메뉴 건너뛰기




Volumn 11, Issue 23, 2002, Pages 2855-2866

Novel membrane traffic steps regulate the exocytosis of the Menkes disease ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CD4 ANTIGEN; COPPER ION; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; GUANOSINE TRIPHOSPHATASE; MUTANT PROTEIN; PROTEIN CDC42; PROTEIN KINASE; RAC PROTEIN;

EID: 0036847903     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/11.23.2855     Document Type: Article
Times cited : (49)

References (58)
  • 1
    • 78651124591 scopus 로고
    • A sex-linked recessive disorder with retardation of growth, peculiar hair, and focal cerebral and cerebellar degeneration
    • Menkes, J., Alter, M., Steigleder, G., Weakley, D. and Sung, J. (1962) A sex-linked recessive disorder with retardation of growth, peculiar hair, and focal cerebral and cerebellar degeneration. Pediatrics, 29, 764-779.
    • (1962) Pediatrics , vol.29 , pp. 764-779
    • Menkes, J.1    Alter, M.2    Steigleder, G.3    Weakley, D.4    Sung, J.5
  • 2
    • 0028242939 scopus 로고
    • Wilson disease and Menkes disease: New handles on heavy-metal transport
    • Bull, P.C. and Cox, D.W. (1994) Wilson disease and Menkes disease: new handles on heavy-metal transport. Trends Genet., 10, 246-252.
    • (1994) Trends Genet , vol.10 , pp. 246-252
    • Bull, P.C.1    Cox, D.W.2
  • 3
    • 0027376523 scopus 로고
    • Human Menkes X-chromosome disease and the staphylococcal cadmium-resistance ATPase: A remarkable similarity in protein sequences
    • Silver, S., Nucifora, G. and Phung, L.T. (1993) Human Menkes X-chromosome disease and the staphylococcal cadmium-resistance ATPase: a remarkable similarity in protein sequences. Mol. Microbiol., 10, 7-12.
    • (1993) Mol. Microbiol , vol.10 , pp. 7-12
    • Silver, S.1    Nucifora, G.2    Phung, L.T.3
  • 4
    • 0031055871 scopus 로고    scopus 로고
    • Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network
    • Dierick, H.A., Adam, A.N., Escara-Wilke, J.F. and Glover, T.W. (1997) Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network. Hum. Mol. Genet., 6, 409-416.
    • (1997) Hum. Mol. Genet , vol.6 , pp. 409-416
    • Dierick, H.A.1    Adam, A.N.2    Escara-Wilke, J.F.3    Glover, T.W.4
  • 5
    • 0032837679 scopus 로고    scopus 로고
    • The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal
    • Petris, M.J. and Mercer, J.F. (1999) The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal. Hum. Mol. Genet., 8, 2107-2115.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 2107-2115
    • Petris, M.J.1    Mercer, J.F.2
  • 6
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris, M.J., Mercer, J.F., Culvenor, J.G., Lockhart, P., Gleeson, P.A. and Camakaris, J. (1996) Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J., 15, 6084-6095.
    • (1996) EMBO J , vol.15 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 7
    • 0030467256 scopus 로고    scopus 로고
    • Biochemical characterization and intracellular localization of the Menkes disease protein
    • Yamaguchi, Y., Heiny, M.E., Suzuki, M. and Gitlin, J.D. (1996) Biochemical characterization and intracellular localization of the Menkes disease protein. Proc. Natl Acad. Sci. USA, 93, 14030-14035.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14030-14035
    • Yamaguchi, Y.1    Heiny, M.E.2    Suzuki, M.3    Gitlin, J.D.4
  • 8
    • 0034641603 scopus 로고    scopus 로고
    • Copper-dependent trafficking of Wilson disease mutant ATP7B proteins
    • Forbes, J.R. and Cox, D.W. (2000) Copper-dependent trafficking of Wilson disease mutant ATP7B proteins. Hum. Mol. Genet., 9, 1927-1935.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 1927-1935
    • Forbes, J.R.1    Cox, D.W.2
  • 9
    • 0035864917 scopus 로고    scopus 로고
    • Effect of the toxic milk mutation (tx) on the function and intracellular localization of Wnd, the murine homologue of the Wilson copper ATPase
    • La Fontaine, S., Theophilos, M.B., Firth, S.D., Gould, R., Parton, R.G. and Mercer, J.F. (2001) Effect of the toxic milk mutation (tx) on the function and intracellular localization of Wnd, the murine homologue of the Wilson copper ATPase. Hum. Mol. Genet., 10, 361-370.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 361-370
    • La Fontaine, S.1    Theophilos, M.B.2    Firth, S.D.3    Gould, R.4    Parton, R.G.5    Mercer, J.F.6
  • 12
    • 0028972922 scopus 로고
    • Gene amplification of the Menkes (MNK; ATP7A) P-type ATPase gene of CHO cells is associated with copper resistance and enhanced copper efflux
    • Camakaris, J., Petris, M.J., Bailey, L., Shen, P., Lockhart, P., Glover, T.W., Barcroft, C., Patton, J. and Mercer, J.F. (1995) Gene amplification of the Menkes (MNK; ATP7A) P-type ATPase gene of CHO cells is associated with copper resistance and enhanced copper efflux, Hum. Mol. Genet., 4, 2117-2123.
    • (1995) Hum. Mol. Genet , vol.4 , pp. 2117-2123
    • Camakaris, J.1    Petris, M.J.2    Bailey, L.3    Shen, P.4    Lockhart, P.5    Glover, T.W.6    Barcroft, C.7    Patton, J.8    Mercer, J.F.9
  • 13
    • 0031829339 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of the human Menkes protein (MNK) stably expressed from a cDNA construct in Chinese hamster ovary cells (CHO-K1)
    • La Fontaine, S., Firth, S.D., Lockhart, P.J., Brooks, H., Parton, R.G., Camakaris, J. and Mercer, J.F. (1998) Functional analysis and intracellular localization of the human Menkes protein (MNK) stably expressed from a cDNA construct in Chinese hamster ovary cells (CHO-K1). Hum. Mol. Genet., 7, 1293-1300.
    • (1998) Hum. Mol. Genet , vol.7 , pp. 1293-1300
    • La Fontaine, S.1    Firth, S.D.2    Lockhart, P.J.3    Brooks, H.4    Parton, R.G.5    Camakaris, J.6    Mercer, J.F.7
  • 16
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron, C.L. and Malhotra, V. (2002) Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science, 295, 325-328.
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 17
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl, M., Maeda, Y., Colanzi, A., Ayala, I., Van Lint, J. and Malhotra, V. (2001) Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell, 104, 409-420.
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 19
    • 0033983938 scopus 로고    scopus 로고
    • Regulation of endocytic traffic by Rho family GTPases
    • Ellis, S. and Mellor, H. (2000) Regulation of endocytic traffic by Rho family GTPases. Trends Cell Biol., 10, 85-88.
    • (2000) Trends Cell Biol , vol.10 , pp. 85-88
    • Ellis, S.1    Mellor, H.2
  • 20
    • 0034997092 scopus 로고    scopus 로고
    • Rho proteins: Linking signaling with membrane trafficking
    • Ridley, A.J. (2001) Rho proteins: linking signaling with membrane trafficking. Traffic, 2, 303-310.
    • (2001) Traffic , vol.2 , pp. 303-310
    • Ridley, A.J.1
  • 21
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R., Hall, A. and Mellman, I. (1999) Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell. Biol., 1, 8-13.
    • (1999) Nat. Cell. Biol , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 22
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A.L. and Hall, A. (2000) Rho GTPases and their effector proteins. Biochem. J., 348, 241-255.
    • (2000) Biochem. J , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 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 Howell, K.E. (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
    • 0025943380 scopus 로고
    • Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes
    • Wood, S.A., Park, J.E. and Brown, W.J. (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
  • 26
    • 0027379099 scopus 로고
    • Mitogen-activated protein kinase activation is not sufficient for stimulation of glucose transport or glycogen synthase in 3T3-L1 adipocytes
    • Robinson, L.J., Razzack, Z.F., Lawrence, J.C., Jr, and James, D.E. (1993) Mitogen-activated protein kinase activation is not sufficient for stimulation of glucose transport or glycogen synthase in 3T3-L1 adipocytes. J. Biol. Chem., 268, 26422-26427.
    • (1993) J. Biol. Chem , vol.268 , pp. 26422-26427
    • Robinson, L.J.1    Razzack, Z.F.2    Lawrence J.C., Jr.3    James, D.E.4
  • 27
    • 0035831216 scopus 로고    scopus 로고
    • Protein kinase C μ selectively activates the mitogen-activated protein kinase (MAPK) p42 pathway
    • Hausser, A., Storz, P., Hubner, S., Braendlin, I., Martinez-Moya, M., Link, G. and Johannes, F.J. (2001) Protein kinase C μ selectively activates the mitogen-activated protein kinase (MAPK) p42 pathway. FEBS Lett., 492, 39-44.
    • (2001) FEBS Lett , vol.492 , pp. 39-44
    • Hausser, A.1    Storz, P.2    Hubner, S.3    Braendlin, I.4    Martinez-Moya, M.5    Link, G.6    Johannes, F.J.7
  • 28
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., Jackson, M. and Peterson, P.A. (1989) Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell, 58, 707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 29
    • 0003000807 scopus 로고    scopus 로고
    • Tools of the trade: Use of dominant-inhibitory mutants of Ras-family GTPases
    • Feig, L.A. (1999) Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases. Nat. Cell. Biol., 1, E25-E27.
    • (1999) Nat. Cell. Biol , vol.1
    • Feig, L.A.1
  • 30
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate
    • Rohatgi, R., Ho, H.Y. and Kirschner, M.W. (2000) Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate. J. Cell Biol., 150, 1299-1310.
    • (2000) J. Cell Biol , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 31
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons, M., Derry, J.M., Karlak, B., Jiang, S., Lemahieu, V., McCormick, F., Francke, U. and Abo, A. (1996) Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell, 84, 723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 32
    • 0034683577 scopus 로고    scopus 로고
    • How WASP regulates actin polymerization
    • Zigmond, S.H. (2000) How WASP regulates actin polymerization. J. Cell Biol., 150, F117-F 120.
    • (2000) J. Cell Biol , vol.150
    • Zigmond, S.H.1
  • 33
    • 0035503293 scopus 로고    scopus 로고
    • Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain
    • Maeda, Y., Beznoussenko, G.V, Van Lint, J., Mironov, A.A. and Malhotra, V. (2001) Recruitment of protein kinase D to the trans-Golgi network via the first cysteine-rich domain. EMBO J., 20, 5982-5990.
    • (2001) EMBO J , vol.20 , pp. 5982-5990
    • Maeda, Y.1    Beznoussenko, G.V.2    Van Lint, J.3    Mironov, A.A.4    Malhotra, V.5
  • 34
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science, 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 35
    • 0036056245 scopus 로고    scopus 로고
    • Involvement of Rho GTPases and their effectors in the secretory process of PC12 cells
    • Frantz, C., Coppola, T. and Regazzi, R. (2002) Involvement of Rho GTPases and their effectors in the secretory process of PC12 cells. Exp. Cell. Res., 273, 119-126.
    • (2002) Exp. Cell. Res , vol.273 , pp. 119-126
    • Frantz, C.1    Coppola, T.2    Regazzi, R.3
  • 36
    • 0035341316 scopus 로고    scopus 로고
    • cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network
    • Musch, A., Cohen, D., Kreitzer, G. and Rodriguez-Boulan, E. (2001) cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J., 20, 2171-2179.
    • (2001) EMBO J , vol.20 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 37
    • 0034703872 scopus 로고    scopus 로고
    • The Menkes copper transporter is required for the activation of tyrosinase
    • Petris, M.J., Strausak, D. and Mercer, J.F. (2000) The Menkes copper transporter is required for the activation of tyrosinase. Hum. Mol. Genet., 9, 2845-2851.
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2845-2851
    • Petris, M.J.1    Strausak, D.2    Mercer, J.F.3
  • 38
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg, K., Miller, C.M., Ellenberg, J., Presley, J.F., Siggia, E.D., Phair, R.D. and Lippincott-Schwartz, J. (1998) Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J. Cell. Biol., 143, 1485-1503.
    • (1998) J. Cell. Biol , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 39
    • 0034627793 scopus 로고    scopus 로고
    • Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane
    • Polishchuk, R.S., Polishchuk, E.V., Marra, P., Alberti, S., Buccione, R., Luini, A. and Mironov, A.A. (2000) Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J. Cell. Biol., 148, 45-58.
    • (2000) J. Cell. Biol , vol.148 , pp. 45-58
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Marra, P.3    Alberti, S.4    Buccione, R.5    Luini, A.6    Mironov, A.A.7
  • 40
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection fluorescence microscopy
    • Schmoranzer, J., Goulian, M., Axelrod, D. and Simon, S.M. (2000) Imaging constitutive exocytosis with total internal reflection fluorescence microscopy. J. Cell Biol., 149, 23-32.
    • (2000) J. Cell Biol , vol.149 , pp. 23-32
    • Schmoranzer, J.1    Goulian, M.2    Axelrod, D.3    Simon, S.M.4
  • 41
    • 0034599547 scopus 로고    scopus 로고
    • Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy
    • Toomre, D., Steyer, J.A., Keller, P., Almers, W. and Simons, K. (2000) Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy. J. Cell. Biol., 149, 33-40.
    • (2000) J. Cell. Biol , vol.149 , pp. 33-40
    • Toomre, D.1    Steyer, J.A.2    Keller, P.3    Almers, W.4    Simons, K.5
  • 42
    • 0026039965 scopus 로고
    • Trimeric G-proteins of the trans-Golgi network are involved in the formation of constitutive secretory vesicles and immature secretory granules
    • Barr, F.A., Leyte, A., Mollner, S., Pfeuffer, T., Tooze, S.A. and Huttner, W.B. (1991) Trimeric G-proteins of the trans-Golgi network are involved in the formation of constitutive secretory vesicles and immature secretory granules. FEBS Lett., 294, 239-243.
    • (1991) FEBS Lett , vol.294 , pp. 239-243
    • Barr, F.A.1    Leyte, A.2    Mollner, S.3    Pfeuffer, T.4    Tooze, S.A.5    Huttner, W.B.6
  • 44
    • 0027072502 scopus 로고
    • Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation
    • Leyte, A., Barr, F.A., Kehlenbach, R.H. and Huttner, W.B. (1992) Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation. EMBO J., 11, 4795-4804.
    • (1992) EMBO J , vol.11 , pp. 4795-4804
    • Leyte, A.1    Barr, F.A.2    Kehlenbach, R.H.3    Huttner, W.B.4
  • 45
    • 0029881303 scopus 로고    scopus 로고
    • A role for ADP-ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans-Golgi network
    • Barr, F.A. and Huttner, W.B. (1996) A role for ADP-ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans-Golgi network. FEBS Lett., 384, 65-70.
    • (1996) FEBS Lett , vol.384 , pp. 65-70
    • Barr, F.A.1    Huttner, W.B.2
  • 46
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., Tagaya, M., Ullrich, O., Montecucco, C. and Simons, K. (1995) Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell, 81, 571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 47
    • 0027370762 scopus 로고
    • Rab11, a small GTPase associated with both constitutive and regulated secretory pathways in PC12 cells
    • Urbe, S., Huber, L.A., Zerial, M., Tooze, S.A. and Parton, R.G. (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
    • 0036000011 scopus 로고    scopus 로고
    • Novel mechanism for regulation of epidermal growth factor receptor endocytosis revealed by protein kinase A inhibition
    • Salazar, G. and Gonzalez, A. (2002) Novel mechanism for regulation of epidermal growth factor receptor endocytosis revealed by protein kinase A inhibition. Mol. Biol. Cell., 13, 1677-1693.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1677-1693
    • Salazar, G.1    Gonzalez, A.2
  • 49
    • 0031474609 scopus 로고    scopus 로고
    • Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network
    • Muniz, M., Martin, M.E., Hidalgo, J. and Velasco, A. (1997) Protein kinase A activity is required for the budding of constitutive transport vesicles from the trans-Golgi network. Proc. Natl Acad. Sci. USA, 94, 14461-14466.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14461-14466
    • Muniz, M.1    Martin, M.E.2    Hidalgo, J.3    Velasco, A.4
  • 50
    • 0028033742 scopus 로고
    • An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network
    • Ohashi, M. and Huttner, W.B. (1994) An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network. J. Biol. Chem., 269, 24897-24905.
    • (1994) J. Biol. Chem , vol.269 , pp. 24897-24905
    • Ohashi, M.1    Huttner, W.B.2
  • 51
    • 0034680777 scopus 로고    scopus 로고
    • Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum
    • Aridor, M. and Balch, W.E. (2000) Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. J. Biol. Chem., 275, 35673-35676.
    • (2000) J. Biol. Chem , vol.275 , pp. 35673-35676
    • Aridor, M.1    Balch, W.E.2
  • 52
    • 0025248571 scopus 로고
    • Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells
    • Chijiwa, T., Mishima, A., Hagiwara, M., Sano, M., Hayashi, K., Inoue, T., Naito, K., Toshioka, T. and Hidaka, H. (1990) Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells. J. Biol. Chem., 265, 5267-5272.
    • (1990) J. Biol. Chem , vol.265 , pp. 5267-5272
    • Chijiwa, T.1    Mishima, A.2    Hagiwara, M.3    Sano, M.4    Hayashi, K.5    Inoue, T.6    Naito, K.7    Toshioka, T.8    Hidaka, H.9
  • 53
    • 0031587746 scopus 로고    scopus 로고
    • Pseudusubstrate inhibition of cyclic AMP-dependent protein kinase in intact pancreatic islets: Effects on cyclic AMP-dependent and glucose-dependent insulin secretion
    • Harris, T.E., Persaud, S.J. and Jones, P.M. (1997) Pseudusubstrate inhibition of cyclic AMP-dependent protein kinase in intact pancreatic islets: effects on cyclic AMP-dependent and glucose-dependent insulin secretion. Biochem. Biophys. Res. Commun., 232, 648-651.
    • (1997) Biochem. Biophys. Res. Commun , vol.232 , pp. 648-651
    • Harris, T.E.1    Persaud, S.J.2    Jones, P.M.3
  • 54
    • 0029861189 scopus 로고    scopus 로고
    • Involvement of the endoplasmic reticulurn in the assembly and envelopment of African swine fever virus
    • Cobbold, C., Whittle, J.T. and Wileman, T. (1996) Involvement of the endoplasmic reticulurn in the assembly and envelopment of African swine fever virus. J. Virol., 70, 8382-8390.
    • (1996) J. Virol , vol.70 , pp. 8382-8390
    • Cobbold, C.1    Whittle, J.T.2    Wileman, T.3
  • 55
    • 0030889062 scopus 로고    scopus 로고
    • Distinct compartmentalization of TGN46 and β1,4-galactosyltransferase in HeLa cells
    • Prescott, A.R., Lucocq, J.M., James, J., Lister, J.M. and Ponnambalam, S. (1997) Distinct compartmentalization of TGN46 and β1,4-galactosyltransferase in HeLa cells. Eur. J. Cell Biol., 72, 238-246.
    • (1997) Eur. J. Cell Biol , vol.72 , pp. 238-246
    • Prescott, A.R.1    Lucocq, J.M.2    James, J.3    Lister, J.M.4    Ponnambalam, S.5
  • 56
    • 0034714428 scopus 로고    scopus 로고
    • The manganese cation disrupts membrane dynamics along the secretory pathway
    • Towler, M.C., Prescott, A.R., James, J., Lucocq, J.M. and Ponnambalam, S. (2000) The manganese cation disrupts membrane dynamics along the secretory pathway. Exp. Cell Res., 259, 167-179.
    • (2000) Exp. Cell Res , vol.259 , pp. 167-179
    • Towler, M.C.1    Prescott, A.R.2    James, J.3    Lucocq, J.M.4    Ponnambalam, S.5
  • 57
    • 0024501531 scopus 로고
    • Effects of cytoplasmic acidification on clathrin lattice morphology
    • Heuser, J. (1989) Effects of cytoplasmic acidification on clathrin lattice morphology. J. Cell Biol. 108, 401-411.
    • (1989) J. Cell Biol , vol.108 , pp. 401-411
    • Heuser, J.1
  • 58
    • 0028351154 scopus 로고
    • The TGN38 glycoprotein contains two non-overlapping signals that mediate localization to the trans-Golgi network
    • Ponnambalam, S., Rabouille, C., Luzio, J.P., Nilsson, T. and Warren, G. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.