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Volumn 143, Issue 1, 1998, Pages 65-79

Fab1p is essential for PtdIns(3)P 5-kinase activity and the maintenance of vacuolar size and membrane homeostasis

Author keywords

Lipid kinase; PtdIns(3,5)P2; VAC7; Vacuole; VPS34

Indexed keywords

ARTICLE; CELL MEMBRANE; CELL VACUOLE; ENZYME ACTIVITY; GENE SEQUENCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; SACCHAROMYCES CEREVISIAE; SIGNAL TRANSDUCTION;

EID: 0032487577     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.1.65     Document Type: Article
Times cited : (353)

References (88)
  • 2
    • 0024308812 scopus 로고
    • Phosphatidylinositol 3-kinase and its novel product, phosphatidylinositol 3-phosphate, are present in Saccharomyces cerevisiae
    • Auger, K.R., C.L. Carpenter, L.C. Cantley, and L. Varticovski. 1989. Phosphatidylinositol 3-kinase and its novel product, phosphatidylinositol 3-phosphate, are present in Saccharomyces cerevisiae. J. Biol. Chem. 264:20181-20184.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20181-20184
    • Auger, K.R.1    Carpenter, C.L.2    Cantley, L.C.3    Varticovski, L.4
  • 3
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., T.K, Sato, L.M. Banta, and S.D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO (Eur. Mol. Biol. Organ.) J. 16:1820-1831.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 4
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis, V.A., J.R. Aitken, A.E. Cleves, and W. Dowhan. 1990. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature. 347: 561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 5
    • 0024095176 scopus 로고
    • Organelle assembly in yeast: Characterization of yeast mutants defective in vacuolar biogenesis and protein sorting
    • Banta, L.M., J.S. Robinson, D.J. Klionsky, and S.D. Emr. 1988. Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting. J. Cell Biol. 107:1369-1383.
    • (1988) J. Cell Biol. , vol.107 , pp. 1369-1383
    • Banta, L.M.1    Robinson, J.S.2    Klionsky, D.J.3    Emr, S.D.4
  • 6
    • 0028211009 scopus 로고
    • PCR amplification of up to 35-kb DNA with high fidelity and high yield from lambda bacteriophage templates
    • Barnes, W.M. 1994. PCR amplification of up to 35-kb DNA with high fidelity and high yield from lambda bacteriophage templates. Proc. Natl. Acad. Sci. USA. 91:2216-2220.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2216-2220
    • Barnes, W.M.1
  • 7
    • 0030692711 scopus 로고    scopus 로고
    • Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology
    • Bonangelino, C.J., N.L. Catlett, and L.S. Weisman. 1997. Vac7p, a novel vacuolar protein, is required for normal vacuole inheritance and morphology. Mol. Cell Biol. 17:6847-6858.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6847-6858
    • Bonangelino, C.J.1    Catlett, N.L.2    Weisman, L.S.3
  • 8
    • 0028812255 scopus 로고
    • The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases
    • Boronenkov, I.V., and R.A. Anderson. 1995. The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases. J. Biol. Chem. 270:2881-2884.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2881-2884
    • Boronenkov, I.V.1    Anderson, R.A.2
  • 10
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown, W.J., D.B. DeWald, S.D. Emr, H. Plutner, and W.E. Balch. 1995. Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell Biol. 130:781-796.
    • (1995) J. Cell Biol. , vol.130 , pp. 781-796
    • Brown, W.J.1    DeWald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 11
    • 0031854866 scopus 로고    scopus 로고
    • Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment
    • Bryant, N.J., R.C. Piper, L.S. Weisman, and T.H. Stevens. 1998. Retrograde traffic out of the yeast vacuole to the TGN occurs via the prevacuolar/endosomal compartment. J. Cell Biol. 142:651-663.
    • (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
  • 12
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd, C.G., and S.D. Emr. 1998. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell. 2:157-162.
    • (1998) Mol. Cell. , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 13
    • 0030952211 scopus 로고    scopus 로고
    • A novel Sec18p/ NSF-dependent complex required for Golgi-to-endosome transport in yeast
    • Burd, C.G., M. Peterson, C.R. Cowles, and S.D. Emr. 1997. A novel Sec18p/ NSF-dependent complex required for Golgi-to-endosome transport in yeast. Mol. Biol. Cell. 8:1089-1104.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1089-1104
    • Burd, C.G.1    Peterson, M.2    Cowles, C.R.3    Emr, S.D.4
  • 14
    • 0028605474 scopus 로고
    • Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles
    • Cowles, C., S. Emr, and B. Horazdovsky. 1994. Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein sorting defects and accumulation of membrane vesicles. J. Cell Sci. 107:3449-3459.
    • (1994) J. Cell Sci. , vol.107 , pp. 3449-3459
    • Cowles, C.1    Emr, S.2    Horazdovsky, B.3
  • 15
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole
    • Cowles, C.R., G. Odorizzi, G.S. Payne, and S.D. Emr. 1997a. The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell. 91:109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 16
    • 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., W.B. Snyder, C.G. Burd, S.D. Emr, S.E. Rieder, and S.D. Emr. 1997b. Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component. EMBO (Eur. Mol. Biol. Organ.) J. 16:2769-2782.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 2769-2782
    • Cowles, C.R.1    Snyder, W.B.2    Burd, C.G.3    Emr, S.D.4    Rieder, S.E.5    Emr, S.D.6
  • 17
    • 0029123267 scopus 로고
    • Wortmannin causes mistargeting of procathepsin D. evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes
    • Davidson, H.W. 1995. Wortmannin causes mistargeting of procathepsin D. evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes. J. Cell Biol. 130:797-805.
    • (1995) J. Cell Biol. , vol.130 , pp. 797-805
    • Davidson, H.W.1
  • 18
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli, P., S.D. Emr, P.S. McPherson, and P. Novick. 1996. Phosphoinositides as regulators in membrane traffic. Science. 271:1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 19
    • 0032546798 scopus 로고    scopus 로고
    • MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Desrivieres, S., F.T. Cooke, P.J. Parker, and M.N. Hall. 1998. MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae. J. Biol. Chem. 273:15787-15793.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15787-15793
    • Desrivieres, S.1    Cooke, F.T.2    Parker, P.J.3    Hall, M.N.4
  • 21
    • 0027768699 scopus 로고
    • Phosphatidylinositol 4-kinase: Gene structure and requirement for yeast cell viability
    • Flanagan, C.A., E.A. Schnieders, A.W. Emerick, R. Kunisawa, A. Admon, and J. Thorner. 1993. Phosphatidylinositol 4-kinase: gene structure and requirement for yeast cell viability. Science. 262:1444-1448.
    • (1993) Science , vol.262 , pp. 1444-1448
    • Flanagan, C.A.1    Schnieders, E.A.2    Emerick, A.W.3    Kunisawa, R.4    Admon, A.5    Thorner, J.6
  • 22
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor, E.C., S. te Heesen, T.R. Graham, M. Aebi, and S.D. Emr. 1994. Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J. Cell Biol. 127:653-665.
    • (1994) J. Cell Biol. , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Te Heesen, S.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 23
    • 0032568629 scopus 로고    scopus 로고
    • Kinetic analyses of mutations in the glycine-rich loop of cAMP-dependent protein kinase
    • Grant, B.D., W. Hemmer, I. Tsigelny, J.A. Adams, and S.S. Taylor. 1998. Kinetic analyses of mutations in the glycine-rich loop of cAMP-dependent protein kinase. Biochemistry. 37:7708-7715.
    • (1998) Biochemistry , vol.37 , pp. 7708-7715
    • Grant, B.D.1    Hemmer, W.2    Tsigelny, I.3    Adams, J.A.4    Taylor, S.S.5
  • 24
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg, J., and F.R. Maxfield. 1995. Membrane transport in the endocytic pathway. Curr. Opin. Cell Biol. 7:552-563.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.R.2
  • 26
    • 0027765507 scopus 로고
    • Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion
    • Hay, J.C., and T.F. Martin. 1993. Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion. Nature. 366:572-575.
    • (1993) Nature , vol.366 , pp. 572-575
    • Hay, J.C.1    Martin, T.F.2
  • 27
    • 0030859238 scopus 로고    scopus 로고
    • Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase
    • Hemmer, W., M. McGlone, I. Tsigelny, and S.S. Taylor. 1997. Role of the glycine triad in the ATP-binding site of cAMP-dependent protein kinase. J. Biol. Chem. 272:16946-16954.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16946-16954
    • Hemmer, W.1    McGlone, M.2    Tsigelny, I.3    Taylor, S.S.4
  • 28
    • 0025200830 scopus 로고
    • Characterization of VPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae
    • Herman, P.K., and S.D. Emr. 1990. Characterization of VPS34, a gene required for vacuolar protein sorting and vacuole segregation in Saccharomyces cerevisiae. Mol. Cell Biol. 10:6742-6754.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 6742-6754
    • Herman, P.K.1    Emr, S.D.2
  • 29
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman, C.S., and F. Winston. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene. 57:267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 30
    • 0032546932 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis
    • Homma, K., S. Terui, M. Minemura, H. Qadota, Y. Anraku, Y. Kanaho, and Y. Ohya. 1998. Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis. J. Biol. Chem. 273:15779-15786.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15779-15786
    • Homma, K.1    Terui, S.2    Minemura, M.3    Qadota, H.4    Anraku, Y.5    Kanaho, Y.6    Ohya, Y.7
  • 32
    • 0026537450 scopus 로고
    • Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors
    • Hu, P., B. Margolis, E.Y. Skolnik, R. Lammers, A. Ullrich, and J. Schlessinger. 1992. Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors. Mol. Cell Biol. 12:981-990.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 981-990
    • Hu, P.1    Margolis, B.2    Skolnik, E.Y.3    Lammers, R.4    Ullrich, A.5    Schlessinger, J.6
  • 33
    • 0032546013 scopus 로고    scopus 로고
    • Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma
    • Huang, C.L., S. Feng, and D.W. Hilgemann. 1998. Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma. Nature. 391:803-806.
    • (1998) Nature , vol.391 , pp. 803-806
    • Huang, C.L.1    Feng, S.2    Hilgemann, D.W.3
  • 34
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 35
    • 14444285079 scopus 로고
    • Internalization of activated platelet-derived growth factor receptor-phosphatidylinositol-3′ kinase complexes: Potential interactions with the microtubule cytoskeleton
    • Kapeller, R., R. Chakrabarti, E. Cantley, F. Fay, and S. Corvera. 1994. Internalization of activated platelet-derived growth factor receptor-phosphatidylinositol-3′ kinase complexes: potential interactions with the microtubule cytoskeleton. J. Biol. Chem. 269:6052-6063.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6052-6063
    • Kapeller, R.1    Chakrabarti, R.2    Cantley, E.3    Fay, F.4    Corvera, S.5
  • 36
    • 0032404324 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins: The long and winding road to physiological function
    • Kearns, B.G., J.G. Alb, Jr., and V.A. Bankaitis. 1998. Phosphatidylinositol transfer proteins: the long and winding road to physiological function. Trends Cell Biol. 8:276-281.
    • (1998) Trends Cell Biol. , vol.8 , pp. 276-281
    • Kearns, B.G.1    Alb Jr., J.G.2    Bankaitis, V.A.3
  • 37
    • 0026640551 scopus 로고
    • Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
    • Klionsky, D.J., R. Cueva, and D.S. Yaver. 1992. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway. J. Cell Biol. 119:287-299.
    • (1992) J. Cell Biol. , vol.119 , pp. 287-299
    • Klionsky, D.J.1    Cueva, R.2    Yaver, D.S.3
  • 38
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Klionsky, D.J., and S.D. Emr. 1989. Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO (Eur. Mol. Biol. Organ.) J. 8:2241-2250.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 2241-2250
    • Klionsky, D.J.1    Emr, S.D.2
  • 39
    • 0025170681 scopus 로고
    • The fungal vacuole: Composition, function, and biogenesis
    • Klionsky, D.J., P.K. Herman, and S.D. Emr. 1990. The fungal vacuole: composition, function, and biogenesis. Microbiol. Rev. 54:266-292.
    • (1990) Microbiol. Rev. , vol.54 , pp. 266-292
    • Klionsky, D.J.1    Herman, P.K.2    Emr, S.D.3
  • 41
    • 0027311858 scopus 로고
    • Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression
    • Kunz, J., R. Henriquez, U. Schneider, M. Deuter-Reinhard, N.R. Movva, and M.N. Hall. 1993. Target of rapamycin in yeast, TOR2, is an essential phosphatidylinositol kinase homolog required for G1 progression. Cell. 73:585-596.
    • (1993) Cell , vol.73 , pp. 585-596
    • Kunz, J.1    Henriquez, R.2    Schneider, U.3    Deuter-Reinhard, M.4    Movva, N.R.5    Hall, M.N.6
  • 42
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M., and L.C. Cantley. 1995. Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell. 81:659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 43
    • 16944365378 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family
    • Loijens, J.C., and R.A. Anderson. 1996. Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family. J. Biol. Chem. 271:32937-32943.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32937-32943
    • Loijens, J.C.1    Anderson, R.A.2
  • 45
    • 0030838702 scopus 로고    scopus 로고
    • Phosphoinositides as spatial regulators of membrane traffic
    • Martin, T.F. 1997. Phosphoinositides as spatial regulators of membrane traffic. Curr. Opin. Neurobiol. 7:331-338.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 331-338
    • Martin, T.F.1
  • 46
    • 2642622186 scopus 로고    scopus 로고
    • A presynaptic inositol-5-phosphatase p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson, P.S., E.P. Garcia, V.I. Slepnev, C. David, X. Zhang, D. Grabs, W.S. Sossin, R. Bauerfeind, Y. Nemoto, P. De Camilli, et al. 1996. A presynaptic inositol-5-phosphatase p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. Nature. 379:353-357.
    • (1996) Nature , vol.379 , pp. 353-357
    • McPherson, P.S.1    Garcia, E.P.2    Slepnev, V.I.3    David, C.4    Zhang, X.5    Grabs, D.6    Sossin, W.S.7    Bauerfeind, R.8    Nemoto, Y.9    De Camilli, P.10
  • 47
    • 0028073746 scopus 로고
    • p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation
    • McPherson, P.S., K. Takei, S.L. Schmid, and P. De Camilli. 1994. p145, a major Grb2-binding protein in brain, is co-localized with dynamin in nerve terminals where it undergoes activity-dependent dephosphorylation. J. Biol. Chem. 269:30132-30139.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30132-30139
    • McPherson, P.S.1    Takei, K.2    Schmid, S.L.3    De Camilli, P.4
  • 48
    • 0024273702 scopus 로고
    • Mutational analysis of a phosphotransfer motif essential for v-fps tyrosine kinase activity
    • Moran, M.F., C.A. Koch, I. Sadowski, and T. Pawson. 1988. Mutational analysis of a phosphotransfer motif essential for v-fps tyrosine kinase activity. Oncogene. 3:665-672.
    • (1988) Oncogene , vol.3 , pp. 665-672
    • Moran, M.F.1    Koch, C.A.2    Sadowski, I.3    Pawson, T.4
  • 49
    • 0028035426 scopus 로고
    • Differential effects of compartment deacidification on the targeting of membrane and soluble proteins to the vacuole in yeast
    • Morano, K.A., and D.J. Klionsky. 1994. Differential effects of compartment deacidification on the targeting of membrane and soluble proteins to the vacuole in yeast. J. Cell Sci. 107:2813-2824.
    • (1994) J. Cell Sci. , vol.107 , pp. 2813-2824
    • Morano, K.A.1    Klionsky, D.J.2
  • 50
    • 0026501752 scopus 로고
    • A rapid method for localized mutagenesis of yeast genes
    • Muhlrad, D., R. Hunter, and R. Parker. 1992. A rapid method for localized mutagenesis of yeast genes. Yeast. 8:79-82.
    • (1992) Yeast , vol.8 , pp. 79-82
    • Muhlrad, D.1    Hunter, R.2    Parker, R.3
  • 51
    • 0027997975 scopus 로고
    • Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: Identification of six new END genes
    • Munn, A.L., and H. Riezman. 1994. Endocytosis is required for the growth of vacuolar H(+)-ATPase-defective yeast: identification of six new END genes. J. Cell Biol. 127:373-386.
    • (1994) J. Cell Biol. , vol.127 , pp. 373-386
    • Munn, A.L.1    Riezman, H.2
  • 52
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P., and M. Zerial. 1997. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9:496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 54
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G. 1975. Intracellular aspects of the process of protein synthesis. Science. 189:347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 56
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper, R.C., A.A. Cooper, H. Yang, and T.H. Stevens. 1995. VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J. Cell Biol. 131:603-617.
    • (1995) J. Cell Biol. , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 57
    • 0030852699 scopus 로고    scopus 로고
    • The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway
    • Piper, R.C., N.J. Bryant, and T.H. Stevens. 1997. The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. J. Cell Biol. 138:531-545.
    • (1997) J. Cell Biol. , vol.138 , pp. 531-545
    • Piper, R.C.1    Bryant, N.J.2    Stevens, T.H.3
  • 58
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh, L.E., K.F. Tolias, B.C. Duckworth, and L.C. Cantley. 1997. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature. 390: 192-196.
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 59
    • 14444281433 scopus 로고    scopus 로고
    • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
    • Redding, K., C. Holcomb, and R.S. Fuller. 1997. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell. 8:527-538.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 527-538
    • Redding, K.1    Holcomb, C.2    Fuller, R.S.3
  • 60
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant
    • Rieder, S.E., L.M. Banta, K. Kohrer, J.M. McCaffery, and S.D. Emr. 1996. Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant. Mol. Biol. Cell. 7:985-999.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 985-999
    • Rieder, S.E.1    Banta, L.M.2    Kohrer, K.3    McCaffery, J.M.4    Emr, S.D.5
  • 61
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., D.J. Klionsky, L.M. Banta, and S.D. Emr. 1988. Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol. Cell Biol. 8:4936-4948.
    • (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
  • 62
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. 1994. Mechanisms of intracellular protein transport. Nature. 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 63
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science. 271:1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 64
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S.L. 1997. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu. Rev. Biochem. 66:511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 65
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu, P.V., K. Takegawa, M.J. Fry, J.H. Stack, M.D. Waterfield, and S.D. Emr. 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
  • 66
    • 0030852279 scopus 로고    scopus 로고
    • Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism
    • Scott, S.V., M. Baba, Y. Ohsumi, and D.J. Klionsky. 1997. Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism. J. Cell Biol. 138:37-44.
    • (1997) J. Cell Biol. , vol.138 , pp. 37-44
    • Scott, S.V.1    Baba, M.2    Ohsumi, Y.3    Klionsky, D.J.4
  • 67
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., I. Moarefi, and J. Kuriyan. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature. 385:602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 68
    • 0028140347 scopus 로고
    • pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro
    • Sorensen, S.O., H.B. Van Den Hazel, M.C. Kielland-Brandt, and J.R. Winther. 1994. pH-dependent processing of yeast procarboxypeptidase Y by proteinase A in vivo and in vitro. Eur. J. Biochem. 220:19-27.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 19-27
    • Sorensen, S.O.1    Van Den Hazel, H.B.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 69
    • 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., M. Seaman, Y. Nemoto, L. Daniell, S.F. Suchy, S. Emr, P. De Camilli, and R. Nussbaum. 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. 74:350-360.
    • (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    Emr, S.6    De Camilli, P.7    Nussbaum, R.8
  • 70
    • 0028964232 scopus 로고
    • Vesicle-mediated protein transport: Regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast
    • Stack, J.H., D.B. DeWald, K. Takegawa, and S.D. Emr. 1995. Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast. J. Cell Biol. 129:321-334.
    • (1995) J. Cell Biol. , vol.129 , pp. 321-334
    • Stack, J.H.1    DeWald, D.B.2    Takegawa, K.3    Emr, S.D.4
  • 71
    • 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, J.H., P.K. Herman, P.V. Schu, and S.D. Emr. 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 (Eur. Mol. Biol. Organ.) J. 12:2195-2204.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2195-2204
    • Stack, J.H.1    Herman, P.K.2    Schu, P.V.3    Emr, S.D.4
  • 72
    • 0029618201 scopus 로고
    • Receptor-mediated protein sorting to the vacuole in yeast: Roles for a protein kinase, a lipid kinase and GTP-binding proteins
    • Stack, J.H., B. Horazdovsky, and S.D. Emr. 1995. Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding proteins. Annu. Rev. Cell Dev. Biol. 11:1-33.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 1-33
    • Stack, J.H.1    Horazdovsky, B.2    Emr, S.D.3
  • 74
    • 0031893414 scopus 로고    scopus 로고
    • Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae
    • Stolz, L.E., C.V. Huynh, J. Thorner, and J.D. York. 1998. Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae. Genetics. 148:1715-1729.
    • (1998) Genetics , vol.148 , pp. 1715-1729
    • Stolz, L.E.1    Huynh, C.V.2    Thorner, J.3    York, J.D.4
  • 77
    • 0025192609 scopus 로고
    • The dominant W42 spotting phenotype results from a missense mutation in the c-kit receptor kinase
    • Tan, J.C., K. Nocka, P. Ray, P. Traktman, and P. Besmer. 1990. The dominant W42 spotting phenotype results from a missense mutation in the c-kit receptor kinase. Science. 247:209-212.
    • (1990) Science , vol.247 , pp. 209-212
    • Tan, J.C.1    Nocka, K.2    Ray, P.3    Traktman, P.4    Besmer, P.5
  • 78
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A., and L.C. Cantley. 1997. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 79
    • 0029692438 scopus 로고    scopus 로고
    • Review: Biosynthesis and function of yeast vacuolar proteases
    • Van Den Hazel, H.B., M.C. Kielland-Brandt, and J.R. Winther. 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
  • 80
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and S.D. Emr. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128:779-792.
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 81
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to the vacuole
    • Wang, Y.-U., N.L. Catlett, and L.S. Weisman. 1998. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to the vacuole. J. Cell Biol. 140:1063-1074.
    • (1998) J. Cell Biol. , vol.140 , pp. 1063-1074
    • Wang, Y.-U.1    Catlett, N.L.2    Weisman, L.S.3
  • 83
    • 0026544213 scopus 로고
    • Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting
    • Weisman, L.S., and W. Wickner. 1992. Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting. J. Biol. Chem. 267:618-623.
    • (1992) J. Biol. Chem. , vol.267 , pp. 618-623
    • Weisman, L.S.1    Wickner, W.2
  • 84
    • 0030944761 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,5-bisphosphate defines a novel PI 3-kinase pathway in resting mouse fibroblasts
    • Whiteford, C.C., C.A. Brearley, and E.T. Ulug. 1997. Phosphatidylinositol 3,5-bisphosphate defines a novel PI 3-kinase pathway in resting mouse fibroblasts. Biochem. J. 323:597-601.
    • (1997) Biochem. J. , vol.323 , pp. 597-601
    • Whiteford, C.C.1    Brearley, C.A.2    Ulug, E.T.3
  • 85
    • 0032168684 scopus 로고    scopus 로고
    • Phosphoinositide signaling and turnover: PtdIns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities
    • Wurmser, A., and S.D. Emr. 1998. Phosphoinositide signaling and turnover: PtdIns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities. EMBO (Eur. Mol. Biol. Organ.) J. 17:4930-4942.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 4930-4942
    • Wurmser, A.1    Emr, S.D.2
  • 86
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., S.C. Harrison, and M.J. Eck. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature. 385:595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 87
    • 0029024442 scopus 로고
    • Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast
    • Yamamoto, A., D.B. DeWald, I.V. Boronenkov, R.A. Anderson, S.D. Emr, and D. Koshland. 1995. Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast. Mol. Biol. Cell. 6:525-539.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 525-539
    • Yamamoto, A.1    DeWald, D.B.2    Boronenkov, I.V.3    Anderson, R.A.4    Emr, S.D.5    Koshland, D.6
  • 88
    • 0027979837 scopus 로고
    • A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae
    • Yoshida, S., Y. Ohya, M. Goebl, A. Nakano, and Y. Anraku. 1994. A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae. J. Biol. Chem. 269:1166-1172.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1166-1172
    • Yoshida, S.1    Ohya, Y.2    Goebl, M.3    Nakano, A.4    Anraku, Y.5


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