메뉴 건너뛰기




Volumn 132, Issue 4, 1996, Pages 523-536

The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE TRIPHOSPHATE; CLATHRIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); PEPTIDE; PROTEIN;

EID: 0030051441     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.132.4.523     Document Type: Article
Times cited : (146)

References (57)
  • 1
    • 0024317024 scopus 로고
    • Identification of a clathrin binding subunit in the HA2 adaptor protein complex
    • Ahle, S., and E. Ungewickell. 1989. Identification of a clathrin binding subunit in the HA2 adaptor protein complex. J. Biol Chem. 264:20089-20093.
    • (1989) J. Biol Chem. , vol.264 , pp. 20089-20093
    • Ahle, S.1    Ungewickell, E.2
  • 2
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane
    • Ahle, S., A Mann, U. Eichelsbacher, and E. Ungewickell. 1988. Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane. EMBO (Eur. Mol. Biol. Organ.) J. 7:919-929
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickell, E.4
  • 3
    • 0027299702 scopus 로고
    • Dissecting clathrin-coated pits
    • Anderson, R.G.W. 1993 Dissecting clathrin-coated pits Trends Cell Biol. 3: 177-179.
    • (1993) Trends Cell Biol. , vol.3 , pp. 177-179
    • Anderson, R.G.W.1
  • 4
    • 0027639817 scopus 로고
    • Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles
    • Bauerfeind, R., and W.B. Huttner. 1993. Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles. Curr. Opin. Cell Biol. 5: 628-635.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 628-635
    • Bauerfeind, R.1    Huttner, W.B.2
  • 5
    • 0028904466 scopus 로고
    • Arf proteins: The membrane traffic police?
    • Boman, A.L., and R.A. Kahn. 1995. Arf proteins: the membrane traffic police? Trends Biol Sci 20:147-150.
    • (1995) Trends Biol Sci , vol.20 , pp. 147-150
    • Boman, A.L.1    Kahn, R.A.2
  • 6
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T.L., and R.B. Kelly. 1987. Constitutive and regulated secretion of proteins Annu. Rev. Cell Biol. 3:243-293.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 7
    • 0026239981 scopus 로고
    • What the granins tell us about the formation of secretory granules in neuroendocrine cells
    • Chanat, E., S.W Pimplikar, J.C. Stinchcombe, and W.B. Huttner. 1992. What the granins tell us about the formation of secretory granules in neuroendocrine cells Cell Biophysics 19:85-91.
    • (1992) Cell Biophysics , vol.19 , pp. 85-91
    • Chanat, E.1    Pimplikar, S.W.2    Stinchcombe, J.C.3    Huttner, W.B.4
  • 8
    • 0027207340 scopus 로고
    • Adaptor self-aggregation, adaptor-receptor recognition and binding of α-adaptin subunits to the plasma membrane contribute to recruitment of adaptor (AP2) components of clathrin-coated pits
    • Chang, M P., W.G. Mallett, K E Mostov, and F.M Brodsky. 1993. Adaptor self-aggregation, adaptor-receptor recognition and binding of α-adaptin subunits to the plasma membrane contribute to recruitment of adaptor (AP2) components of clathrin-coated pits. EMBO (Eur. Mol Biol. Organ.) J 12: 2169-2180.
    • (1993) EMBO (Eur. Mol Biol. Organ.) J , vol.12 , pp. 2169-2180
    • Chang, M.P.1    Mallett, W.G.2    Mostov, K.E.3    Brodsky, F.M.4
  • 9
    • 0029088728 scopus 로고
    • Characterization of the endopeptidase PC2 activity towards secretogranin II in stably transfected PC12 cells
    • Dittié, A.S., and S.A. Tooze. 1995. Characterization of the endopeptidase PC2 activity towards secretogranin II in stably transfected PC12 cells. Biochem J. 310:777-787.
    • (1995) Biochem J. , vol.310 , pp. 777-787
    • Dittié, A.S.1    Tooze, S.A.2
  • 10
    • 0028128334 scopus 로고
    • ARF: A key regulatory switch in membrane traffic and organelle structure
    • Donaldson, J.G., and R D. Klausner. 1994. ARF: a key regulatory switch in membrane traffic and organelle structure. Curr. Opin Cell Biol. 6:527-532
    • (1994) Curr. Opin Cell Biol. , vol.6 , pp. 527-532
    • Donaldson, J.G.1    Klausner, R.D.2
  • 11
    • 0026327556 scopus 로고
    • Binding of ARF and β-Cop to Golgi membranes: Possible regulation by a trimeric G protein
    • Donaldson, J G., R.A. Kahn, J. Lippincott-Schwartz, and R D. Klausner. 1991. Binding of ARF and β-Cop to Golgi membranes: possible regulation by a trimeric G protein. Science (Wash. DC). 254:1197-1199.
    • (1991) Science (Wash. DC) , vol.254 , pp. 1197-1199
    • Donaldson, J.G.1    Kahn, R.A.2    Lippincott-Schwartz, J.3    Klausner, R.D.4
  • 12
    • 0017838948 scopus 로고
    • Intracellular transport and packaging of prolactin: A quantitative electron microscope autoradiographic study of mammotrophs dissociated from rat pituitaries
    • Farquhar, M.G., J.J Reid, and L.W. Daniell. 1978. Intracellular transport and packaging of prolactin: a quantitative electron microscope autoradiographic study of mammotrophs dissociated from rat pituitaries. Endocrinology. 102: 296-311.
    • (1978) Endocrinology , vol.102 , pp. 296-311
    • Farquhar, M.G.1    Reid, J.J.2    Daniell, L.W.3
  • 13
    • 0028290272 scopus 로고
    • Aluminium fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes
    • Finazzi, D., D. Cassel, J.G. Donaldson, and R D Klausner. 1994. Aluminium fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes. J. Biol. Chem. 269:3325-13330
    • (1994) J. Biol. Chem. , vol.269 , pp. 3325-13330
    • Finazzi, D.1    Cassel, D.2    Donaldson, J.G.3    Klausner, R.D.4
  • 14
    • 0024468967 scopus 로고
    • Specificity of binding of clathrin adaptors to signals on the mannose-6-phosphate/insulin-like growth factor 11 receptor
    • Glickman, J.N., E. Conibear, and B.M F. Pearse. 1989. Specificity of binding of clathrin adaptors to signals on the mannose-6-phosphate/insulin-like growth factor 11 receptor. EMBO (Eur. Mol Biol. Organ.) J. 8:1041-1047.
    • (1989) EMBO (Eur. Mol Biol. Organ.) J. , vol.8 , pp. 1041-1047
    • Glickman, J.N.1    Conibear, E.2    Pearse, B.M.F.3
  • 15
    • 0027153957 scopus 로고
    • Two distinct populations of ARF bound to Golgi membranes
    • Helms, J B , D.J Palmer, and J.E. Rothman. 1993. Two distinct populations of ARF bound to Golgi membranes J Cell Biol. 121.751-760
    • (1993) J Cell Biol. , vol.121 , pp. 751-760
    • Helms, J.B.1    Palmer, D.J.2    Rothman, J.E.3
  • 16
    • 0020578970 scopus 로고
    • Relationship between NGF-mediated volume increase and "priming effect" in fast and slow reacting clones of PC12 pheochromocytoma cells
    • Heumann, R., V. Kachel, and H. Thoenen. 1983. Relationship between NGF-mediated volume increase and "priming effect" in fast and slow reacting clones of PC12 pheochromocytoma cells. Exp. Cell Res. 145:179-190.
    • (1983) Exp. Cell Res. , vol.145 , pp. 179-190
    • Heumann, R.1    Kachel, V.2    Thoenen, H.3
  • 17
    • 0028232868 scopus 로고
    • Okadaic acid treatment leads to fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell surface
    • Horn, M., and G. Banting. 1994. Okadaic acid treatment leads to fragmentation of the trans-Golgi network and an increase in expression of TGN38 at the cell surface. Biochem. J 301:69-73.
    • (1994) Biochem. J , vol.301 , pp. 69-73
    • Horn, M.1    Banting, G.2
  • 18
    • 0026708135 scopus 로고
    • The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport
    • Kahn, R.A., P. Randazzo, T. Serafini, O. Weiss, C. Rulka, J. Clark, M. Amherdt, P. Roller, L. Orci, and J.E Rothman. 1992. The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport. J. Biol. Chem 267: 13039-13046.
    • (1992) J. Biol. Chem , vol.267 , pp. 13039-13046
    • Kahn, R.A.1    Randazzo, P.2    Serafini, T.3    Weiss, O.4    Rulka, C.5    Clark, J.6    Amherdt, M.7    Roller, P.8    Orci, L.9    Rothman, J.E.10
  • 19
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol 116.1071-1080.
    • (1992) J. Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 20
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells
    • Kuliawat, R., and P. Arvan. 1994. Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells. J Cell Biol. 126:77-86.
    • (1994) J Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 21
    • 0027371853 scopus 로고
    • Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor
    • Le Borgne, R., A. Schmidt, F. Mauxion, G. Griffiths, and B. Hoflack. 1993. Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor. J Biol. Chem 268:22552-22556.
    • (1993) J Biol. Chem , vol.268 , pp. 22552-22556
    • Le Borgne, R.1    Schmidt, A.2    Mauxion, F.3    Griffiths, G.4    Hoflack, B.5
  • 22
    • 0026632366 scopus 로고
    • Evidence for ADP-ribosylation factor (ARF) as a regulator in endosome-endosome fusion
    • Lenhard, J.M., R.A. Kahn, and P.D. Stahl. 1992. Evidence for ADP-ribosylation factor (ARF) as a regulator in endosome-endosome fusion. J. Biol. Chem. 267:13047-13052.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13047-13052
    • Lenhard, J.M.1    Kahn, R.A.2    Stahl, P.D.3
  • 23
    • 0028905657 scopus 로고
    • Roles for the mannose-6-phosphate receptors in lysosomal enzyme sorting, IGF-II binding and clathrin-coat assembly
    • Ludwig, T., R. Le Borgne, and B. Hoflack. 1995. Roles for the mannose-6-phosphate receptors in lysosomal enzyme sorting, IGF-II binding and clathrin-coat assembly. Trends Cell Biol. 5:202-205.
    • (1995) Trends Cell Biol. , vol.5 , pp. 202-205
    • Ludwig, T.1    Le Borgne, R.2    Hoflack, B.3
  • 24
    • 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.E. 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.E.4    Braghetta, P.5    Stanley, K.K.6
  • 25
    • 0024340753 scopus 로고
    • Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack
    • Malhotra, V., T. Serafini, L. Orci, J.C Shepherd, and J.E. Rothman. 1989 Purification of a novel class of coated vesicles mediating biosynthetic protein transport through the Golgi stack. Cell. 64:329-336.
    • (1989) Cell. , vol.64 , pp. 329-336
    • Malhotra, V.1    Serafini, T.2    Orci, L.3    Shepherd, J.C.4    Rothman, J.E.5
  • 26
    • 0023645960 scopus 로고
    • Studies ou the molecular organization of rat insulin secretory granules
    • Michael, J , R. Carrol, H.H. Swift, and D.F. Steiner. 1987. Studies ou the molecular organization of rat insulin secretory granules. J. Biol. Chem. 262:16531-16535.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16531-16535
    • Michael, J.1    Carrol, R.2    Swift, H.H.3    Steiner, D.F.4
  • 28
    • 0026503136 scopus 로고
    • Folding and trimerization of clathrin subunits at the triskelion hub
    • Näthke, I.S., J. Heuser, A. Lupas, J. Stock, C.W. Turck, and F.M. Brodsky. 1992. Folding and trimerization of clathrin subunits at the triskelion hub. Cell. 68:899-910.
    • (1992) Cell. , vol.68 , pp. 899-910
    • Näthke, I.S.1    Heuser, J.2    Lupas, A.3    Stock, J.4    Turck, C.W.5    Brodsky, F.M.6
  • 29
    • 0028270798 scopus 로고
    • ADP ribosylation factor and a 14-kD polypeptide are associated with heparan sulfate-carrying post-trans-Golgi network secretory vesicles in rat hepatocytes
    • Nickel, W., L.A. Huber, R.A. Kahn, N. Kipper, A Barthel, D. Fasshauer, and H.-D. Söling. 1994. ADP ribosylation factor and a 14-kD polypeptide are associated with heparan sulfate-carrying post-trans-Golgi network secretory vesicles in rat hepatocytes. J. Cell Biol. 125.721-732.
    • (1994) J. Cell Biol. , vol.125 , pp. 721-732
    • Nickel, W.1    Huber, L.A.2    Kahn, R.A.3    Kipper, N.4    Barthel, A.5    Fasshauer, D.6    Söling, H.-D.7
  • 30
    • 0021869149 scopus 로고
    • Clathrin-immunoreactive sites in the Golgi apparatus are concentrated at the trans pole in polypeptide hormone-secreting cells
    • Orci, L., M. Ravazzola, M. Amherdt, D Louvard, and A. Perrelet. 1985a. Clathrin-immunoreactive sites in the Golgi apparatus are concentrated at the trans pole in polypeptide hormone-secreting cells. Proc. Natl. Acad. Sci. USA. 82:5385-5389.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5385-5389
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Louvard, D.4    Perrelet, A.5
  • 31
    • 0022129515 scopus 로고
    • Direct identification of prohormone conversion site in insulin-secreting cells
    • Orci, L., M. Ravazzola, M. Amherdt, O. Madsen, J.-D. Vassalli, and A. Perrelet. 1985b Direct identification of prohormone conversion site in insulin-secreting cells. Cell. 42:671-681.
    • (1985) Cell. , vol.42 , pp. 671-681
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Vassalli, J.-D.5    Perrelet, A.6
  • 33
    • 0027448777 scopus 로고
    • Clathrin: Its role in receptor-mediated vesicular transport and specialized functions in neurons
    • Pley, U., and P. Parham. 1993. Clathrin: its role in receptor-mediated vesicular transport and specialized functions in neurons. Crit. Rev. Biochem Mol. Biol. 28:431-464.
    • (1993) Crit. Rev. Biochem Mol. Biol. , vol.28 , pp. 431-464
    • Pley, U.1    Parham, P.2
  • 34
    • 0027024348 scopus 로고
    • Preparation of recombinant ADP-ribosylation factor
    • Randazzo, P.A., O. Weiss, and R.A. Kahn. 1992. Preparation of recombinant ADP-ribosylation factor. Methods Enzymol. 219:362-369.
    • (1992) Methods Enzymol. , vol.219 , pp. 362-369
    • Randazzo, P.A.1    Weiss, O.2    Kahn, R.A.3
  • 35
    • 0027968347 scopus 로고
    • Overexpression of TGN38/41 leads to mislocalization of γ-adaptin
    • Reaves, B., and G. Banting. 1994. Overexpression of TGN38/41 leads to mislocalization of γ-adaptin. FEBS Lett. 251:448-456.
    • (1994) FEBS Lett. , vol.251 , pp. 448-456
    • Reaves, B.1    Banting, G.2
  • 36
    • 0025642375 scopus 로고
    • Cloning and expression of γ-adaptin, a component of clathrin-coated vesicles associated with the Golgi apparatus
    • Robinson, M.S. 1990. Cloning and expression of γ-adaptin, a component of clathrin-coated vesicles associated with the Golgi apparatus. J. Cell Biol. 111: 2319-2326.
    • (1990) J. Cell Biol. , vol.111 , pp. 2319-2326
    • Robinson, M.S.1
  • 38
    • 0027490848 scopus 로고
    • Assembly and targeting of adaptin chimeras in transfected cells
    • Robinson, M.S. 1993. Assembly and targeting of adaptin chimeras in transfected cells. J. Cell Biol. 123:67-77.
    • (1993) J. Cell Biol. , vol.123 , pp. 67-77
    • Robinson, M.S.1
  • 39
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamm in endocytosis
    • Robinson, M.S. 1994. The role of clathrin, adaptors and dynamm in endocytosis. Curr. Opin Cell Biol 6:538-544.
    • (1994) Curr. Opin Cell Biol , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 40
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of Brefeldin A and G protein activators
    • Robinson, M.S., and T.E. Kreis. 1992. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of Brefeldin A and G protein activators Cell 69.129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 41
    • 0022341945 scopus 로고
    • Secretogranins I and II: Two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway
    • Rosa, P., A. Hille, R.W.H. Lee, A. Zanini, P. De Camilli, and W.B. Huttner. 1985. Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway. J. Cell Biol. 101:1999-2011.
    • (1985) J. Cell Biol. , vol.101 , pp. 1999-2011
    • Rosa, P.1    Hille, A.2    Lee, R.W.H.3    Zanini, A.4    De Camilli, P.5    Huttner, W.B.6
  • 43
    • 0019817369 scopus 로고
    • High resolution analysis of the secretory pathway in mammotrophs of the rat anterior pituitary
    • Salpeter, M.M., and M.G. Farquhar. 1981. High resolution analysis of the secretory pathway in mammotrophs of the rat anterior pituitary. J. Cell Biol. 91: 240-246.
    • (1981) J. Cell Biol. , vol.91 , pp. 240-246
    • Salpeter, M.M.1    Farquhar, M.G.2
  • 44
    • 0027639816 scopus 로고
    • Biochemical requirements for the formation of clathrin- And COP-coated transport vesicles
    • Schmid, S.L. 1993. Biochemical requirements for the formation of clathrin- and COP-coated transport vesicles. Curr. Opin. Cell Biol. 5:621-627.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 621-627
    • Schmid, S.L.1
  • 45
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein
    • Serafini, T., L. Orci, M Amherdt, M. Brunner, R.A. Kahn, and J.E. Rothman. 1991. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein Cell. 67:239-253.
    • (1991) Cell. , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 46
    • 0020514619 scopus 로고
    • Immunoelectron microscopic exploration of the Golgi complex
    • Slot, J.W., and H.J. Geuze. 1983. Immunoelectron microscopic exploration of the Golgi complex. J. Histochem. Cytochem. 31:1049-1056.
    • (1983) J. Histochem. Cytochem. , vol.31 , pp. 1049-1056
    • Slot, J.W.1    Geuze, H.J.2
  • 47
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes, M.A., and J.E. Rothman. 1993. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell. 73:999-1005.
    • (1993) Cell. , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 48
    • 0024318954 scopus 로고
    • Use of poly (vinylpyrrolidone) and poly (vinyl alcohol) for cryoultramicrotomy
    • Tokuyasu, T. 1989. Use of poly (vinylpyrrolidone) and poly (vinyl alcohol) for cryoultramicrotomy. Histochem. J. 21:163-171
    • (1989) Histochem. J. , vol.21 , pp. 163-171
    • Tokuyasu, T.1
  • 49
    • 0025812030 scopus 로고
    • Biogenesis of secretory granules. Implications arising from the immature secretory granule in the regulated pathway of secretion
    • Tooze, S.A 1991. Biogenesis of secretory granules. Implications arising from the immature secretory granule in the regulated pathway of secretion FEBS Lett. 285:220-224.
    • (1991) FEBS Lett. , vol.285 , pp. 220-224
    • Tooze, S.A.1
  • 50
    • 0023008920 scopus 로고
    • Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells
    • Tooze, J., and S A. Tooze. 1986. Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells. J. Cell Biol. 103:839-850.
    • (1986) J. Cell Biol. , vol.103 , pp. 839-850
    • Tooze, J.1    Tooze, S.A.2
  • 51
    • 0025248051 scopus 로고
    • Cell-free protein sorting to the regulated and constitutive secretory pathways
    • Tooze, S.A., and W.B. Huttner 1990. Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell 60.837-847.
    • (1990) Cell , vol.60 , pp. 837-847
    • Tooze, S.A.1    Huttner, W.B.2
  • 52
    • 0027022489 scopus 로고
    • Cell-free formation of immature secretory granules and constitutive secretory vesicles from trans-Golgi network
    • Tooze, S.A., and W.B. Huttner. 1992. Cell-free formation of immature secretory granules and constitutive secretory vesicles from trans-Golgi network. Methods Enzymol. 219:81-93.
    • (1992) Methods Enzymol. , vol.219 , pp. 81-93
    • Tooze, S.A.1    Huttner, W.B.2
  • 53
    • 0026332190 scopus 로고
    • Characterization of the immature secretory granule, an intermediate in granule biogenesis
    • Tooze, S.A., T. Flatmark, J. Tooze, and W.B. Huttner. 1991. Characterization of the immature secretory granule, an intermediate in granule biogenesis. J. Cell Biol. 115:1491-1503.
    • (1991) J. Cell Biol. , vol.115 , pp. 1491-1503
    • Tooze, S.A.1    Flatmark, T.2    Tooze, J.3    Huttner, W.B.4
  • 54
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • Traub, L.M , J. A. Ostrom, and S. Kornfeld. 1993 Biochemical dissection of AP-1 recruitment onto Golgi membranes. J. Cell Biol. 123:561-573.
    • (1993) J. Cell Biol. , vol.123 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfeld, S.3
  • 55
    • 0028956745 scopus 로고
    • Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment
    • Traub, L.M., S. Kornfeld, and E. Ungewickell. 1995. Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment. J. Biol Chem. 270:4933-4942.
    • (1995) J. Biol Chem. , vol.270 , pp. 4933-4942
    • Traub, L.M.1    Kornfeld, S.2    Ungewickell, E.3
  • 56
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated pathways in PC12 cells
    • Urbé, S., L.A. Huber, M. Zerial, S.A. Tooze, and R.G. Parton. 1993. Rab11, a small GTPase associated with both constitutive and regulated pathways in PC12 cells. FEBS Lett. 334:175-182.
    • (1993) FEBS Lett. , vol.334 , pp. 175-182
    • Urbé, S.1    Huber, L.A.2    Zerial, M.3    Tooze, S.A.4    Parton, R.G.5
  • 57
    • 0026628312 scopus 로고
    • 100-kD proteins of Golgi- And trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties
    • Wong, D.H., and F M. Brodsky 1992 100-kD proteins of Golgi- and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties. J Cell Biol 117:1171-1179.
    • (1992) J Cell Biol , vol.117 , pp. 1171-1179
    • Wong, D.H.1    Brodsky, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.