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Volumn 140, Issue 6, 1998, Pages 1347-1356

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

Author keywords

[No Author keywords available]

Indexed keywords

FRUCTOSE BISPHOSPHATASE; GENE PRODUCT; GLUCOSE; MEMBRANE PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG; VID24P PROTEIN;

EID: 0032559855     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.6.1347     Document Type: Article
Times cited : (65)

References (41)
  • 1
    • 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. Klinosky, and S. 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    Klinosky, D.J.3    Emr, S.4
  • 2
    • 0017254334 scopus 로고
    • Protein degradation and proteinases during yeast sporulation: Enzymes and cytochrome patterns
    • Betz, H., and U. Weiser. 1976. Protein degradation and proteinases during yeast sporulation: enzymes and cytochrome patterns. Eur. J. Biochem. 62: 65-76.
    • (1976) Eur. J. Biochem. , vol.62 , pp. 65-76
    • Betz, H.1    Weiser, U.2
  • 3
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang, H.-L., and J.F. Dice. 1988. Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J. Biol. Chem. 263:6797-6805.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6797-6805
    • Chiang, H.-L.1    Dice, J.F.2
  • 4
    • 0025804582 scopus 로고
    • Regulated import and degradation of a cytosolic protein in the yeast vacuole
    • Chiang, H.-L., and R. Schekman. 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
  • 5
    • 0343172098 scopus 로고
    • Site of calabolite inactivation
    • Chiang, H.-L., and R. Schekman. 1994. Site of calabolite inactivation. Nature. 369:284.
    • (1994) Nature , vol.369 , pp. 284
    • Chiang, H.-L.1    Schekman, R.2
  • 6
    • 0024975155 scopus 로고
    • A role for a 70 kD heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H.-L., S.R. Terlecky, C.P. Plant, and J.F. Dice. 1989. A role for a 70 kD 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
  • 7
    • 0029875385 scopus 로고    scopus 로고
    • Selective uptake of cytosolic, peroxisomal and plasma membrane proteins by the yeast vacuole
    • Chiang, H.-L., R. Schekman, and S. Hamamoto. 1996. Selective uptake of cytosolic, peroxisomal and plasma membrane proteins by the yeast vacuole. 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
  • 8
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • Cooper, A.A., and T.H. Stevens. 1996. Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J. Cell Biol. 133:529-541.
    • (1996) J. Cell Biol. , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 9
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A.M., and J.F. Dice. 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
  • 10
    • 0027944153 scopus 로고
    • Selective binding and uptake of RNase A and glyceraldehyde-3-phosphate dehydrogenase by isolated rat liver lysosome
    • Cuervo, A.M., S.R. Terlecky, J.F. Dice, and E. Knecht. 1994. Selective binding and uptake of RNase A and glyceraldehyde-3-phosphate dehydrogenase by isolated rat liver lysosome. Y. Biol. Chem. 269:26374-26380.
    • (1994) Y. Biol. Chem. , vol.269 , pp. 26374-26380
    • Cuervo, A.M.1    Terlecky, S.R.2    Dice, J.F.3    Knecht, E.4
  • 11
    • 0027175829 scopus 로고
    • Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptor
    • Davis, N.G., J.L. Horecka, and G.F. Sparague. 1993. Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptor. J. Cell Biol. 122:53-65.
    • (1993) J. Cell Biol. , vol.122 , pp. 53-65
    • Davis, N.G.1    Horecka, J.L.2    Sparague, G.F.3
  • 12
    • 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 in Biochem. 15:305-309.
    • (1990) Trends in Biochem. , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 13
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stresses
    • Finley, D., E. Ozakaynak, and A. Varshavsky. 1987. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stresses. Cell. 48:1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Ozakaynak, E.2    Varshavsky, A.3
  • 14
    • 0015100291 scopus 로고
    • Inactivation of fructose-1,6-bisphosphatase by glucose in yeast
    • Gancedo, C. 1971. Inactivation of fructose-1,6-bisphosphatase by glucose in yeast. J. Bacteriol. 107:401-405.
    • (1971) J. Bacteriol. , vol.107 , pp. 401-405
    • Gancedo, C.1
  • 15
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C. and G. Fink. 1991. Guide to yeast genetics and molecular biology. Methods Enzymol. 194:21-37.
    • (1991) Methods Enzymol. , vol.194 , pp. 21-37
    • Guthrie, C.1    Fink, G.2
  • 16
    • 0028800171 scopus 로고
    • Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
    • Harding, T.M., K.A. Morano, S.V. Scott, and D.J. Klionsky. 1995. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J. Cell Biol. 131:591-602.
    • (1995) J. Cell Biol. , vol.131 , pp. 591-602
    • Harding, T.M.1    Morano, K.A.2    Scott, S.V.3    Klionsky, D.J.4
  • 17
    • 0029953575 scopus 로고    scopus 로고
    • Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway
    • Harding T.M., A. Hefner-Gravink, M. Thumn, and D.J. Klionsky. 1996. Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway. J. Biol. Chem. 30:17621-17624.
    • (1996) J. Biol. Chem. , vol.30 , pp. 17621-17624
    • Harding, T.M.1    Hefner-Gravink, A.2    Thumn, M.3    Klionsky, D.J.4
  • 18
    • 0017842062 scopus 로고
    • Biosynthesis of the vacuolar yeast glycoprotein. Carboxypeptidase Y conversion of precursor into the enzyme
    • Hasilik, A., and W. Tanner. 1978. Biosynthesis of the vacuolar yeast glycoprotein. Carboxypeptidase Y conversion of precursor into the enzyme. Eur. J. Biochem. 85:599-608.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 599-608
    • Hasilik, A.1    Tanner, W.2
  • 19
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Haves, S., and J.F. Dice. 1996. Roles of molecular chaperones in protein degradation. J. Cell Biol. 132:255-258.
    • (1996) J. Cell Biol. , vol.132 , pp. 255-258
    • Haves, S.1    Dice, J.F.2
  • 20
    • 0009353803 scopus 로고
    • Mutants defective in processing of an enzyme located in the lysosome-like vacuole of Saccharomyces cerevisiae
    • Hemmings, B., G. Zubenko, A. Hasilik, and E.W. Jones. 1981. Mutants defective in processing of an enzyme located in the lysosome-like vacuole of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 78:435-439.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 435-439
    • Hemmings, B.1    Zubenko, G.2    Hasilik, A.3    Jones, E.W.4
  • 21
    • 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 H.-L. Chiang. 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
  • 22
    • 0031019152 scopus 로고    scopus 로고
    • Identification of novel vesicles in the cytosol to vacuole protein degradation pathway
    • Huang, P-H., and H.-L. Chiang. 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
  • 23
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones, E.W. 1991. Three proteolytic systems in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 266:7963-7966.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 24
    • 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
  • 25
    • 0028277963 scopus 로고
    • The ABC transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kolling, R., and C. Hollenberg. 1994. The ABC transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO (Eur. Mol. Biol. Organ.) J. 13:3261-3271.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.2
  • 26
    • 0028819235 scopus 로고
    • Regulation of inositol transport in Saccharomyces cerevisiae involves inositol-induced changes in permease stability and endocytic degradation in the vacuole
    • Lai, K., C. Bolognese, S. Swift, and P. McGraw. 1995. Regulation of inositol transport in Saccharomyces cerevisiae involves inositol-induced changes in permease stability and endocytic degradation in the vacuole. J. Biol. Chem. 270:2525-2534.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2525-2534
    • Lai, K.1    Bolognese, C.2    Swift, S.3    McGraw, P.4
  • 27
    • 0026043846 scopus 로고
    • Isolation and characterization of osmosensitive vacuolar mutants of Saccharomyces cerevisiae
    • Latterich, M., and M.D. Watson. 1991. Isolation and characterization of osmosensitive vacuolar mutants of Saccharomyces cerevisiae. Mol. Microbiol. 5:2417-2426.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2417-2426
    • Latterich, M.1    Watson, M.D.2
  • 28
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E.G., B.F. Horadovsky, J.L. Cereghino, E. Gharakhanian, and S. Emr. 1994. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell. 77:579-586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horadovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.5
  • 29
    • 0027455339 scopus 로고
    • end3 and end 4: Two mutants defective in receptor-mediated and fluid phase endocytosis in S. cerevisiae
    • Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end 4: Two mutants defective in receptor-mediated and fluid phase endocytosis in S. 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
  • 30
    • 0029560314 scopus 로고
    • Catabolite inactivation of the yeast maltose transporter occurs in the vacuole after internalization by endocytosis
    • Riballo, E., M. Herwerjer, D.H. Wolf, and R. Lagunas. 1995. Catabolite inactivation of the yeast maltose transporter occurs in the vacuole after internalization by endocytosis. J. Bacteriol. 177:5622-5627.
    • (1995) J. Bacteriol. , vol.177 , pp. 5622-5627
    • Riballo, E.1    Herwerjer, M.2    Wolf, D.H.3    Lagunas, R.4
  • 31
    • 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
  • 32
    • 0022898326 scopus 로고
    • Protein sorting in yeast: Mutants defective in vacuolar biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • Rothman, J., and T. Stevens. 1986. Protein sorting in yeast: mutants defective in vacuolar biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell. 47:1041-1051.
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.1    Stevens, T.2
  • 33
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast α-factor pheromone receptor
    • Schandel, K., and D. Jennes. 1994. Direct evidence for ligand-induced internalization of the yeast α-factor pheromone receptor. Mol. Cell. Biol. 14:7245-7255.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7245-7255
    • Schandel, K.1    Jennes, D.2
  • 34
    • 0029913505 scopus 로고    scopus 로고
    • Cytoplasm to vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
    • Scott, S.V., A. Hefner-Gravink, K.A. Morano, T. Noda, Y. Ohsumi, and D. Klionsky. 1996. Cytoplasm to vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc. Natl. Acad. Sci. USA. 93:12304-12308.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12304-12308
    • Scott, S.V.1    Hefner-Gravink, A.2    Morano, K.A.3    Noda, T.4    Ohsumi, Y.5    Klionsky, D.6
  • 35
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige, K., M. Baba, S. Tsuboi, T. Noda, and Y. Ohsumi. 1992. Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 119:301-311.
    • (1992) J. Cell Biol. , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 36
    • 0026808914 scopus 로고
    • Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by 73 kD heat shock cognate protein
    • Terlecky, S.R., H.-L. Chiang, T.S. Oslon, and J.F. Dice. 1992. Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by 73 kD 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    Oslon, T.S.3    Dice, J.F.4
  • 37
    • 0027379661 scopus 로고
    • Polypeptide import and degradation by isolated lysosomes
    • Terlecky, S.R., and J.F. Dice. 1993. Polypeptide import and degradation by isolated lysosomes. J. Biol. Chem. 268:23490-23495.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23490-23495
    • Terlecky, S.R.1    Dice, J.F.2
  • 38
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada, M., and Y. Ohsumi. 1993. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS (Fed. Eur. Biochem. Soc.) Lett. 333:169-174.
    • (1993) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 39
    • 0028855325 scopus 로고
    • Divergent modes of autophagy in the methylotrophic yeast Pichia pastoris
    • Tuttle, D.L., and W.A. Dunn. 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.2
  • 40
    • 0025696339 scopus 로고
    • A novel pathway of import of α-mannosidase, a marker enzyme for vacuolar membrane, in Sacchuromyces cerevisiae
    • Yoshihisa, T., and Y. Anraku. 1990. A novel pathway of import of α-mannosidase, a marker enzyme for vacuolar membrane, in Sacchuromyces cerevisiae. J. Biol. Chem. 265:22418-22425.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22418-22425
    • Yoshihisa, T.1    Anraku, Y.2
  • 41
    • 0019345573 scopus 로고
    • Protein degradation, meiosis and sporulation in proteinase-deficient mutants of Saccharomyces cerevisiae
    • Zuhenko, G.S., and E.W. Jones. 1981. Protein degradation, meiosis and sporulation in proteinase-deficient mutants of Saccharomyces cerevisiae. Genetics 97:45-64.
    • (1981) Genetics , vol.97 , pp. 45-64
    • Zuhenko, G.S.1    Jones, E.W.2


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