus 로고    scopus 로고
    • Divide and multiply: Organelle partitioning in yeast
    • Catlett N, Weisman L. 2000. Divide and multiply: organelle partitioning in yeast. Curr. Opin. Cell Biol. 12:509-16
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 509-516
    • Catlett, N.1    Weisman, L.2
  • 12
    • 0032426664 scopus 로고    scopus 로고
    • The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth
    • Catlett NL, Weisman LS. 1998. The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth. Proc. Natl. Acad. Sci. USA 95:14799-804
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14799-14804
    • Catlett, N.L.1    Weisman, L.S.2
  • 13
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis
    • Chamberlain LH, Burgoyne RD, Gould GW. 2001. SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. Proc. Natl. Acad. Sci. USA 98:5619-24
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 14
    • 0031028059 scopus 로고    scopus 로고
    • apd1(+), a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: A role for glutathione and a glutathione-conjugate pump
    • 13a. Chaudhuri B, Ingavale S, Bachhawat AK. 1997. apd1(+), a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: A role for glutathione and a glutathione-conjugate pump. Genetics 145:7583
    • (1997) Genetics , vol.145 , pp. 7583
    • Chaudhuri, B.1    Ingavale, S.2    Bachhawat, A.K.3
  • 15
    • 0043160475 scopus 로고    scopus 로고
    • The glutathione-mediated detoxification pathway in yeast: An analysis using the red pigment that accumulates in certain adenine biosynthetic mutants of yeasts reveals the involvement of novel genes
    • DOI 10.1007/s00203-003-0566-z
    • 13b. Sharma KG, Kaur R, Bachhawat AK. 2003. The glutathione-mediated detoxification pathway in yeast: An analysis using the red pigment that accumulates in certain adenine biosynthetic mutants of yeasts reveals the involvement of novel genes. Arch. Microbiol. DOI 10.1007/s00203-003-0566-z
    • (2003) Arch. Microbiol.
    • Sharma, K.G.1    Kaur, R.2    Bachhawat, A.K.3
  • 17
    • 0035861863 scopus 로고    scopus 로고
    • Yeast Cbk1 and Mob2 activate daughter-specific genetic programs to induce asymmetric cell fates
    • Colman-Lerner A, Chin TE, Brent R. 2001. Yeast Cbk1 and Mob2 activate daughter-specific genetic programs to induce asymmetric cell fates. Cell 107:739-50
    • (2001) Cell , vol.107 , pp. 739-750
    • Colman-Lerner, A.1    Chin, T.E.2    Brent, R.3
  • 18
    • 0032516807 scopus 로고    scopus 로고
    • Multiple sorting pathways between the late Golgi and the vacuole in yeast
    • Conibear E, Stevens TH. 1998. Multiple sorting pathways between the late Golgi and the vacuole in yeast. Biochim. Biophys. Acta 1404:211-30
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 211-230
    • Conibear, E.1    Stevens, T.H.2
  • 19
  • 20
    • 0037018842 scopus 로고    scopus 로고
    • Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body
    • Dove SK, McEwen RK, Mayes A, Hughes DC, Beggs JD, Michell RH. 2002. Vac14 controls PtdIns(3,5)P(2) synthesis and Fab1-dependent protein trafficking to the multivesicular body. Curr. Biol. 12:885-93
    • (2002) Curr. Biol. , vol.12 , pp. 885-893
    • Dove, S.K.1    McEwen, R.K.2    Mayes, A.3    Hughes, D.C.4    Beggs, J.D.5    Michell, R.H.6
  • 21
    • 0035158456 scopus 로고    scopus 로고
    • Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae
    • Du Y, Pypaert M, Novick P, Ferro-Novick S. 2001. Aux1p/Swa2p is required for cortical endoplasmic reticulum inheritance in Saccharomyces cerevisiae. Mol. Biol. Cell 12:2614-28
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2614-2628
    • Du, Y.1    Pypaert, M.2    Novick, P.3    Ferro-Novick, S.4
  • 22
    • 0035967873 scopus 로고    scopus 로고
    • Vps9, Rabex-5 and DSS4: Proteins with weak but distinct nucleotide-exchange activities for Rab proteins
    • Esters H, Alexandrov K, Iakovenko A, Ivanova T, Thoma N, et al. 2001. Vps9, Rabex-5 and DSS4: proteins with weak but distinct nucleotide-exchange activities for Rab proteins. J. Mol. Biol. 310:141-56
    • (2001) J. Mol. Biol. , vol.310 , pp. 141-156
    • Esters, H.1    Alexandrov, K.2    Iakovenko, A.3    Ivanova, T.4    Thoma, N.5
  • 23
    • 0036198747 scopus 로고    scopus 로고
    • Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast
    • Fehrenbacher KL, Davis D, Wu M, Boldogh I, Pon LA. 2002. Endoplasmic reticulum dynamics, inheritance, and cytoskeletal interactions in budding yeast. Mol. Biol. Cell 13:854-65
    • (2002) Mol. Biol. Cell , vol.13 , pp. 854-865
    • Fehrenbacher, K.L.1    Davis, D.2    Wu, M.3    Boldogh, I.4    Pon, L.A.5
  • 24
    • 0031739531 scopus 로고    scopus 로고
    • Ye1013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin alpha is associated with the yeast vacuole membrane
    • Fleckenstein D, Rohde M, Klionsky DJ, Rudiger M. 1998. Ye1013p (Vac8p), an armadillo repeat protein related to plakoglobin and importin alpha is associated with the yeast vacuole membrane. J. Cell Sci. 111:3109-18
    • (1998) J. Cell Sci. , vol.111 , pp. 3109-3118
    • Fleckenstein, D.1    Rohde, M.2    Klionsky, D.J.3    Rudiger, M.4
  • 25
    • 0037044819 scopus 로고    scopus 로고
    • Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin
    • Fukuda M, Kuroda TS. 2002. Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin. J. Biol. Chem. 277: 43096-103
    • (2002) J. Biol. Chem. , vol.277 , pp. 43096-43103
    • Fukuda, M.1    Kuroda, T.S.2
  • 26
    • 0036231465 scopus 로고    scopus 로고
    • Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member
    • Gary JD, Sato TK, Stefan CJ, Bonangelino CJ, Weisman LS, Emr SD. 2002. Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member. Mol. Biol. Cell 13:1238-51
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1238-1251
    • Gary, J.D.1    Sato, T.K.2    Stefan, C.J.3    Bonangelino, C.J.4    Weisman, L.S.5    Emr, S.D.6
  • 27
    • 0032487577 scopus 로고    scopus 로고
    • Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis
    • Gary JD, Wurmser AE, Bonangelino CJ, Weisman LS, Emr SD. 1998. Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis. J. Cell Biol. 143:65-79
    • (1998) J. Cell Biol. , vol.143 , pp. 65-79
    • Gary, J.D.1    Wurmser, A.E.2    Bonangelino, C.J.3    Weisman, L.S.4    Emr, S.D.5
  • 28
    • 0030816513 scopus 로고    scopus 로고
    • Vacuole segregation in the Saccharomyces cerevisiaevac2-I mutant: Structural and biochemical quantification of the segregation defect and formation of new vacuoles
    • Gomes de Mesquita DS, Shaw J, Grimbergen JA, Buys MA, Dewi L, Woldringh CL. 1997. Vacuole segregation in the Saccharomyces cerevisiaevac2-I mutant: structural and biochemical quantification of the segregation defect and formation of new vacuoles. Yeast 13:999-1008
    • (1997) Yeast , vol.13 , pp. 999-1008
    • Gomes De Mesquita, D.S.1    Shaw, J.2    Grimbergen, J.A.3    Buys, M.A.4    Dewi, L.5    Woldringh, C.L.6
  • 29
    • 0025952205 scopus 로고
    • Vacuolar segregation to the bud of S. cerevisiae: An analysis of the morphology and timing in the cell cycle
    • Gomes de Mesquita DS, ten Hoopen R, Woldringh CL. 1991. Vacuolar segregation to the bud of S. cerevisiae: an analysis of the morphology and timing in the cell cycle. J. Gen. Microbiol. 137:2447-54
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2447-2454
    • Gomes De Mesquita, D.S.1    Ten Hoopen, R.2    Woldringh, C.L.3
  • 30
    • 0029908193 scopus 로고    scopus 로고
    • Characterization of new vacuolar segregation mutants, isolated by screening for loss of proteinase B self-activation
    • Gomes de Mesquita DS, van den Haazel B, Bouwman J, Woldringh CL. 1996. Characterization of new vacuolar segregation mutants, isolated by screening for loss of proteinase B self-activation. Eur. J. Cell Biol. 71:237-47
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 237-247
    • Gomes De Mesquita, D.S.1    Van Den Haazel, B.2    Bouwman, J.3    Woldringh, C.L.4
  • 31
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan B, Bowser R, Novick P. 1995. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128:1055-68
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 32
    • 0033532062 scopus 로고    scopus 로고
    • SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
    • Guo S, Stolz LE, Lemrow SM, York JD. 1999. SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases. J. Biol. Chem. 274:12990-95
    • (1999) J. Biol. Chem. , vol.274 , pp. 12990-12995
    • Guo, S.1    Stolz, L.E.2    Lemrow, S.M.3    York, J.D.4
  • 33
    • 0033591319 scopus 로고    scopus 로고
    • Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport
    • Hama H, Tall GG, Horazdovsky BF. 1999. Vps9p is a guanine nucleotide exchange factor involved in vesicle-mediated vacuolar protein transport. J. Biol. Chem. 274:15284-91
    • (1999) J. Biol. Chem. , vol.274 , pp. 15284-15291
    • Hama, H.1    Tall, G.G.2    Horazdovsky, B.F.3
  • 35
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke L. 1999. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9:107-12
    • (1999) Trends Cell Biol. , vol.9 , pp. 107-112
    • Hicke, L.1
  • 36
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during yeast cell division in Saccharomyces cerevisiae
    • Hill KL, Catlett NL, Weisman LS. 1996. Actin and myosin function in directed vacuole movement during yeast cell division in Saccharomyces cerevisiae. J. Cell Biol. 135:1535-49
    • (1996) J. Cell Biol. , vol.135 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 37
    • 0035842904 scopus 로고    scopus 로고
    • A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae
    • Hoepfner D, van den Berg M, Philippsen P, Tabak HF, Hettema EH. 2001. A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance and inheritance in Saccharomyces cerevisiae. J. Cell Biol. 155:979-90
    • (2001) J. Cell Biol. , vol.155 , pp. 979-990
    • Hoepfner, D.1    Van Den Berg, M.2    Philippsen, P.3    Tabak, H.F.4    Hettema, E.H.5
  • 38
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann S. 2002. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev. 66:300-72
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 39
    • 0028348688 scopus 로고
    • VPS21 encodes a rab5-like GTP binding protein that is required for the sorting of yeast vacuolar proteins
    • Horazdovsky BF, Busch GR, Emr SD. 1994. VPS21 encodes a rab5-like GTP binding protein that is required for the sorting of yeast vacuolar proteins. EMBO J. 13:1297-309
    • (1994) EMBO J. , vol.13 , pp. 1297-1309
    • Horazdovsky, B.F.1    Busch, G.R.2    Emr, S.D.3
  • 40
    • 0030460781 scopus 로고    scopus 로고
    • A novel RING finger protein, Vps8p, functionally interacts with the small GTPase, Vps21p, to facilitate soluble vacuolar protein localization
    • Horazdovsky BF, Cowles CR, Mustol P, Holmes M, Emr SD. 1996. A novel RING finger protein, Vps8p, functionally interacts with the small GTPase, Vps21p, to facilitate soluble vacuolar protein localization. J. Biol. Chem. 271:33607-15
    • (1996) J. Biol. Chem. , vol.271 , pp. 33607-33615
    • Horazdovsky, B.F.1    Cowles, C.R.2    Mustol, P.3    Holmes, M.4    Emr, S.D.5
  • 41
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin
    • Huber AH, Weis WI. 2001. The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Cell 105:391-402
    • (2001) Cell , vol.105 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 42
    • 0033977744 scopus 로고    scopus 로고
    • SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases
    • Hughes WE, Woscholski R, Cooke FT, Patrick RS, Dove SK, et al. 2000. SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases. J. Biol. Chem. 275:801-8
    • (2000) J. Biol. Chem. , vol.275 , pp. 801-808
    • Hughes, W.E.1    Woscholski, R.2    Cooke, F.T.3    Patrick, R.S.4    Dove, S.K.5
  • 44
    • 0036839610 scopus 로고    scopus 로고
    • Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae
    • Itoh T, Watabe A, Toh EA, Matsui Y. 2002. Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae. Mol. Cell. Biol. 22:7744-57
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7744-7757
    • Itoh, T.1    Watabe, A.2    Toh, E.A.3    Matsui, Y.4
  • 45
    • 0034671142 scopus 로고    scopus 로고
    • Yeast mitochondrial dynamics: Fusion, division, segregation, and shape
    • Jensen RE, Hobbs AE, Cerveny KL, Sesaki H. 2000. Yeast mitochondrial dynamics: fusion, division, segregation, and shape. Microsc. Res. Tech. 51:573-83
    • (2000) Microsc. Res. Tech. , vol.51 , pp. 573-583
    • Jensen, R.E.1    Hobbs, A.E.2    Cerveny, K.L.3    Sesaki, H.4
  • 46
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston GC, Prendergast JA, Singer RA. 1991. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113:539-51
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 47
    • 0036270964 scopus 로고    scopus 로고
    • Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae
    • Jones EW. 2002. Vacuolar proteases and proteolytic artifacts in Saccharomyces cerevisiae. Methods Enzymol. 351:127-50
    • (2002) Methods Enzymol. , vol.351 , pp. 127-150
    • Jones, E.W.1
  • 48
    • 0000773895 scopus 로고
    • Regulation of amino acid and nucleotide biosynthesis in yeast
    • ed. JN Strathern, EW Jones, JR Broach, Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • Jones EW, Fink GR. 1982. Regulation of amino acid and nucleotide biosynthesis in yeast. In The Molecular Biology of the Yeast Saccharomyces. Metabolism and Gene Expression, ed. JN Strathern, EW Jones, JR Broach, pp. 181-299. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • (1982) The Molecular Biology of the Yeast Saccharomyces. Metabolism and Gene Expression , pp. 181-299
    • Jones, E.W.1    Fink, G.R.2
  • 49
    • 0027194161 scopus 로고
    • Video microscopy of organelle inheritance and motility in budding yeast
    • Jones HD, Schliwa M, Drubin DG. 1993. Video microscopy of organelle inheritance and motility in budding yeast. Cell Motil. Cytoskelet. 25:129-42
    • (1993) Cell Motil. Cytoskelet. , vol.25 , pp. 129-142
    • Jones, H.D.1    Schliwa, M.2    Drubin, D.G.3
  • 50
    • 0035423116 scopus 로고    scopus 로고
    • Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion
    • Kato M, Wickner W. 2001. Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion. EMBO J. 20:4035-40
    • (2001) EMBO J. , vol.20 , pp. 4035-4040
    • Kato, M.1    Wickner, W.2
  • 52
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky DJ, Herman PK, Emr SD. 1990. The fungal vacuole: composition, function, and biogenesis. Microbiol. Rev. 54:266-92
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 53
    • 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, et al. 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. 21:109-25
    • (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
  • 54
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • Lang T, Bruns D, Wenzel D, Riedel D, Holroyd P, et al. 2001. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J. 20:2202-13
    • (2001) EMBO J. , vol.20 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3    Riedel, D.4    Holroyd, P.5
  • 56
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie SH, Brown SS. 1994. Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J. Cell Biol. 125:825-42
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.H.1    Brown, S.S.2
  • 57
    • 0037022847 scopus 로고    scopus 로고
    • Golgi complex: Biogenesis de novo?
    • Lowe M. 2002. Golgi complex: biogenesis de novo? Curr. Biol. 12:R166-67
    • (2002) Curr. Biol. , vol.12
    • Lowe, M.1
  • 58
    • 0033607548 scopus 로고    scopus 로고
    • Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases
    • McEwen RK, Dove SK, Cooke FT, Painter GF, Holmes AB, et al. 1999. Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases. J. Biol. Chem. 274:33905-12
    • (1999) J. Biol. Chem. , vol.274 , pp. 33905-33912
    • McEwen, R.K.1    Dove, S.K.2    Cooke, F.T.3    Painter, G.F.4    Holmes, A.B.5
  • 59
    • 0023371690 scopus 로고
    • Maturation of vacuolar (lysosomal) enzymes in yeast: Proteinase yscA and proteinase yscB are catalysts of the processing and activation event of carboxypeptidase yscY
    • Mechler B, Muller H, Wolf DH. 1987. Maturation of vacuolar (lysosomal) enzymes in yeast: proteinase yscA and proteinase yscB are catalysts of the processing and activation event of carboxypeptidase yscY. EMBO J. 6:2157-63
    • (1987) EMBO J. , vol.6 , pp. 2157-2163
    • Mechler, B.1    Muller, H.2    Wolf, D.H.3
  • 60
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian KA, Ostermeyer AG, Chen JZ, Roth MG, Brown DA. 1999. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274:3910-17
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 61
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima K, Torii S, Yi Z, Igarashi M, Okamoto K, et al. 2002. Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 517:233-38
    • (2002) FEBS Lett. , vol.517 , pp. 233-238
    • Nagashima, K.1    Torii, S.2    Yi, Z.3    Igarashi, M.4    Okamoto, K.5
  • 62
    • 0029086961 scopus 로고
    • A truncated form of the Pho80 cyclin redirects the Pho85 kinase to disrupt vacuole inheritance in S. cerevisiae
    • Nicolson TA, Weisman LS, Payne G, Wickner WT. 1995. A truncated form of the Pho80 cyclin redirects the Pho85 kinase to disrupt vacuole inheritance in S. cerevisiae. J. Cell Biol. 130:835-45
    • (1995) J. Cell Biol. , vol.130 , pp. 835-845
    • Nicolson, T.A.1    Weisman, L.S.2    Payne, G.3    Wickner, W.T.4
  • 63
    • 0030040689 scopus 로고    scopus 로고
    • Regulation of organelle biogenesis
    • Nunnari J, Walter P. 1996. Regulation of organelle biogenesis. Cell 84:389-94
    • (1996) Cell , vol.84 , pp. 389-394
    • Nunnari, J.1    Walter, P.2
  • 64
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • Odorizzi G, Babst M, Emr SD. 1998. Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 95:847-58
    • (1998) Cell , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 65
    • 0037054540 scopus 로고    scopus 로고
    • Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast
    • Ortiz D, Medkova M, Walch-Solimena C, Novick P. 2002. Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J. Cell Biol. 157:1005-15
    • (2002) J. Cell Biol. , vol.157 , pp. 1005-1015
    • Ortiz, D.1    Medkova, M.2    Walch-Solimena, C.3    Novick, P.4
  • 66
    • 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. 1998. YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance. J. Cell Sci. 111:2137-47
    • (1998) J. Cell Sci. , vol.111 , pp. 2137-2147
    • Pan, X.1    Goldfarb, D.S.2
  • 67
    • 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, et al. 2000. Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p. Mol. Biol. Cell 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
  • 68
    • 0033545389 scopus 로고    scopus 로고
    • Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/ fusion at the endosome
    • Peterson MR, Burd CG, Emr SD. 1999. Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/ fusion at the endosome. Curr. Biol. 9: 159-62
    • (1999) Curr. Biol. , vol.9 , pp. 159-162
    • Peterson, M.R.1    Burd, C.G.2    Emr, S.D.3
  • 69
    • 0034943323 scopus 로고    scopus 로고
    • The class C Vps complex functions at multiple stages of the vacuolar transport pathway
    • Peterson MR, Emr SD. 2001. The class C Vps complex functions at multiple stages of the vacuolar transport pathway. Traffic 2:476-86
    • (2001) Traffic , vol.2 , pp. 476-486
    • Peterson, M.R.1    Emr, S.D.2
  • 70
    • 0034618102 scopus 로고    scopus 로고
    • Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae
    • Prinz WA, Grzyb L, Veenhuis M, Kahana JA, Silver PA, Rapoport TA. 2000. Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Biol. 150:461-74
    • (2000) J. Cell Biol. , vol.150 , pp. 461-474
    • Prinz, W.A.1    Grzyb, L.2    Veenhuis, M.3    Kahana, J.A.4    Silver, P.A.5    Rapoport, T.A.6
  • 71
    • 0036107354 scopus 로고    scopus 로고
    • Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes
    • Provance DW, James TL, Mercer JA. 2002. Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes. Traffic 3:124-32
    • (2002) Traffic , vol.3 , pp. 124-132
    • Provance, D.W.1    James, T.L.2    Mercer, J.A.3
  • 73
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class e vps mutants
    • Raymond CK, Howald-Stevenson I, Vater CA, Stevens TH. 1992. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell. 3:1389-402
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald-Stevenson, I.2    Vater, C.A.3    Stevens, T.H.4
  • 74
    • 0024997814 scopus 로고
    • Molecular analysis of the yeast VPS 3 gene and the role of its product in vacuolar protein sorting and vacuolar segregation during the cell cycle
    • Raymond CK, O'Hara PJ, Eichinger G, Rothman JH, Stevens TH. 1990. Molecular analysis of the yeast VPS 3 gene and the role of its product in vacuolar protein sorting and vacuolar segregation during the cell cycle. J. Cell Biol. 111:877-92
    • (1990) J. Cell Biol. , vol.111 , pp. 877-892
    • Raymond, C.K.1    O'Hara, P.J.2    Eichinger, G.3    Rothman, J.H.4    Stevens, T.H.5
  • 77
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • Reggiori F, Pelham HR. 2002. A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nat. Cell Biol. 4:117-23
    • (2002) Nat. Cell Biol. , vol.4 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 78
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451:1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 80
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson JS, Klionsky DJ, Banta LM, Emr SD. 1988. Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol. Cell Biol. 8:4936-48
    • (1988) Mol. Cell Biol. , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 81
    • 0035795423 scopus 로고    scopus 로고
    • A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae
    • Rossanese OW, Reinke CA, Bevis BJ, Hammond AT, Sears IB, et al. 2001. A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi elements in Saccharomyces cerevisiae. J. Cell Biol. 153:47-62
    • (2001) J. Cell Biol. , vol.153 , pp. 47-62
    • Rossanese, O.W.1    Reinke, C.A.2    Bevis, B.J.3    Hammond, A.T.4    Sears, I.B.5
  • 82
    • 0024445121 scopus 로고
    • Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae
    • Rothman JH, Howald I, Stevens TH. 1989. Characterization of genes required for protein sorting and vacuolar function in the yeast Saccharomyces cerevisiae. EMBO J. 8:2057-65
    • (1989) EMBO J. , vol.8 , pp. 2057-2065
    • Rothman, J.H.1    Howald, I.2    Stevens, T.H.3
  • 83
    • 0022898326 scopus 로고
    • Protein sorting in yeast: Mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • Rothman JH, Stevens TH. 1986. Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell 47:1041-51
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.H.1    Stevens, T.H.2
  • 84
    • 0037155216 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve endomembrane localization
    • Sbrissa D, Ikonomov OC, Shisheva A. 2002. Phosphatidylinositol 3-phosphate-interacting domains in PIKfyve. Binding specificity and role in PIKfyve endomembrane localization. J. Biol. Chem. 277:6073-79
    • (2002) J. Biol. Chem. , vol.277 , pp. 6073-6079
    • Sbrissa, D.1    Ikonomov, O.C.2    Shisheva, A.3
  • 85
    • 0033571411 scopus 로고    scopus 로고
    • The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting
    • Schott D, Ho J, Pruyne D, Bretscher A. 1999. The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting. J. Cell Biol. 147:791-808
    • (1999) J. Cell Biol. , vol.147 , pp. 791-808
    • Schott, D.1    Ho, J.2    Pruyne, D.3    Bretscher, A.4
  • 86
    • 0037033787 scopus 로고    scopus 로고
    • Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length
    • Schott DH, Collins RN, Bretscher A. 2002. Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length. J. Cell Biol. 156:35-39
    • (2002) J. Cell Biol. , vol.156 , pp. 35-39
    • Schott, D.H.1    Collins, R.N.2    Bretscher, A.3
  • 87
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, Emr SD. 1993. Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260:88-91
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 88
    • 0034682772 scopus 로고    scopus 로고
    • Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting
    • Scott SV, Nice DC, 3rd, Nau JJ, Weisman LS, Kamada Y, et al. 2000. Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting. J. Biol. Chem. 275:25840-49
    • (2000) J. Biol. Chem. , vol.275 , pp. 25840-25849
    • Scott, S.V.1    Nice III, D.C.2    Nau, J.J.3    Weisman, L.S.4    Kamada, Y.5
  • 90
    • 0025806504 scopus 로고
    • vac2: A yeast mutant which distinguishes vacuole segregation from Golgi-to-vacuole protein targeting
    • Shaw JM, Wickner W. 1991. vac2: a yeast mutant which distinguishes vacuole segregation from Golgi-to-vacuole protein targeting. EMBO J. 10:1741-48
    • (1991) EMBO J. , vol.10 , pp. 1741-1748
    • Shaw, J.M.1    Wickner, W.2
  • 92
    • 0345646448 scopus 로고    scopus 로고
    • Synaptojanin family members are implicated in endocytic membrane traffic in yeast
    • Singer-Kruger B, Nemoto Y, Daniell L, Ferro-Novick S, De Camilli P. 1998. Synaptojanin family members are implicated in endocytic membrane traffic in yeast. J. Cell Sci. 111 (Part 22):3347-56
    • (1998) J. Cell Sci. , vol.111 , Issue.22 PART , pp. 3347-3356
    • Singer-Kruger, B.1    Nemoto, Y.2    Ferro-Novick S, D.L.3    De Camilli, P.4
  • 93
    • 0028847351 scopus 로고
    • Yeast Ypt51p and mammalian Rab5: Counterparts with similar function in the early endocytic pathway
    • Singer-Kruger B, Stenmark H, Zerial M. 1995. Yeast Ypt51p and mammalian Rab5: counterparts with similar function in the early endocytic pathway. J. Cell Sci. 108 (Part 11):3509-21
    • (1995) J. Cell Sci. , vol.108 , Issue.11 PART , pp. 3509-3521
    • Singer-Kruger, B.1    Stenmark, H.2    Zerial, M.3
  • 95
    • 0031742022 scopus 로고    scopus 로고
    • Comprehensive identification of cell cycle-regulated genes of the yeast Saccharomyces cerevisiae by microarray hybridization
    • Spellman PT, Sherlock G, Zhang MQ, Iyer VR, Anders K, et al. 1998. Comprehensive identification of cell cycle-regulated genes of the yeast Saccharomyces cerevisiae by microarray hybridization. Mol. Biol. Cell 9:3273-97
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3273-3297
    • Spellman, P.T.1    Sherlock, G.2    Zhang, M.Q.3    Iyer, V.R.4    Anders, K.5
  • 96
    • 0030686464 scopus 로고    scopus 로고
    • Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape, and osmohomeostasis
    • Srinivasan S, Seaman M, Nemoto Y, Daniell L, Suchy SF, et al. 1997. Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape, and osmohomeostasis. Eur. J. Cell Biol. 74:350-60
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 350-360
    • Srinivasan, S.1    Seaman, M.2    Nemoto, Y.3    Daniell, L.4    Suchy, S.F.5
  • 97
    • 0033832983 scopus 로고    scopus 로고
    • Pep3p/Pep5p complex: A putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae
    • Srivastava A, Woolford CA, Jones EW. 2000. Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Genetics 156:105-22
    • (2000) Genetics , vol.156 , pp. 105-122
    • Srivastava, A.1    Woolford, C.A.2    Jones, E.W.3
  • 98
    • 0027256130 scopus 로고
    • A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
    • Stack JH, Herman PK, Schu PV, Emr SD. 1993. A membrane-associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J. 12:2195-204
    • (1993) EMBO J. , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 99
    • 0037138361 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate-binding FYVE finger
    • Stenmark H, Aasland R, Driscoll PC. 2002. The phosphatidylinositol 3-phosphate-binding FYVE finger. FEBS Lett. 513:77-84
    • (2002) FEBS Lett. , vol.513 , pp. 77-84
    • Stenmark, H.1    Aasland, R.2    Driscoll, P.C.3
  • 100
    • 0032496156 scopus 로고    scopus 로고
    • INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype
    • Stolz LE, Kuo WJ, Longchamps J, Sekhon MK, York JD. 1998. INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype. J. Biol. Chem. 273:11852-61
    • (1998) J. Biol. Chem. , vol.273 , pp. 11852-11861
    • Stolz, L.E.1    Kuo, W.J.2    Longchamps, J.3    Sekhon, M.K.4    York, J.D.5
  • 101
    • 0037067673 scopus 로고    scopus 로고
    • A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport
    • Strom M, Hume AN, Tarafder AK, Barkagianni E, Seabra MC. 2002. A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. J. Biol. Chem. 277:25423-30
    • (2002) J. Biol. Chem. , vol.277 , pp. 25423-25430
    • Strom, M.1    Hume, A.N.2    Tarafder, A.K.3    Barkagianni, E.4    Seabra, M.C.5
  • 102
    • 0346191767 scopus 로고
    • Ultraviolet microscopy of purine compounds in the yeast vacuole
    • Svihla G, Dainko JL, Schlenk F. 1963. Ultraviolet microscopy of purine compounds in the yeast vacuole. J. Bacteriol. 85:399-409
    • (1963) J. Bacteriol. , vol.85 , pp. 399-409
    • Svihla, G.1    Dainko, J.L.2    Schlenk, F.3
  • 103
    • 0032978370 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Seclp homologue to facilitate vesicle-mediated vacuolar protein sorting
    • Tall GG, Kama H, DeWald DB, Horazdovsky BF. 1999. The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Seclp homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol. Biol. Cell 10:1873-89
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1873-1889
    • Tall, G.G.1    Kama, H.2    Dewald, D.B.3    Horazdovsky, B.F.4
  • 104
    • 0037422115 scopus 로고    scopus 로고
    • Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole
    • Tang F, Kauffman EJ, Novak JL, Nau JJ, Catlett NL, Weisman LS. 2003. Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole. Nature 422:87-92
    • (2003) Nature , vol.422 , pp. 87-92
    • Tang, F.1    Kauffman, E.J.2    Novak, J.L.3    Nau, J.J.4    Catlett, N.L.5    Weisman, L.S.6
  • 105
    • 0024259217 scopus 로고
    • +-ATPase and enzymological discrimination of three ATP-driven proton pumps in Saccharomyces cerevisiae
    • +-ATPase and enzymological discrimination of three ATP-driven proton pumps in Saccharomyces cerevisiae. Methods Enzymol. 157:544-63
    • (1988) Methods Enzymol. , vol.157 , pp. 544-563
    • Uchida, E.1    Ohsumi, Y.2    Anraku, Y.3
  • 106
    • 0034852403 scopus 로고    scopus 로고
    • Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
    • Urbanowski JL, Piper RC. 2001. Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole. Traffic 2:622-30
    • (2001) Traffic , vol.2 , pp. 622-630
    • Urbanowski, J.L.1    Piper, R.C.2
  • 107
    • 0029692438 scopus 로고    scopus 로고
    • Review: Biosynthesis and function of yeast vacuolar proteases
    • Van Den Hazel HB, Kielland-Brandt MC, Winther JR. 1996. Review: biosynthesis and function of yeast vacuolar proteases. Yeast 12:1-16
    • (1996) Yeast , vol.12 , pp. 1-16
    • Van Den Hazel, H.B.1    Kielland-Brandt, M.C.2    Winther, J.R.3
  • 108
    • 0035876373 scopus 로고    scopus 로고
    • Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion
    • Veit M, Laage R, Dietrich L, Wang L, Ungermann C. 2001. Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO J. 20:3145-55
    • (2001) EMBO J. , vol.20 , pp. 3145-3155
    • Veit, M.1    Laage, R.2    Dietrich, L.3    Wang, L.4    Ungermann, C.5
  • 109
    • 0036827960 scopus 로고    scopus 로고
    • Role of cholesterol in human immunodeficiency virus type 1 envelope protein-mediated fusion with host cells
    • Viard M, Parolini I, Sargiacomo M, Fecchi K, Ramoni C, et al. 2002. Role of cholesterol in human immunodeficiency virus type 1 envelope protein-mediated fusion with host cells. J. Virol. 76:11584-95
    • (2002) J. Virol. , vol.76 , pp. 11584-11595
    • Viard, M.1    Parolini, I.2    Sargiacomo, M.3    Fecchi, K.4    Ramoni, C.5
  • 110
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida TA, Emr SD. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell. Biol. 128:779-92
    • (1995) J. Cell. Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 111
    • 0026668576 scopus 로고
    • Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. II. VAM7, a gene for regulating morphogenic assembly of the vacuoles
    • Wada Y, Anraku Y. 1992. Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. II. VAM7, a gene for regulating morphogenic assembly of the vacuoles. J. Biol. Chem. 267:18671-75
    • (1992) J. Biol. Chem. , vol.267 , pp. 18671-18675
    • Wada, Y.1    Anraku, Y.2
  • 112
    • 0036180245 scopus 로고    scopus 로고
    • Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle
    • Wang L, Seeley ES, Wickner W, Merz AJ. 2002. Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle. Cell 108:357-69
    • (2002) Cell , vol.108 , pp. 357-369
    • Wang, L.1    Seeley, E.S.2    Wickner, W.3    Merz, A.J.4
  • 113
    • 0029812691 scopus 로고    scopus 로고
    • Multiple classes of yeast mutants are defective in vacuole partitioning yet target vacuole proteins correctly
    • Wang Y-X, Zhao H, Harding T, Gomes de Mesquita D, Woldringh CL, et al. 1996. Multiple classes of yeast mutants are defective in vacuole partitioning yet target vacuole proteins correctly. Mol. Biol. Cell 7:1375-89
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1375-1389
    • Wang, Y.-X.1    Zhao, H.2    Harding, T.3    Gomes De Mesquita, D.4    Woldringh, C.L.5
  • 114
    • 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. 1998. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J. Cell Biol. 140:1063-74
    • (1998) J. Cell Biol. , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 115
    • 0035860689 scopus 로고    scopus 로고
    • Fusion of docked membranes requires the armadillo repeat protein Vac8p
    • Wang YX, Kauffman EJ, Duex JE, Weisman LS. 2001. Fusion of docked membranes requires the armadillo repeat protein Vac8p. J. Biol. Chem. 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
  • 116
    • 0030040690 scopus 로고    scopus 로고
    • Organelle inheritance
    • Warren G, Wickner W. 1996. Organelle inheritance. Cell 84:395-400
    • (1996) Cell , vol.84 , pp. 395-400
    • Warren, G.1    Wickner, W.2
  • 117
    • 0030774801 scopus 로고    scopus 로고
    • Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: Evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome
    • Webb GC, Hoedt M, Poole LJ, Jones EW. 1997. Genetic interactions between a pep7 mutation and the PEP12 and VPS45 genes: evidence for a novel SNARE component in transport between the Saccharomyces cerevisiae Golgi complex and endosome. Genetics 147:467-78
    • (1997) Genetics , vol.147 , pp. 467-478
    • Webb, G.C.1    Hoedt, M.2    Poole, L.J.3    Jones, E.W.4
  • 118
    • 0030918921 scopus 로고    scopus 로고
    • Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome
    • Webb GC, Zhang J, Garlow SJ, Wesp A, Riezman H, Jones EW. 1997. Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome. Mol. Biol. Cell 8:871-95
    • (1997) Mol. Biol. Cell , vol.8 , pp. 871-895
    • Webb, G.C.1    Zhang, J.2    Garlow, S.J.3    Wesp, A.4    Riezman, H.5    Jones, E.W.6
  • 119
    • 0023432180 scopus 로고
    • Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle
    • Weisman LS, Bacallao R, Wickner W. 1987. Multiple methods of visualizing the yeast vacuole permit evaluation of its morphology and inheritance during the cell cycle. J. Cell Biol. 105:1539-47
    • (1987) J. Cell Biol. , vol.105 , pp. 1539-1547
    • Weisman, L.S.1    Bacallao, R.2    Wickner, W.3
  • 120
    • 0025070007 scopus 로고
    • Mutants of Saccharomyces cerevisiae that block intervacuole vesicular traffic and vacuole division and segregation
    • Weisman LS, Emr SD, Wickner WT. 1990. Mutants of Saccharomyces cerevisiae that block intervacuole vesicular traffic and vacuole division and segregation. Proc. Natl. Acad. Sci. USA 87:1076-80
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1076-1080
    • Weisman, L.S.1    Emr, S.D.2    Wickner, W.T.3
  • 121
    • 0024299493 scopus 로고
    • Intervacuole exchange in the yeast zygote: A new pathway in organelle communication
    • Weisman LS, Wickner W. 1988. Intervacuole exchange in the yeast zygote: a new pathway in organelle communication. Science 241:589-91
    • (1988) Science , vol.241 , pp. 589-591
    • Weisman, L.S.1    Wickner, W.2
  • 122
    • 0026544213 scopus 로고
    • Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting
    • Weisman LS, Wickner W. 1992. Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting. J. Biol. Chem. 267:618-23
    • (1992) J. Biol. Chem. , vol.267 , pp. 618-623
    • Weisman, L.S.1    Wickner, W.2
  • 123
    • 0037009076 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Mob2p-Cbk1p kinase complex promotes polarized growth and acts with the mitotic exit network to facilitate daughter cell-specific localization of Ace2p transcription factor
    • Weiss EL, Kurischko C, Zhang C, Shokat K, Drubin DG, Luca FC. 2002. The Saccharomyces cerevisiae Mob2p-Cbk1p kinase complex promotes polarized growth and acts with the mitotic exit network to facilitate daughter cell-specific localization of Ace2p transcription factor. J. Cell Biol. 158:885-900
    • (2002) J. Cell Biol. , vol.158 , pp. 885-900
    • Weiss, E.L.1    Kurischko, C.2    Zhang, C.3    Shokat, K.4    Drubin, D.G.5    Luca, F.C.6
  • 124
    • 0027269974 scopus 로고
    • SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast
    • Whitters EA, Cleves AE, McGee TP, Skinner HB, Bankaitis VA. 1993. SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast. J. Cell Biol. 122:79-94
    • (1993) J. Cell Biol. , vol.122 , pp. 79-94
    • Whitters, E.A.1    Cleves, A.E.2    McGee, T.P.3    Skinner, H.B.4    Bankaitis, V.A.5
  • 125
    • 0014727710 scopus 로고
    • Vacuolar dynamics in synchronously budding yeast
    • Wiemken A, Matile P, Moor H. 1970. Vacuolar dynamics in synchronously budding yeast. Arch. Mikrobiol. 70:89-103
    • (1970) Arch. Mikrobiol. , vol.70 , pp. 89-103
    • Wiemken, A.1    Matile, P.2    Moor, H.3
  • 126
    • 0035967888 scopus 로고    scopus 로고
    • Phoxy lipids: Revealing PX domains as phosphoinositide binding modules
    • Wishart MJ, Taylor GS, Dixon JE. 2001. Phoxy lipids: revealing PX domains as phosphoinositide binding modules. Cell 105:817-20
    • (2001) Cell , vol.105 , pp. 817-820
    • Wishart, M.J.1    Taylor, G.S.2    Dixon, J.E.3
  • 127
    • 0031932615 scopus 로고    scopus 로고
    • Genetic interaction with vps8-200 allows partial suppression of the vestigial vacuole phenotype caused by a pep5 mutation in Saccharomyces cerevisiae
    • Woolford CA, Bounoutas GS, Frew SE, Jones EW. 1998. Genetic interaction with vps8-200 allows partial suppression of the vestigial vacuole phenotype caused by a pep5 mutation in Saccharomyces cerevisiae. Genetics 148:71-83
    • (1998) Genetics , vol.148 , pp. 71-83
    • Woolford, C.A.1    Bounoutas, G.S.2    Frew, S.E.3    Jones, E.W.4
  • 128
    • 0022755757 scopus 로고
    • The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
    • Woolford CA, Daniels LB, Park FJ, Jones EW, Van Arsdell JN, Innis MA. 1986. The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases. Mol. Cell Biol. 6:2500-10
    • (1986) Mol. Cell Biol. , vol.6 , pp. 2500-2510
    • Woolford, C.A.1    Daniels, L.B.2    Park, F.J.3    Jones, E.W.4    Van Arsdell, J.N.5    Innis, M.A.6
  • 129
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
    • Wu X, Bowers B, Rao K, Wei Q, Hammer JAR. 1998. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function In vivo. J. Cell Biol. 143:1899-918
    • (1998) J. Cell Biol. , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer, J.A.R.5
  • 132
    • 0037135980 scopus 로고    scopus 로고
    • Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy
    • Wurmser AE, Emr SD. 2002. Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 PtdIns 3-kinase in autophagy. J. Cell Biol. 158:761-72
    • (2002) J. Cell Biol. , vol.158 , pp. 761-772
    • Wurmser, A.E.1    Emr, S.D.2
  • 133
    • 0033525615 scopus 로고    scopus 로고
    • The machinery of mitochondrial inheritance and behavior
    • Yaffe MP. 1999. The machinery of mitochondrial inheritance and behavior. Science 283:1493-97
    • (1999) Science , vol.283 , pp. 1493-1497
    • Yaffe, M.P.1
  • 134
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin H, Pruyne D, Huffaker TC, Bretscher A. 2000. Myosin V orientates the mitotic spindle in yeast. Nature 406:1013-15
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4
  • 135
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296:913-16
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 136
    • 0342868306 scopus 로고    scopus 로고
    • Two yeast fork-head genes regulate the cell cycle and pseudohyphal growth
    • Zhu G, Spellman PT, Volpe T, Brown PO, Botstein D, et al. 2000. Two yeast fork-head genes regulate the cell cycle and pseudohyphal growth. Nature 406:90-94
    • (2000) Nature , vol.406 , pp. 90-94
    • Zhu, G.1    Spellman, P.T.2    Volpe, T.3    Brown, P.O.4    Botstein, D.5
  • 137
    • 0020340108 scopus 로고
    • Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae
    • Zubenko GS, Park FJ, Jones EW. 1982. Genetic properties of mutations at the PEP4 locus in Saccharomyces cerevisiae. Genetics 102:679-90
    • (1982) Genetics , vol.102 , pp. 679-690
    • Zubenko, G.S.1    Park, F.J.2    Jones, E.W.3
  • 138
    • 0020696481 scopus 로고
    • Mutations in PEP4 locus of Saccharomyces cerevisiae block final step in maturation of two vacuolar hydrolases
    • Zubenko GS, Park FJ, Jones EW. 1983. Mutations in PEP4 locus of Saccharomyces cerevisiae block final step in maturation of two vacuolar hydrolases. Proc. Natl. Acad. Sci. USA 80:510-14
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 510-514
    • Zubenko, G.S.1    Park, F.J.2    Jones, E.W.3


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