메뉴 건너뛰기




Volumn 142, Issue 4, 1998, Pages 923-936

An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells

Author keywords

Endocytosis; Endosome; Protein sorting; Trans Golgi network

Indexed keywords

ANIMAL CELL; ARTICLE; BINDING KINETICS; CHO CELL; CONFOCAL MICROSCOPY; ENDOCYTOSIS; MICROSCOPIC ANATOMY; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; QUANTITATIVE DIAGNOSIS; STEADY STATE;

EID: 0032563568     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.142.4.923     Document Type: Article
Times cited : (214)

References (52)
  • 1
    • 0031052040 scopus 로고    scopus 로고
    • TGN38 and its orthologues: Roles in post-TGN vesicle formation and maintenance of TGN morphology
    • Banting, G., and S. Ponnambalam. 1997. TGN38 and its orthologues: roles in post-TGN vesicle formation and maintenance of TGN morphology. Biochim. Biophys. Acta. 1355:209-217.
    • (1997) Biochim. Biophys. Acta , vol.1355 , pp. 209-217
    • Banting, G.1    Ponnambalam, S.2
  • 2
    • 0019865351 scopus 로고
    • Exocytosis of pinocytosed fluid in cultured cells: Kinetic evidence for rapid turnover and compartmentation
    • Besterman, J.M., J.A. Airhart, R.C. Woodworth, and R.B. Low. 1981. Exocytosis of pinocytosed fluid in cultured cells: kinetic evidence for rapid turnover and compartmentation. J. Cell Biol. 91:716-727.
    • (1981) J. Cell Biol. , vol.91 , pp. 716-727
    • Besterman, J.M.1    Airhart, J.A.2    Woodworth, R.C.3    Low, R.B.4
  • 3
    • 0027159260 scopus 로고
    • TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain
    • Bos, K., C. Wraight, and K.K. Stanley. 1993. TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain. EMBO (Eur. Mol. Biol. Organ.) J. 12:2219-2228.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 2219-2228
    • Bos, K.1    Wraight, C.2    Stanley, K.K.3
  • 5
    • 0026535445 scopus 로고
    • Delivery of ligands from sorting endosomes to late endosomes occurs by maturation of sorting endosomes
    • Dunn, K.W., and F.R. Maxfield. 1992. Delivery of ligands from sorting endosomes to late endosomes occurs by maturation of sorting endosomes. J. Cell Biol. 117:301-310.
    • (1992) J. Cell Biol. , vol.117 , pp. 301-310
    • Dunn, K.W.1    Maxfield, F.R.2
  • 6
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn, K.W., T.E. McGraw, and F.R. Maxfield. 1989. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J. Cell Biol. 109:3303-3314.
    • (1989) J. Cell Biol. , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 7
    • 0021103957 scopus 로고
    • Multiple pathways of exocytosis, endocytosis, and membrane recycling: Validation of a Golgi route
    • Farquhar, M.G. 1983. Multiple pathways of exocytosis, endocytosis, and membrane recycling: validation of a Golgi route. Fed. Proc. 42:2407-2413.
    • (1983) Fed. Proc. , vol.42 , pp. 2407-2413
    • Farquhar, M.G.1
  • 8
    • 0026574126 scopus 로고
    • Kinetics of binding, endocytosis, and recycling of EGF receptor mutants
    • Felder, S., J. LaVin, A. Ullrich, and J. Schlessinger. 1992. Kinetics of binding, endocytosis, and recycling of EGF receptor mutants. J. Cell Biol. 117: 203-212.
    • (1992) J. Cell Biol. , vol.117 , pp. 203-212
    • Felder, S.1    Lavin, J.2    Ullrich, A.3    Schlessinger, J.4
  • 9
    • 0028085865 scopus 로고
    • Quantification of low density lipoprotein and transferrin endocytic sorting in HEp2 cells using confocal microscopy
    • Ghosh, R.N., D.L. Gelman, and F.R. Maxfield. 1994. Quantification of low density lipoprotein and transferrin endocytic sorting in HEp2 cells using confocal microscopy. J. Cell Sci. 107:2177-2189.
    • (1994) J. Cell Sci. , vol.107 , pp. 2177-2189
    • Ghosh, R.N.1    Gelman, D.L.2    Maxfield, F.R.3
  • 10
    • 0028890380 scopus 로고
    • Evidence for nonvectorial, retrograde transferrin trafficking in the early endosomes of HEp2 cells
    • Ghosh, R.N., and F.R. Maxfield. 1995. Evidence for nonvectorial, retrograde transferrin trafficking in the early endosomes of HEp2 cells. J. Cell Biol. 128:549-561.
    • (1995) J. Cell Biol. , vol.128 , pp. 549-561
    • Ghosh, R.N.1    Maxfield, F.R.2
  • 11
    • 0026528446 scopus 로고
    • Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC12 cells
    • Green, S.A., and R.B. Kelly. 1992. Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC12 cells. J. Cell Biol. 117:47-55.
    • (1992) J. Cell Biol. , vol.117 , pp. 47-55
    • Green, S.A.1    Kelly, R.B.2
  • 12
    • 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
  • 15
    • 0027395956 scopus 로고
    • Localization of TGN38 to the trans-Golgi network: Involvement of a cytoplasmic tyrosine containing sequence
    • Humphrey, J.S., P.J. Peters, L.C. Yuan, and J.S. Bonifacino. 1993. Localization of TGN38 to the trans-Golgi network: involvement of a cytoplasmic tyrosine containing sequence. J. Cell Biol. 120:1123-1135.
    • (1993) J. Cell Biol. , vol.120 , pp. 1123-1135
    • Humphrey, J.S.1    Peters, P.J.2    Yuan, L.C.3    Bonifacino, J.S.4
  • 16
    • 0028230349 scopus 로고
    • Insulin stimulation of GLUT-4 translocation: A model for regulated recycling
    • James, D.E., R.C. Piper, and J.W. Slot. 1994. Insulin stimulation of GLUT-4 translocation: a model for regulated recycling. Trends Cell Biol. 4:120-126.
    • (1994) Trends Cell Biol. , vol.4 , pp. 120-126
    • James, D.E.1    Piper, R.C.2    Slot, J.W.3
  • 17
    • 0024603422 scopus 로고
    • Transport of surface mannose 6-phosphate receptor to the Golgi complex in cultured human cells
    • Jin, M., G.G. Sahagian, and M.D. Snider. 1989. Transport of surface mannose 6-phosphate receptor to the Golgi complex in cultured human cells. J. Biol. Chem. 264:7675-7680.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7675-7680
    • Jin, M.1    Sahagian, G.G.2    Snider, M.D.3
  • 18
    • 0030474309 scopus 로고    scopus 로고
    • Transferrin receptor containing the SDYQRL motif of TGN38 causes a reorganization of the recycling compartment but is not targeted to the TGN
    • Johnson, A.O., R.N. Ghosh, K.W. Dunn, R. Garippa, G. Park, S. Mayor, F.R. Maxfield, and T.E. McGraw. 1996. Transferrin receptor containing the SDYQRL motif of TGN38 causes a reorganization of the recycling compartment but is not targeted to the TGN. J. Cell Biol. 135:1749-1762.
    • (1996) J. Cell Biol. , vol.135 , pp. 1749-1762
    • Johnson, A.O.1    Ghosh, R.N.2    Dunn, K.W.3    Garippa, R.4    Park, G.5    Mayor, S.6    Maxfield, F.R.7    McGraw, T.E.8
  • 19
    • 0026757062 scopus 로고
    • The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi
    • Johnson, K.F., and S. Kornfeld. 1992. The cytoplasmic tail of the mannose 6-phosphate/insulin-like growth factor-II receptor has two signals for lysosomal enzyme sorting in the Golgi. J. Cell Biol. 119:249-257.
    • (1992) J. Cell Biol. , vol.119 , pp. 249-257
    • Johnson, K.F.1    Kornfeld, S.2
  • 20
    • 0026806542 scopus 로고
    • A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function
    • Johnson, K.F., and S. Kornfeld. 1992. A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor is necessary for the lysosomal enzyme sorting function. J. Biol. Chem. 267:17110-17115.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17110-17115
    • Johnson, K.F.1    Kornfeld, S.2
  • 21
    • 0028866530 scopus 로고
    • Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail
    • Jones, B.C., L. Thomas, S.S. Molloy, C.D. Thulin, M.D. Fry, K.A. Walsh, and G. Thomas. 1995. Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail. EMBO (Eur. Mol. Biol. Organ.) J. 14:5869-5883.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 5869-5883
    • Jones, B.C.1    Thomas, L.2    Molloy, S.S.3    Thulin, C.D.4    Fry, M.D.5    Walsh, K.A.6    Thomas, G.7
  • 22
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors
    • Kornfeld, S. 1992. Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors. Annu. Rev. Biochem. 61:307-330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 23
    • 0026472647 scopus 로고
    • The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A
    • Ladinsky, M.S., and K.E. Howell. 1992. The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A. Eur. J. Cell Biol. 59:92-105.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 92-105
    • Ladinsky, M.S.1    Howell, K.E.2
  • 24
    • 0027727324 scopus 로고
    • An electron microscopy study of TGN38/41 dynamics
    • Ladinsky, M.S., and K.E. Howell. 1993. An electron microscopy study of TGN38/41 dynamics. J. Cell Sci. 17(Suppl.):41-47.
    • (1993) J. Cell Sci. , vol.17 , Issue.SUPPL. , pp. 41-47
    • Ladinsky, M.S.1    Howell, K.E.2
  • 25
    • 0024807218 scopus 로고
    • Ligand-mediated internalization, recycling, and downregulation of the epidermal growth factor receptor in vivo
    • Lai, W.H., P.H. Cameron, I. Wada, J.J. Doherty II, D.G. Kay, B.I. Posner, and J.J. Bergeron. 1989. Ligand-mediated internalization, recycling, and downregulation of the epidermal growth factor receptor in vivo. J. Cell Biol. 109:2741-2749.
    • (1989) J. Cell Biol. , vol.109 , pp. 2741-2749
    • Lai, W.H.1    Cameron, P.H.2    Wada, I.3    Doherty II, J.J.4    Kay, D.G.5    Posner, B.I.6    Bergeron, J.J.7
  • 26
    • 0025940101 scopus 로고
    • Brefeldin A's effects on endosomes, lysosomes and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., L. Yuan. C. Tipper, M. Amherdt, L. Orci, and R.D. Klausner. 1991. Brefeldin A's effects on endosomes, lysosomes and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell. 67:601-616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.D.6
  • 27
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)
    • Luzio, J.P., B. Brake, G. Banting, K. Howell, P. Braghetta, and K.K. Stanley. 1990. Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). Biochem. J. 270:97-102.
    • (1990) Biochem. J. , vol.270 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.4    Braghetta, P.5    Stanley, K.K.6
  • 28
    • 0029050487 scopus 로고
    • Oligomerized transferrin receptors are selectively retained by a lumenal sorting signal in a long-lived endocytic recycling compartment
    • Marsh, E.W., P.L. Leopold, N.L. Jones, and F.R. Maxfield. 1995. Oligomerized transferrin receptors are selectively retained by a lumenal sorting signal in a long-lived endocytic recycling compartment. J. Cell Biol. 129:1509-1522.
    • (1995) J. Cell Biol. , vol.129 , pp. 1509-1522
    • Marsh, E.W.1    Leopold, P.L.2    Jones, N.L.3    Maxfield, F.R.4
  • 29
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor, S., J.F. Presley, and F.R. Maxfield. 1993. Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol. 121:1257-1269.
    • (1993) J. Cell Biol. , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 31
    • 0023243675 scopus 로고
    • Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor
    • McGraw, T.E., L. Greenfield, and F.R. Maxfield. 1987. Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. J. Cell Biol. 105:207-214.
    • (1987) J. Cell Biol. , vol.105 , pp. 207-214
    • McGraw, T.E.1    Greenfield, L.2    Maxfield, F.R.3
  • 32
    • 0025402516 scopus 로고
    • Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain
    • McGraw, T.E., and F.R. Maxfield. 1990. Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain. Cell Regul. 1:369-377.
    • (1990) Cell Regul. , vol.1 , pp. 369-377
    • McGraw, T.E.1    Maxfield, F.R.2
  • 33
    • 0026095523 scopus 로고
    • Functional expression of furin demonstrating its intracellular localization and endoprotease activity for processing of proalbumin and complement pro-C3
    • Misumi, Y., K. Oda, T. Fujiwara, N. Takami, K. Tachiro, and Y. Ikehara. 1991. Functional expression of furin demonstrating its intracellular localization and endoprotease activity for processing of proalbumin and complement pro-C3. J. Biol. Chem. 266:16954-16959.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16954-16959
    • Misumi, Y.1    Oda, K.2    Fujiwara, T.3    Takami, N.4    Tachiro, K.5    Ikehara, Y.6
  • 34
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localization to the TGN and recycling from the cell surface
    • Molloy, S.S., L. Thomas, J.K. VanSlyke, P.E. Stenberg, and G. Thomas. 1994. Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. EMBO (Eur. Mol. Biol. Organ.) J. 13:18-33.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    Vanslyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 36
    • 0028916337 scopus 로고
    • Endocytosis and lysosomal targeting of epidermal growth factor receptors are mediated by distinct sequences independent of the tyrosine kinase domain
    • Opresko, L.K., C.P. Chang, B.H. Will, P.M. Burke, G.N. Gill, and H.S. Wiley. 1995. Endocytosis and lysosomal targeting of epidermal growth factor receptors are mediated by distinct sequences independent of the tyrosine kinase domain. J. Biol. Chem. 270:4325-4333.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4325-4333
    • Opresko, L.K.1    Chang, C.P.2    Will, B.H.3    Burke, P.M.4    Gill, G.N.5    Wiley, H.S.6
  • 37
    • 0024470450 scopus 로고
    • Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: Interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy
    • Pagano, R.E., M.A. Sepanski, and O.C. Martin. 1989. Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy. J Cell Biol. 109:2067-2079.
    • (1989) J Cell Biol. , vol.109 , pp. 2067-2079
    • Pagano, R.E.1    Sepanski, M.A.2    Martin, O.C.3
  • 38
    • 0028351154 scopus 로고
    • The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
    • Ponnambalam, S., C. Rabouille, J.P. Luzio, T. Nilsson, and G. Warren. 1994. The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network. J. Cell Biol. 125:253-268.
    • (1994) J. Cell Biol. , vol.125 , pp. 253-268
    • Ponnambalam, S.1    Rabouille, C.2    Luzio, J.P.3    Nilsson, T.4    Warren, G.5
  • 39
    • 0027203163 scopus 로고
    • The End2 mutation in CHO cells slows the rate of exit of transferrin receptors from the recycling compartment but bulk membrane recycling is unaffected
    • Presley, J.F., S. Mayor, K.W. Dunn, L.S. Johnson, T.E. McGraw, and F.R. Maxfield. 1993. The End2 mutation in CHO cells slows the rate of exit of transferrin receptors from the recycling compartment but bulk membrane recycling is unaffected. J. Cell Biol. 122:1231-1241.
    • (1993) J. Cell Biol. , vol.122 , pp. 1231-1241
    • Presley, J.F.1    Mayor, S.2    Dunn, K.W.3    Johnson, L.S.4    McGraw, T.E.5    Maxfield, F.R.6
  • 41
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: Brefeldin a affects its rate of return to the TGN
    • Reaves, B., M. Horn, and G. Banting. 1993. TGN38/41 recycles between the cell surface and the TGN: Brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell. 4:93-105.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 42
    • 0023887115 scopus 로고
    • Intracellular fusion of sequentially formed endocytic compartments
    • Salzman, N.H., and F.R. Maxfield. 1988. Intracellular fusion of sequentially formed endocytic compartments. J. Cell Biol. 106:1083-1091.
    • (1988) J. Cell Biol. , vol.106 , pp. 1083-1091
    • Salzman, N.H.1    Maxfield, F.R.2
  • 43
    • 0024454465 scopus 로고
    • Fusion accessibility of endocytic compartments along the recycling and lysosomal endocytic pathway in intact cells
    • Salzman, N.H., and F.R. Maxfield. 1989. Fusion accessibility of endocytic compartments along the recycling and lysosomal endocytic pathway in intact cells. J. Cell Biol. 109:2097-2104.
    • (1989) J. Cell Biol. , vol.109 , pp. 2097-2104
    • Salzman, N.H.1    Maxfield, F.R.2
  • 44
    • 0021955354 scopus 로고
    • Intracellular movement of cell surface receptors after endocytosis: Resialylation of asialo-transferrin receptor in human crythroleukemia cells
    • Snider, M.D., and O.C. Rogers. 1985. Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human crythroleukemia cells. J. Cell Biol. 100:826-834.
    • (1985) J. Cell Biol. , vol.100 , pp. 826-834
    • Snider, M.D.1    Rogers, O.C.2
  • 45
    • 0027178838 scopus 로고
    • TGN38/41: A molecule on the move
    • Stanley, K.K., and K.E. Howell. 1993. TGN38/41: a molecule on the move. Trends Cell Biol. 3:252-255.
    • (1993) Trends Cell Biol. , vol.3 , pp. 252-255
    • Stanley, K.K.1    Howell, K.E.2
  • 46
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich, O., S. Reinsch, S. Urbe, M. Zerial, and R.G. Parton. 1996. Rab11 regulates recycling through the pericentriolar recycling endosome J Cell Biol. 135:913-924.
    • (1996) J Cell Biol. , vol.135 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 47
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells
    • Urbe, S., L.A. Huber, M. Zerial, S.A. Tooze, and R.G. Parton. 1993. Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells. FEBS Lett. 334:175-182.
    • (1993) FEBS Lett. , vol.334 , pp. 175-182
    • Urbe, S.1    Huber, L.A.2    Zerial, M.3    Tooze, S.A.4    Parton, R.G.5
  • 48
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • Voorhees, P., E. Deignan, E.V. Donselaar, J. Humphrey, M.S. Marks, P.J. Peters, and J.S. Bonifacino. 1995. An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO (Eur. Mol. Biol. Organ.) J. 14:4961-4975.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 4961-4975
    • Voorhees, P.1    Deignan, E.2    Donselaar, E.V.3    Humphrey, J.4    Marks, M.S.5    Peters, P.J.6    Bonifacino, J.S.7
  • 49
    • 0019945866 scopus 로고
    • The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis
    • Wiley, H.S., and D.D. Cunningham. 1982. The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis. J. Biol. Chem. 257:4222-4229.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4222-4229
    • Wiley, H.S.1    Cunningham, D.D.2
  • 50
    • 0027519431 scopus 로고
    • The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization
    • Wong, S.H., and W. Hong. 1993. The SXYQRL sequence in the cytoplasmic domain of TGN38 plays a major role in trans-Golgi network localization. J. Biol. Chem. 268:22853-22862.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22853-22862
    • Wong, S.H.1    Hong, W.2
  • 51
    • 0025943380 scopus 로고
    • Brefeldin a causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes
    • Wood, S.A., J.E. Park, and W.J. Brown. 1991. Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes. Cell. 67:591-600.
    • (1991) Cell , vol.67 , pp. 591-600
    • Wood, S.A.1    Park, J.E.2    Brown, W.J.3
  • 52
    • 0021734410 scopus 로고
    • Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway
    • Yamashiro, D.J., B. Tycko, S.R. Fluss, and F.R. Maxfield. 1984. Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway. Cell. 37:789-800.
    • (1984) Cell , vol.37 , pp. 789-800
    • Yamashiro, D.J.1    Tycko, B.2    Fluss, S.R.3    Maxfield, F.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.