메뉴 건너뛰기




Volumn 10, Issue 9, 1999, Pages 2879-2889

Import into and degradation of cytosolic proteins by isolated yeast vacuoles

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 70; PROTEIN;

EID: 0032823270     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.9.2879     Document Type: Article
Times cited : (32)

References (58)
  • 1
    • 0021721357 scopus 로고
    • Proteolysis in eukaryotic cells. Identification of multiple proteolytic enzymes in yeast
    • Achstetter, T., Emter, O., Ehmann, C., and Wolf, D.H. (1984). Proteolysis in eukaryotic cells. Identification of multiple proteolytic enzymes in yeast. J. Biol. Chem. 259, 13334-13343.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13334-13343
    • Achstetter, T.1    Emter, O.2    Ehmann, C.3    Wolf, D.H.4
  • 2
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes, F.A., Terlecky, S.R., and Dice, J.F. (1997). An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J. Cell Biol. 137, 825-834.
    • (1997) J. Cell Biol. , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 3
    • 0028302033 scopus 로고
    • GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high osmolarity glycerol response pathway
    • Albertyn, J., Hohmann, S., Thevelein, J.M., and Prior, B.A. (1994). GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high osmolarity glycerol response pathway. Mol. Cell. Biol. 14, 4135-4144.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4135-4144
    • Albertyn, J.1    Hohmann, S.2    Thevelein, J.M.3    Prior, B.A.4
  • 4
    • 0027280820 scopus 로고
    • Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes
    • Aniento, F., Roche, E., Cuervo, A.M., and Knecht, E. (1993). Uptake and degradation of glyceraldehyde-3-phosphate dehydrogenase by rat liver lysosomes. J. Biol. Chem. 268, 10463-10470.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10463-10470
    • Aniento, F.1    Roche, E.2    Cuervo, A.M.3    Knecht, E.4
  • 5
    • 0030957959 scopus 로고    scopus 로고
    • Autophagic proteolysis: Control and specificity
    • Blommaart, E.F.C., Luiken, J.J.P., and Meijer, A.J. (1997). Autophagic proteolysis: control and specificity. Histochem. J. 29, 365-385.
    • (1997) Histochem. J. , vol.29 , pp. 365-385
    • Blommaart, E.F.C.1    Luiken, J.J.P.2    Meijer, A.J.3
  • 6
    • 0031911736 scopus 로고    scopus 로고
    • Vacuole biogenesis of Saccharomyces cerevisiae: Protein transport pathways to the yeast vacuole
    • Bryant, N.J., and Stevens, T.H. (1998). Vacuole biogenesis of Saccharomyces cerevisiae: protein transport pathways to the yeast vacuole. Microbiol. Mol. Biol. Rev. 62, 230-247.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 230-247
    • Bryant, N.J.1    Stevens, T.H.2
  • 7
    • 0032559855 scopus 로고    scopus 로고
    • Vid24p, a novel protein localized to the fructose-1,6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation
    • Chiang, M.C., and Chiang, H.-L. (1998). Vid24p, a novel protein localized to the fructose-1,6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation. J. Cell Biol. 140, 1347-1356.
    • (1998) J. Cell Biol. , vol.140 , pp. 1347-1356
    • Chiang, M.C.1    Chiang, H.-L.2
  • 8
    • 0025804582 scopus 로고
    • Regulated import and degradation of a cytosolic protein in the yeast vacuole
    • Chiang, H.-L., and Schekman, R. (1991). Regulated import and degradation of a cytosolic protein in the yeast vacuole. Nature 350, 313-318.
    • (1991) Nature , vol.350 , pp. 313-318
    • Chiang, H.-L.1    Schekman, R.2
  • 9
    • 0029875385 scopus 로고    scopus 로고
    • Selective uptake of cytosolic, peroxisomal, and plasma membrane proteins into the yeast lysosome for degradation
    • Chiang, H.-L., Schekman, R., and Hamamoto, S. (1996). Selective uptake of cytosolic, peroxisomal, and plasma membrane proteins into the yeast lysosome for degradation. J. Biol. Chem. 271, 9934-9941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9934-9941
    • Chiang, H.-L.1    Schekman, R.2    Hamamoto, S.3
  • 10
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H.-L., Terlecky, S.R., Plant, C.P., and Dice, J.F. (1989). A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382-385.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.-L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 11
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico, W.J., Waters, M.G., and Blobel, G. (1988). 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332, 805-810.
    • (1988) Nature , vol.332 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 12
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., and Goldberg, A.L. (1996). Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 13
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A.M., and Dice, J.F. (1996). A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501-503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 14
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • Cuervo, A.M., Dice, J.F., and Knecht, E. (1997). A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J. Biol. Chem. 272, 5606-5615.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 15
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo, A.M., Knecht, E., Terlecky, S.R., and Dice, J.F. (1995). Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am. J. Physiol. 269, C1200-C1208.
    • (1995) Am. J. Physiol. , vol.269
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 16
    • 0027175829 scopus 로고
    • Cis- and transacting functions required for the endocytosis of the yeast pheromone receptors
    • Davis, N.G., Horecka, J.L., and Sprague, G.F. (1993). Cis- and transacting functions required for the endocytosis of the yeast pheromone receptors. J. Cell Biol. 122, 53-65.
    • (1993) J. Cell Biol. , vol.122 , pp. 53-65
    • Davis, N.G.1    Horecka, J.L.2    Sprague, G.F.3
  • 17
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies, R.J., Koch, B.D., Werner-Washburne, M., Craig, E.A., and Schekman, R. (1988). A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332, 800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 18
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice, J.F. (1990). Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15, 305-309.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 19
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome mediated protein degradation
    • Dunn, W.A. (1994). Autophagy and related mechanisms of lysosome mediated protein degradation. Trends Cell Biol. 4, 139-143.
    • (1994) Trends Cell Biol. , vol.4 , pp. 139-143
    • Dunn, W.A.1
  • 20
    • 0027716683 scopus 로고
    • Tracing intracellular proteolytic pathways. Proteolysis of fatty acid synthase and other cytoplasmic proteins in the yeast Saccharomyces cerevisiae
    • Egner, R., Thumm, M., Straub, M., Simeon, A., Schuller, H.J., and Wolf, D.H. (1993). Tracing intracellular proteolytic pathways. Proteolysis of fatty acid synthase and other cytoplasmic proteins in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 268, 27269-27276.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27269-27276
    • Egner, R.1    Thumm, M.2    Straub, M.3    Simeon, A.4    Schuller, H.J.5    Wolf, D.H.6
  • 21
    • 0029097555 scopus 로고
    • Cloning and characterization of GPD2, a second gene encoding sn-glycerol-3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae and its comparison with GPD1
    • Eriksson, P., Andre, L., Ansell, R., Blomberg, A., and Adler, L. (1995). Cloning and characterization of GPD2, a second gene encoding sn-glycerol-3-phosphate dehydrogenase (NAD+) in Saccharomyces cerevisiae and its comparison with GPD1. Mol. Microbiol. 17, 95-107.
    • (1995) Mol. Microbiol. , vol.17 , pp. 95-107
    • Eriksson, P.1    Andre, L.2    Ansell, R.3    Blomberg, A.4    Adler, L.5
  • 22
    • 0032514213 scopus 로고    scopus 로고
    • Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex
    • Graham, L.A., Hill, K.J., and Stevens, T.H. (1998), Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex. J. Cell Biol. 142, 39-49.
    • (1998) J. Cell Biol. , vol.142 , pp. 39-49
    • Graham, L.A.1    Hill, K.J.2    Stevens, T.H.3
  • 23
    • 0001199243 scopus 로고
    • A quantitative assay to measure homotypic vacuole fusion in vitro
    • Haas, A. (1995). A quantitative assay to measure homotypic vacuole fusion in vitro. Methods Cell Sci. 17, 283-294.
    • (1995) Methods Cell Sci. , vol.17 , pp. 283-294
    • Haas, A.1
  • 24
    • 0029096887 scopus 로고
    • Reconstitution of the initial steps of mitochondrial protein import
    • Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G., and Lithgow, T. (1995). Reconstitution of the initial steps of mitochondrial protein import. Nature 376, 705-709.
    • (1995) Nature , vol.376 , pp. 705-709
    • Hachiya, N.1    Mihara, K.2    Suda, K.3    Horst, M.4    Schatz, G.5    Lithgow, T.6
  • 25
    • 0017599706 scopus 로고
    • Effects of glucose and nitrogen source on the levels of proteinases, peptidases, and proteinase inhibitors in yeast
    • Hansen, R.J., Switzer, R.L., Hinze, H., and Holzer, H. (1977). Effects of glucose and nitrogen source on the levels of proteinases, peptidases, and proteinase inhibitors in yeast. Biochim. Biophys. Acta 496, 103-114.
    • (1977) Biochim. Biophys. Acta , vol.496 , pp. 103-114
    • Hansen, R.J.1    Switzer, R.L.2    Hinze, H.3    Holzer, H.4
  • 26
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes, S.A., and Dice, J.F. (1996). Roles of molecular chaperones in protein degradation. J. Cell Biol. 132, 255-258.
    • (1996) J. Cell Biol. , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 27
    • 0029844569 scopus 로고    scopus 로고
    • Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae
    • Hoffman, M., and Chiang, H.-L. (1996). Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae. Genetics 143, 1555-1566.
    • (1996) Genetics , vol.143 , pp. 1555-1566
    • Hoffman, M.1    Chiang, H.-L.2
  • 28
    • 0031025479 scopus 로고    scopus 로고
    • What is the driving force for protein import into mitochondria?
    • Horst, M., Azem, A., Schatz, G., and Glick, B.S. (1997). What is the driving force for protein import into mitochondria? Biochim. Biophys. Acta 2328, 71-78.
    • (1997) Biochim. Biophys. Acta , vol.2328 , pp. 71-78
    • Horst, M.1    Azem, A.2    Schatz, G.3    Glick, B.S.4
  • 29
    • 0029052947 scopus 로고
    • Dynamic interaction of the protein translocation systems in the inner and outer membranes of yeast mitochondria
    • Horst, M., Hilfiker-Rothenfluh, S., Oppliger, W., and Schatz, G. (1995). Dynamic interaction of the protein translocation systems in the inner and outer membranes of yeast mitochondria. EMBO J. 14, 2293-2297.
    • (1995) EMBO J. , vol.14 , pp. 2293-2297
    • Horst, M.1    Hilfiker-Rothenfluh, S.2    Oppliger, W.3    Schatz, G.4
  • 30
    • 0031019152 scopus 로고    scopus 로고
    • Identification of novel vesicles in the cytosol to vacuole protein degradation pathway
    • Huang, P.-H., and Chiang, H.-L. (1997). Identification of novel vesicles in the cytosol to vacuole protein degradation pathway. J. Cell Biol. 136, 803-810.
    • (1997) J. Cell Biol. , vol.136 , pp. 803-810
    • Huang, P.-H.1    Chiang, H.-L.2
  • 31
    • 0032079372 scopus 로고    scopus 로고
    • Nonclassical protein sorting in the yeast vacuole
    • Klionsky, D.J. (1998). Nonclassical protein sorting in the yeast vacuole. J. Biol. Chem. 273, 10807-10810.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10807-10810
    • Klionsky, D.J.1
  • 32
    • 0026640551 scopus 로고
    • Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
    • Klionsky, D.J., Cueva, R., and Yaver, D.S. (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
  • 33
    • 0012708269 scopus 로고    scopus 로고
    • Pathways for the degradation of intracellular proteins within lysosomes in higher eukaryotes
    • Knecht, E., Martín de Llano, J.J., Andreu, E.J., and Moreno Miralles, I. (1998). Pathways for the degradation of intracellular proteins within lysosomes in higher eukaryotes. Adv. Cell Mol. Biol. 27, 201-234.
    • (1998) Adv. Cell Mol. Biol. , vol.27 , pp. 201-234
    • Knecht, E.1    Martín De Llano, J.J.2    Andreu, E.J.3    Moreno Miralles, I.4
  • 35
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D.A., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 36
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham, H.R.B. (1989). Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 1-23.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 37
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., Rohrer, J., Crausaz, F., and Riezman, H. (1993). end3 and end4: two mutants defective in receptor mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120, 55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 38
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and Dobberstein, B. (1996). Common principles of protein translocation across membranes. Science 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 39
    • 0028108317 scopus 로고
    • Catabolite inactivation of fructose-1,6-bisphosphatase in yeast is mediated by the proteasome
    • Schork, S.M., Bee, G., Thumm, M., and Wolf, D.H. (1994a). Catabolite inactivation of fructose-1,6-bisphosphatase in yeast is mediated by the proteasome. FEBS Lett. 349, 270-274.
    • (1994) FEBS Lett. , vol.349 , pp. 270-274
    • Schork, S.M.1    Bee, G.2    Thumm, M.3    Wolf, D.H.4
  • 40
    • 0028243911 scopus 로고
    • Site of catabolite inactivation
    • Schork, S.M., Bee, G., Thumm, M., and Wolf, D.H. (1994b). Site of catabolite inactivation. Nature 369, 283-284.
    • (1994) Nature , vol.369 , pp. 283-284
    • Schork, S.M.1    Bee, G.2    Thumm, M.3    Wolf, D.H.4
  • 41
  • 42
    • 0026584008 scopus 로고
    • Autophagy and other vacuolar protein degradation mechanisms
    • Seglen, P.O., and Bohley, P. (1992). Autophagy and other vacuolar protein degradation mechanisms. Experientia 48, 158-172.
    • (1992) Experientia , vol.48 , pp. 158-172
    • Seglen, P.O.1    Bohley, P.2
  • 43
    • 0028842924 scopus 로고
    • Yeast aminopeptidase I is posttranslationally sorted from the cytosol to the vacuole by a mechanism mediated by ist bipartite N-terminal extension
    • Seguí-Real, B., Martinez, M., and Sandoval, I.V. (1995). Yeast aminopeptidase I is posttranslationally sorted from the cytosol to the vacuole by a mechanism mediated by ist bipartite N-terminal extension. EMBO J. 14, 5476-5484.
    • (1995) EMBO J. , vol.14 , pp. 5476-5484
    • Seguí-Real, B.1    Martinez, M.2    Sandoval, I.V.3
  • 44
    • 0032488997 scopus 로고    scopus 로고
    • In vitro reconstitution of glucose-induced targeting of fructose-1.6-bisphosphatase into the vacuole in semiintact yeast cells
    • Shieh, H.-L., and Chiang, H.-L. (1998). In vitro reconstitution of glucose-induced targeting of fructose-1.6-bisphosphatase into the vacuole in semiintact yeast cells. J. Biol. Chem. 273, 3381-3387.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3381-3387
    • Shieh, H.-L.1    Chiang, H.-L.2
  • 45
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige, K., Baba, M., Tsuboi, S., Noda, T., and Ohsumi, Y. (1992). Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 219, 301-311.
    • (1992) J. Cell Biol. , vol.219 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 46
    • 0024459376 scopus 로고
    • Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival
    • Teichert, U., Mechler, B., Müller, H., and Wolf, D.H. (1989). Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. J. Biol. Chem. 264, 16037-16045.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16037-16045
    • Teichert, U.1    Mechler, B.2    Müller, H.3    Wolf, D.H.4
  • 47
    • 0028135554 scopus 로고
    • Hsp70s and lysosomal proteolysis
    • Terlecky, S.R. (1994). Hsp70s and lysosomal proteolysis. Experientia 50, 1021-1025.
    • (1994) Experientia , vol.50 , pp. 1021-1025
    • Terlecky, S.R.1
  • 48
    • 0026808914 scopus 로고
    • Protein and pepride binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein
    • Terlecky, S.R., Chiang, H.-L., Olson, T.S., and Dice, J.F. (1992). Protein and pepride binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. J. Biol. Chem. 267, 9202-9209.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9202-9209
    • Terlecky, S.R.1    Chiang, H.-L.2    Olson, T.S.3    Dice, J.F.4
  • 49
    • 0345615615 scopus 로고    scopus 로고
    • From proteasome to lysosome: Studies on yeast demonstrate the principles of protein degradation in the eukaryotic cell
    • Thumm, M., and Wolf, D.H, (1998). From proteasome to lysosome: studies on yeast demonstrate the principles of protein degradation in the eukaryotic cell. Adv. Cell Mol. Biol. 27, 43-70.
    • (1998) Adv. Cell Mol. Biol. , vol.27 , pp. 43-70
    • Thumm, M.1    Wolf, D.H.2
  • 50
    • 0028855325 scopus 로고
    • Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris
    • Tuttle, D.L., and Dunn, W.A., Jr. (1995). Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris. J. Cell Sci. 108, 25-35.
    • (1995) J. Cell Sci. , vol.108 , pp. 25-35
    • Tuttle, D.L.1    Dunn W.A., Jr.2
  • 51
    • 0023375806 scopus 로고
    • Complex interactions among members of the essential subfamily of hsp70 genes in Saccharomyces cerevisiae
    • Werner-Washburne, M., Stone, D.E., and Craig, E.A. (1987). Complex interactions among members of the essential subfamily of hsp70 genes in Saccharomyces cerevisiae. Mol. Cell. Biol. 7, 2568-2577.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2568-2577
    • Werner-Washburne, M.1    Stone, D.E.2    Craig, E.A.3
  • 52
    • 0016588191 scopus 로고
    • Isolation of vacuoles from yeast. Methods
    • Wiemken, A. (1975). Isolation of vacuoles from yeast. Methods Cell Biol. 12, 99-109.
    • (1975) Cell Biol. , vol.12 , pp. 99-109
    • Wiemken, A.1
  • 53
    • 0025801067 scopus 로고
    • Proteins containing peptide sequences related to Lys-Phe-Glu-Arg-Gln are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats
    • Wing, S.S., Chiang, H.-L., Goldberg, A.L., and Dice, J.F. (1991). Proteins containing peptide sequences related to Lys-Phe-Glu-Arg-Gln are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats. Biochem. J. 275, 165-169.
    • (1991) Biochem. J. , vol.275 , pp. 165-169
    • Wing, S.S.1    Chiang, H.-L.2    Goldberg, A.L.3    Dice, J.F.4
  • 54
    • 0029679761 scopus 로고    scopus 로고
    • Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A
    • Wolff, A.M., Din, N., and Petersen, J.G. (1996). Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A. Yeast 12, 823-832.
    • (1996) Yeast , vol.12 , pp. 823-832
    • Wolff, A.M.1    Din, N.2    Petersen, J.G.3
  • 55
    • 0027156142 scopus 로고
    • Vacuolar ATPase mutants accumulate precursor proteins in a prevacuolar compartment
    • Yaver, D.S., Nelson, H., Nelson, N., and Klionsky, D.J. (1993). Vacuolar ATPase mutants accumulate precursor proteins in a prevacuolar compartment. J. Biol. Chem. 268, 10564-10572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10564-10572
    • Yaver, D.S.1    Nelson, H.2    Nelson, N.3    Klionsky, D.J.4
  • 56
    • 0025696339 scopus 로고
    • A novel pathway of import of α-mannosidase, a marker enzyme of vacuolar membrane in Saccharomyces cerevisiae
    • Yoshihisa, T., and Anraku, Y. (1990). A novel pathway of import of α-mannosidase, a marker enzyme of vacuolar membrane in Saccharomyces cerevisiae. J. Biol. Chem. 265, 22418-22425.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22418-22425
    • Yoshihisa, T.1    Anraku, Y.2
  • 57
    • 0023939244 scopus 로고
    • Solubilization and purification of alpha-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae
    • Yoshihisa, T., Ohsumi, Y., and Anraku, Y. (1988). Solubilization and purification of alpha-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae. J. Biol. Chem. 263, 5158-5163.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5158-5163
    • Yoshihisa, T.1    Ohsumi, Y.2    Anraku, Y.3
  • 58
    • 0030883562 scopus 로고    scopus 로고
    • Glucose-induced microautophagy in Pichia pastoris requires the alpha subunit of phosphofructokinase
    • Yuan, W., Tuttle, D.L., Shi, Y.-J., Ralph, G.S., and Dunn, W.A., Jr. (1997). Glucose-induced microautophagy in Pichia pastoris requires the alpha subunit of phosphofructokinase. J. Cell Sci. 110, 1935-1945.
    • (1997) J. Cell Sci. , vol.110 , pp. 1935-1945
    • Yuan, W.1    Tuttle, D.L.2    Shi, Y.-J.3    Ralph, G.S.4    Dunn W.A., Jr.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.