메뉴 건너뛰기




Volumn 112, Issue 10, 1999, Pages 1417-1423

The ubiquitin-proteosome system and endocytosis

Author keywords

Downregulation; Endocytosis; Growth hormone; Proteasome; Receptor; Ubiquitin

Indexed keywords

CLATHRIN; GROWTH HORMONE; GROWTH HORMONE RECEPTOR; MEMBRANE PROTEIN; PROTEASOME; UBIQUITIN;

EID: 0033054154     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (178)

References (79)
  • 1
    • 0030978351 scopus 로고    scopus 로고
    • β-catenin is a target for the ubiquitin-proteasome pathway
    • Aberle, H., Bauer, A., Stappert, J., Kispert, A. and Kemler, R. (1997). β-catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 16, 3797-3804.
    • (1997) EMBO J. , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 2
    • 0030271387 scopus 로고    scopus 로고
    • NF-κ B: Ten years after
    • Baeuerle, P. A. and Baltimore, D. (1996). NF-κ B: ten years after. Cell 87, 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 3
    • 0028108747 scopus 로고
    • Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system
    • Cahoreau, C., Garnier, L., Djiane, J., Devauchelle, G. and Cerutti, M. (1994). Evidence for N-glycosylation and ubiquitination of the prolactin receptor expressed in a baculovirus-insect cell system. FEBS Lett. 350, 230-234.
    • (1994) FEBS Lett. , vol.350 , pp. 230-234
    • Cahoreau, C.1    Garnier, L.2    Djiane, J.3    Devauchelle, G.4    Cerutti, M.5
  • 6
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K. and Varshavsky, A. (1989). A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 7
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cyloplasmic tails, is required for coated pit-mediated internalization of the LDL receptor
    • Chen, W.-J., Goldstein, J. L. and Brown, M. S. (1990). NPXY, a sequence often found in cyloplasmic tails, is required for coated pit-mediated internalization of the LDL receptor. J. Biol. Chem. 265, 3116-3123.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3116-3123
    • Chen, W.-J.1    Goldstein, J.L.2    Brown, M.S.3
  • 8
    • 0025635559 scopus 로고
    • Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
    • Collawn, J. F., Stangel, M., Kuhn, L. A., Esekogwu, V., Jing, S. Q., Trowbridge, I. S. and Tainer, J. A. (1990). Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell 63, 1061-1072.
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawn, J.F.1    Stangel, M.2    Kuhn, L.A.3    Esekogwu, V.4    Jing, S.Q.5    Trowbridge, I.S.6    Tainer, J.A.7
  • 10
    • 17544365657 scopus 로고    scopus 로고
    • Molecular characterization of the di-leucine-based internalization motif of the T cell receptor
    • Dietrich, J., Hou, X. H., Wegener, A. M. K., Pedersen, L. O., Odum, N. and Geisler, C. (1996). Molecular characterization of the di-leucine-based internalization motif of the T cell receptor. J. Biol. Chem. 271, 11441-11448.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11441-11448
    • Dietrich, J.1    Hou, X.H.2    Wegener, A.M.K.3    Pedersen, L.O.4    Odum, N.5    Geisler, C.6
  • 11
    • 0029961666 scopus 로고    scopus 로고
    • A di-leucine motif and an upstream serine in the interleukin-6 (IL-6) signal transducer gpl30 mediate ligand-induced endocytosis and down-regulation of the il-6 receptor
    • Dittrich, E., Haft, C. R., Muys, L., Heinrich, P. C. and Graeve, L. (1996). A di-leucine motif and an upstream serine in the interleukin-6 (IL-6) signal transducer gpl30 mediate ligand-induced endocytosis and down-regulation of the il-6 receptor. J. Biol Chem. 271, 5487-5494.
    • (1996) J. Biol Chem. , vol.271 , pp. 5487-5494
    • Dittrich, E.1    Haft, C.R.2    Muys, L.3    Heinrich, P.C.4    Graeve, L.5
  • 12
    • 0024463635 scopus 로고
    • Ubiquitin-protein conjugates accumulate in the lysosomal system of fibroblasts treated with cysteine proteinase inhibitors
    • Doherty, F. J., Osborn, N. U., Wassell, J. A., Heggie, P. E., Laszlo, L. and Mayer, R. J. (1989). Ubiquitin-protein conjugates accumulate in the lysosomal system of fibroblasts treated with cysteine proteinase inhibitors. Biochem. J. 263, 47-55.
    • (1989) Biochem. J. , vol.263 , pp. 47-55
    • Doherty, F.J.1    Osborn, N.U.2    Wassell, J.A.3    Heggie, P.E.4    Laszlo, L.5    Mayer, R.J.6
  • 13
    • 0030041980 scopus 로고    scopus 로고
    • The yeast multidrug transporter pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole
    • Egner, R. and Kuchler, K. (1996). The yeast multidrug transporter pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole. FEBS Lett. 378, 177-181.
    • (1996) FEBS Lett. , vol.378 , pp. 177-181
    • Egner, R.1    Kuchler, K.2
  • 16
    • 0028362030 scopus 로고
    • The yeast plasma membrane uracil permease is stabilized against stress induced degradation by a point mutation in a cyclin-like destruction box
    • Galan, J. M., Volland, C., Urban-Grimal, D. and Haguenauer-Tsapis, R. (1994). The yeast plasma membrane uracil permease is stabilized against stress induced degradation by a point mutation in a cyclin-like destruction box. Biochem. Biophys. Res. Commun. 201, 769-775.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 769-775
    • Galan, J.M.1    Volland, C.2    Urban-Grimal, D.3    Haguenauer-Tsapis, R.4
  • 17
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the npi1p/rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J. M., Moreau, V. andré, B., Volland, C. and Haguenauer-Tsapis, R. (1996). Ubiquitination mediated by the npi1p/rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271, 10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    André, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 18
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M. and Haguenauer-Tsapis, R. (1997). Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854.
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 19
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalently linked to ubiquitin
    • Galcheva-Gargova, Z., Theroux, S. J. and Davis, R. J. (1995). The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene 11, 2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Gargova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 20
    • 0028211775 scopus 로고
    • The amino terminus of GLUT4 functions as an internalization motif but not an intracellular retention signal when substituted for the transferrin receptor cytoplasmic domain
    • Garippa, R. J., Judge, T. W., James, D. E. and McGraw, T. E. (1994). The amino terminus of GLUT4 functions as an internalization motif but not an intracellular retention signal when substituted for the transferrin receptor cytoplasmic domain. J. Cell Biol. 124, 705-715.
    • (1994) J. Cell Biol. , vol.124 , pp. 705-715
    • Garippa, R.J.1    Judge, T.W.2    James, D.E.3    McGraw, T.E.4
  • 21
    • 0029832206 scopus 로고    scopus 로고
    • The carboxyl terminus of Glut4 contains a serine-leucine-leucine sequence that functions as a potent internalization motif in Chinese hamster ovary cells
    • Garippa, R. J., Johnson, A., Park, J., Petrush, R. L. and McGraw, T. E. (1996). The carboxyl terminus of Glut4 contains a serine-leucine-leucine sequence that functions as a potent internalization motif in Chinese hamster ovary cells. J. Biol. Chem. 271, 20660-20668.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20660-20668
    • Garippa, R.J.1    Johnson, A.2    Park, J.3    Petrush, R.L.4    McGraw, T.E.5
  • 23
    • 0030797998 scopus 로고    scopus 로고
    • Linkage of the ubiquitin-conjugating system and the endocytic pathway in ligand-induced internalization of the growth hormone receptor
    • Govers, R., van Kerkhof, P., Schwartz, A. L. and Strous, G. J. (1997). Linkage of the ubiquitin-conjugating system and the endocytic pathway in ligand-induced internalization of the growth hormone receptor. EMBO J. 16, 4851-4858.
    • (1997) EMBO J. , vol.16 , pp. 4851-4858
    • Govers, R.1    Van Kerkhof, P.2    Schwartz, A.L.3    Strous, G.J.4
  • 24
    • 0032568841 scopus 로고    scopus 로고
    • Dileucine-mediated internalization of ligand by a truncated growth hormone receptor is independent of the ubiquitin conjugation system
    • Govers, R., van Kerkhof, P., Schwartz, A. L. and Strous, G. J. (1998). Dileucine-mediated internalization of ligand by a truncated growth hormone receptor is independent of the ubiquitin conjugation system. J. Biol. Chem. 273, 16426-16433.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16426-16433
    • Govers, R.1    Van Kerkhof, P.2    Schwartz, A.L.3    Strous, G.J.4
  • 25
    • 0033521670 scopus 로고    scopus 로고
    • Identification of a novel conjugation motif, required for ligand-induced internalization of the growth hormone receptor
    • Govers, R., ten Broeke, T., van Kerkhof, P., Schwartz, A. L. and Strous, G. J. (1999). Identification of a novel conjugation motif, required for ligand-induced internalization of the growth hormone receptor. EMBO J. 18, 28-36.
    • (1999) EMBO J. , vol.18 , pp. 28-36
    • Govers, R.1    Ten Broeke, T.2    Van Kerkhof, P.3    Schwartz, A.L.4    Strous, G.J.5
  • 26
    • 0031763351 scopus 로고    scopus 로고
    • Analysis of the juxtamembrane dileucine motif in the insulin receptor
    • Haft, C. R., Sierra, N. D. L., Hamer, I., Carpentier, J. L. and Taylor, I. (1998). Analysis of the juxtamembrane dileucine motif in the insulin receptor. Endocrinology 139, 1618-1629.
    • (1998) Endocrinology , vol.139 , pp. 1618-1629
    • Haft, C.R.1    Sierra, N.D.L.2    Hamer, I.3    Carpentier, J.L.4    Taylor, I.5
  • 27
    • 0028971506 scopus 로고
    • Npi1, an essential yeast gene involved in induced degradation of gap1 and fur4 permeases, encodes the rsp5 ubiquitin-protein ligase
    • Hein, C., Springael, J. Y., Volland, C., Haguenauer-Tsapis, R. and André, B. (1995). Npi1, an essential yeast gene involved in induced degradation of gap1 and fur4 permeases, encodes the rsp5 ubiquitin-protein ligase. Mol. Microbiol. 18, 77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 28
    • 0031858995 scopus 로고    scopus 로고
    • Ubiquitination and dimerization of complement receptor type 2 on sheep B cells
    • Hein, W. R., Dudler, L., Marston, W. L., Landsverk, T., Young, A. J. and Avila, D. (1998). Ubiquitination and dimerization of complement receptor type 2 on sheep B cells. J. Immunol. 161, 458-466.
    • (1998) J. Immunol. , vol.161 , pp. 458-466
    • Hein, W.R.1    Dudler, L.2    Marston, W.L.3    Landsverk, T.4    Young, A.J.5    Avila, D.6
  • 30
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke, L. (1997). Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. 11, 1215-1226.
    • (1997) FASEB J. , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 31
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L. and Riezman, H. (1996). Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 32
    • 0031047133 scopus 로고    scopus 로고
    • Catabolite inactivation of the galactose transporter in the yeast Saccharomyces cerevisiae: Ubiquitination, endocytosis and degradation in the vacuole
    • Horak, J. and Wolf, D. H. (1997). Catabolite inactivation of the galactose transporter in the yeast Saccharomyces cerevisiae: Ubiquitination, endocytosis and degradation in the vacuole. J. Bacteriol. 179, 1541-1549.
    • (1997) J. Bacteriol. , vol.179 , pp. 1541-1549
    • Horak, J.1    Wolf, D.H.2
  • 33
    • 0031045984 scopus 로고    scopus 로고
    • Degradation of the met tyrosine kinase receptor by the ubiquitin-proteasome pathway
    • Jeffers, M., Taylor, G. A., Weidner, K. M., Omura, S. and Vandewoude, G. F. (1997). Degradation of the met tyrosine kinase receptor by the ubiquitin-proteasome pathway. Mol. Cell Biol. 17, 799-808.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 799-808
    • Jeffers, M.1    Taylor, G.A.2    Weidner, K.M.3    Omura, S.4    Vandewoude, G.F.5
  • 34
    • 0029937513 scopus 로고    scopus 로고
    • The 'destruction box' of cyclin A allows B-type cyclins to be ubiquitinated, but not efficiently destroyed
    • Klotzbucher, A., Stewart, E., Harrison, D. and Hunt, T. (1996). The 'destruction box' of cyclin A allows B-type cyclins to be ubiquitinated, but not efficiently destroyed. EMBO J. 15, 3053-3064.
    • (1996) EMBO J. , vol.15 , pp. 3053-3064
    • Klotzbucher, A.1    Stewart, E.2    Harrison, D.3    Hunt, T.4
  • 35
    • 0028277963 scopus 로고
    • The ABC-transpporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kölling, R. and Hollenberg, C. P. (1994). The ABC-transpporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13, 3261-3271.
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Kölling, R.1    Hollenberg, C.P.2
  • 36
    • 0040123316 scopus 로고    scopus 로고
    • The linker region of this ABC-transporter ste6 mediates ubiquitination and fast turnover of the protein
    • Kölling, R. and Losko, S. (1997). The linker region of this ABC-transporter ste6 mediates ubiquitination and fast turnover of the protein. EMBO J. 16, 2251-2261.
    • (1997) EMBO J. , vol.16 , pp. 2251-2261
    • Kölling, R.1    Losko, S.2
  • 37
    • 0025098673 scopus 로고
    • Ubiquitinated protein conjugates are specifically enriched in the lysosomal system of fibroblasts
    • Laszlo, L., Doherty, F. J., Osborn, N. U. and Mayer, R. J. (1990). Ubiquitinated protein conjugates are specifically enriched in the lysosomal system of fibroblasts. FEBS Lett. 261, 365-368.
    • (1990) FEBS Lett. , vol.261 , pp. 365-368
    • Laszlo, L.1    Doherty, F.J.2    Osborn, N.U.3    Mayer, R.J.4
  • 38
    • 0026690834 scopus 로고
    • Ubiquitin-activating enzyme, E1, is associated with maturation of autophagic vacuoles
    • Lenk, S. E., Dunn, W. A., Trausch, J. S., Ciechanover, A. and Schwartz, A. L. (1992). Ubiquitin-activating enzyme, E1, is associated with maturation of autophagic vacuoles. J. Cell Biol. 118, 301-308.
    • (1992) J. Cell Biol. , vol.118 , pp. 301-308
    • Lenk, S.E.1    Dunn, W.A.2    Trausch, J.S.3    Ciechanover, A.4    Schwartz, A.L.5
  • 40
    • 0031055949 scopus 로고    scopus 로고
    • Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4
    • Lucero, P. and Lagunas, R. (1997). Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4. FEMS Microbiol. Lett. 147, 273-277.
    • (1997) FEMS Microbiol. Lett. , vol.147 , pp. 273-277
    • Lucero, P.1    Lagunas, R.2
  • 41
    • 0031961993 scopus 로고    scopus 로고
    • A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease
    • Marchal, C., Haguenauer-Tsapis, R. and Urbangrimal, D. (1998). A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease. Mol. Cell Biol. 18, 314-321.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 314-321
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urbangrimal, D.3
  • 42
    • 0031106781 scopus 로고    scopus 로고
    • Protein sorting by tyrosine-based signals: Adapting to the Ys and wherefores
    • Marks, M. S., Ohno, H., Kirchhausen, T. and Bonifacino, S. J. (1997). Protein sorting by tyrosine-based signals: adapting to the Ys and wherefores. Trends Cell Biol. 7, 124-128.
    • (1997) Trends Cell Biol. , vol.7 , pp. 124-128
    • Marks, M.S.1    Ohno, H.2    Kirchhausen, T.3    Bonifacino, S.J.4
  • 43
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. (1996). Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12, 575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 44
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185(c-erbB-2) receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh, E. G., Chavany, C. and Neckers, L. (1996). Polyubiquitination and proteasomal degradation of the p185(c-erbB-2) receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796-22801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 45
    • 0032493444 scopus 로고    scopus 로고
    • The tyrosine kinase regulator Cb1 enhances the ubiquitination and degradation of the platelet-derived growth factor receptor α
    • Miyake, S., Lupher, M. L., Druker, B. and Band, H. (1998). The tyrosine kinase regulator Cb1 enhances the ubiquitination and degradation of the platelet-derived growth factor receptor α. Proc. Nat. Acad. Sci. USA 95, 7927-7932.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 7927-7932
    • Miyake, S.1    Lupher, M.L.2    Druker, B.3    Band, H.4
  • 46
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product: A possible mechanism of receptor down regulation in M107e cells
    • Miyazawa, K., Toyama, K., Gotoh, A., Hendrie, P. C., Mantel, C. and Broxmeyer, H. E. (1994). Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down regulation in M107e cells. Blood 83, 137-145.
    • (1994) Blood , vol.83 , pp. 137-145
    • Miyazawa, K.1    Toyama, K.2    Gotoh, A.3    Hendrie, P.C.4    Mantel, C.5    Broxmeyer, H.E.6
  • 47
    • 0030813921 scopus 로고    scopus 로고
    • The yeast actin-related protein Arp2p is required for the internalization step of endocytosis
    • Moreau, V., Galan, J. M., Devilliers, G., Haguenauer-Tsapis, R. and Winsor, B. (1997). The yeast actin-related protein Arp2p is required for the internalization step of endocytosis. Mol. Biol. Cell 8, 1361-1375.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1361-1375
    • Moreau, V.1    Galan, J.M.2    Devilliers, G.3    Haguenauer-Tsapis, R.4    Winsor, B.5
  • 48
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori, S., Heldin, C. H. and Claesson-Welsh, L. (1992). Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor. J. Biol. Chem. 267, 6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 49
    • 0027997221 scopus 로고
    • A tyrosine residue in the juxtamembrane segment of the platelet-derived growth factor β-receptor is critical for ligand-mediated endocytosis
    • Mori, S., Ronnstrand, L., Claesson-Welsh, L. and Heldin, C. H. (1994). A tyrosine residue in the juxtamembrane segment of the platelet-derived growth factor β-receptor is critical for ligand-mediated endocytosis. J. Biol. Chem. 269, 4917-4921.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4917-4921
    • Mori, S.1    Ronnstrand, L.2    Claesson-Welsh, L.3    Heldin, C.H.4
  • 51
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquitin-proteasome proteolytic pathway
    • Mori, S., Tanaka, K., Omura, S. and Saito, Y. (1995b). Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquitin-proteasome proteolytic pathway. J. Biol. Chem. 270, 29447-29452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 53
    • 0021209107 scopus 로고
    • The mouse fibroblast growth hormone receptor: Ligand processing and receptor modulation and turnover
    • Murphy, L. J. and Lazarus, L. (1984). The mouse fibroblast growth hormone receptor: ligand processing and receptor modulation and turnover. Endocrinology 115, 1625-1632.
    • (1984) Endocrinology , vol.115 , pp. 1625-1632
    • Murphy, L.J.1    Lazarus, L.2
  • 54
    • 0032192447 scopus 로고    scopus 로고
    • Strange bedfellows? Protein degradation and neurological dysfunction
    • Nicholls, R. D. (1998). Strange bedfellows? Protein degradation and neurological dysfunction. Neuron 21, 647-649.
    • (1998) Neuron , vol.21 , pp. 647-649
    • Nicholls, R.D.1
  • 55
    • 0029942123 scopus 로고    scopus 로고
    • Ubiquitinylation and ubiquitin-dependent proteolysis in vertebrate photoreceptors (rod outer segments) - Evidence for ubiquitinylation of g(t) and rhodopsin
    • Obin, M. S., Jahngenhodge, J., Nowell, T. and Taylor, A. (1996). Ubiquitinylation and ubiquitin-dependent proteolysis in vertebrate photoreceptors (rod outer segments) - evidence for ubiquitinylation of g(t) and rhodopsin. J. Biol. Chem. 271, 14473-14484.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14473-14484
    • Obin, M.S.1    Jahngenhodge, J.2    Nowell, T.3    Taylor, A.4
  • 56
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D. and Evans, P. R. (1998). A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282, 1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.1    Evans, P.R.2
  • 57
    • 0027458572 scopus 로고
    • Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors
    • Paolini, R. and Kinet, J. P. (1993). Cell surface control of the multiubiquitination and deubiquitination of high-affinity immunoglobulin E receptors. EMBO J. 12, 779-786.
    • (1993) EMBO J. , vol.12 , pp. 779-786
    • Paolini, R.1    Kinet, J.P.2
  • 60
    • 0029781462 scopus 로고    scopus 로고
    • Ubiquitination of the yeast a-factor receptor
    • Roth, A. F. and Davis, N. G. (1996). Ubiquitination of the yeast a-factor receptor. J. Cell Biol. 134, 661-674.
    • (1996) J. Cell Biol. , vol.134 , pp. 661-674
    • Roth, A.F.1    Davis, N.G.2
  • 61
    • 0032563560 scopus 로고    scopus 로고
    • A large PEST-like sequence directs the ubiquitination, endocytosis and vacuolar degradation of the yeast a-factor receptor
    • Roth, A. F., Sullivan, D. M. and Davis, N. G. (1998). A large PEST-like sequence directs the ubiquitination, endocytosis and vacuolar degradation of the yeast a-factor receptor. J. Cell Biol. 142, 949-961.
    • (1998) J. Cell Biol. , vol.142 , pp. 949-961
    • Roth, A.F.1    Sullivan, D.M.2    Davis, N.G.3
  • 62
    • 0029948974 scopus 로고    scopus 로고
    • Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome
    • Schild, L., Lu, Y., Gautschi, I., Schneeberger, E., Lifton, R. P. and Rossier, B. C. (1996). Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome. EMBO J. 15, 2381-2387.
    • (1996) EMBO J. , vol.15 , pp. 2381-2387
    • Schild, L.1    Lu, Y.2    Gautschi, I.3    Schneeberger, E.4    Lifton, R.P.5    Rossier, B.C.6
  • 63
    • 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
  • 64
    • 0030820814 scopus 로고    scopus 로고
    • The activity of the epithelial sodium channel is regulated by clathrin-mediated endocytosis
    • Shimkets, R. A., Lifton, R. P. and Canessa, C. M. (1997). The activity of the epithelial sodium channel is regulated by clathrin-mediated endocytosis. J. Biol. Chem. 272, 25537-25541.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25537-25541
    • Shimkets, R.A.1    Lifton, R.P.2    Canessa, C.M.3
  • 65
    • 0025779089 scopus 로고
    • Phosphorylation-dependent down-modulation of CD4 requires a specific structure within the cytoplasmic domain of CD4
    • Shin, J., Dunbrack, R. L., Lee, J. S. and Strominger, J. L. (1991). Phosphorylation-dependent down-modulation of CD4 requires a specific structure within the cytoplasmic domain of CD4. J. Biol. Chem. 266, 10658-10665.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10658-10665
    • Shin, J.1    Dunbrack, R.L.2    Lee, J.S.3    Strominger, J.L.4
  • 66
    • 0022644026 scopus 로고
    • Cell surface molecule associated with lymphocyte homing is a ubiquitinated branched-chain glycoprotein
    • Siegelman, M., Bond, M. W., Gallatin, W. M., St. John, T., Smith, H. T., Fried, V. A. and Weissman, I. L. (1986). Cell surface molecule associated with lymphocyte homing is a ubiquitinated branched-chain glycoprotein. Science 231, 823-829.
    • (1986) Science , vol.231 , pp. 823-829
    • Siegelman, M.1    Bond, M.W.2    Gallatin, W.M.3    St. John, T.4    Smith, H.T.5    Fried, V.A.6    Weissman, I.L.7
  • 67
    • 0025043480 scopus 로고
    • The asialoglycoprotein receptor: A model for endocytic transport receptors
    • Spiess, M. (1990). The asialoglycoprotein receptor: a model for endocytic transport receptors. Biochemistry 29, 10009-10018.
    • (1990) Biochemistry , vol.29 , pp. 10009-10018
    • Spiess, M.1
  • 68
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na channel deleted in Liddle's syndrome
    • Staub, O., Dho, S., Henry, P. C., Correa, J., Ishikawa, T., McGlade, J. and Torin, D. (1996). WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na channel deleted in Liddle's syndrome. EMBO J. 15, 2371-2380.
    • (1996) EMBO J. , vol.15 , pp. 2371-2380
    • Staub, O.1    Dho, S.2    Henry, P.C.3    Correa, J.4    Ishikawa, T.5    McGlade, J.6    Torin, D.7
  • 69
    • 0030731428 scopus 로고    scopus 로고
    • Regulation of stability and function of the epithelial Na-channel (ENaC) by ubiquitination
    • Staub, O., Gautschi, I., Ishikawa, T., Breitschopf, K., Ciechanover, A., Schild, L. and Rotin, D. (1997). Regulation of stability and function of the epithelial Na-channel (ENaC) by ubiquitination. EMBO J. 16, 6325-6336.
    • (1997) EMBO J. , vol.16 , pp. 6325-6336
    • Staub, O.1    Gautschi, I.2    Ishikawa, T.3    Breitschopf, K.4    Ciechanover, A.5    Schild, L.6    Rotin, D.7
  • 70
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G. J., van Kerkhof, P., Govers, R., Ciechanover, A. and Schwartz, A. L. (1996). The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 15, 3806-3812.
    • (1996) EMBO J. , vol.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 71
    • 0028957771 scopus 로고
    • The conserved box 1 motif of cytokine receptors is required for association with jak kinases
    • Tanner, J. W., Chen, W., Young, R. L., Longmore, G. D. and Shaw, A. S. (1995). The conserved box 1 motif of cytokine receptors is required for association with jak kinases. J. Biol. Chem. 270, 6523-6530.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6523-6530
    • Tanner, J.W.1    Chen, W.2    Young, R.L.3    Longmore, G.D.4    Shaw, A.S.5
  • 72
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell, J., Shih, S., Dunn, R. and Hicke, L. (1998). A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1, 193-202.
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 73
    • 0026200357 scopus 로고
    • Endocytosis and signals for internalization
    • Trowbridge, I. S. (1991). Endocytosis and signals for internalization. Curr. Opin. Cell Biol. 3, 634-641.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 634-641
    • Trowbridge, I.S.1
  • 74
    • 0031029722 scopus 로고    scopus 로고
    • Association and colocalization of eps15 with adaptor protein-2 and clathrin
    • van Delft, S., Schumacher, C., Hage, W., Verkleij, A. J. and Henegouwen, P. M. (1997a). Association and colocalization of eps15 with adaptor protein-2 and clathrin. J. Cell Biol. 136, 811-821.
    • (1997) J. Cell Biol. , vol.136 , pp. 811-821
    • Van Delft, S.1    Schumacher, C.2    Hage, W.3    Verkleij, A.J.4    Henegouwen, P.M.5
  • 76
    • 0030058105 scopus 로고    scopus 로고
    • c-Cb1 is transiently tyrosine-phosphorylated, ubiquitinated and membrane-targeted following CSF-1 stimulation of macrophages
    • Wang, Y., Yeung, Y.-G., Langdon, W. Y. and Stanley, E. R. (1996). c-Cb1 is transiently tyrosine-phosphorylated, ubiquitinated and membrane-targeted following CSF-1 stimulation of macrophages. J. Biol. Chem. 271, 17-20.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17-20
    • Wang, Y.1    Yeung, Y.-G.2    Langdon, W.Y.3    Stanley, E.R.4
  • 77
    • 12044249985 scopus 로고
    • Cytokine signal transduction and the JAK family of protein tyrosine kinases
    • Wilks, A. F. and Harpur, A. G. (1994). Cytokine signal transduction and the JAK family of protein tyrosine kinases. BioEssays 16, 313-320.
    • (1994) BioEssays , vol.16 , pp. 313-320
    • Wilks, A.F.1    Harpur, A.G.2
  • 78
    • 0023653206 scopus 로고
    • Structure and proteolysis of the growth hormone receptor on rat hepatocytes
    • Yamada, K., Lipson, K. E. and Donner, D. B. (1987). Structure and proteolysis of the growth hormone receptor on rat hepatocytes. Biochemistry 26, 4438-4443.
    • (1987) Biochemistry , vol.26 , pp. 4438-4443
    • Yamada, K.1    Lipson, K.E.2    Donner, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.