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Volumn 4, Issue 12, 2002, Pages 955-962

Regulated exocytosis: A novel, widely expressed system

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DESMOYOKIN; GENE PRODUCT; GLUCOSE TRANSPORTER 4; MARKER; MEMBRANE PROTEIN; PROTEIN AHNAK; TETANUS TOXIN; UNCLASSIFIED DRUG;

EID: 0036903036     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb888     Document Type: Review
Times cited : (154)

References (45)
  • 1
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. & Südhof, T. C. Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 863-911
    • Jahn, R.1    Südhof, T.C.2
  • 2
    • 0033068160 scopus 로고    scopus 로고
    • 2+-dependent exocytosis: Implications of kinetic diversity for secretion function
    • 2+-dependent exocytosis: implications of kinetic diversity for secretion function. Trends Neurosci. 22, 88-93 (1999).
    • (1999) Trends Neurosci. , vol.22 , pp. 88-93
    • Kasai, H.1
  • 3
    • 0029764204 scopus 로고    scopus 로고
    • 2+ triggers massive exocytosis in Chinese hamster ovary cells
    • 2+ triggers massive exocytosis in Chinese hamster ovary cells. EMBO J. 15, 3787-3791 (1996).
    • (1996) EMBO J. , vol.15 , pp. 3787-3791
    • Coorssen, J.R.1    Schmitt, H.2    Almers, W.3
  • 5
    • 0033514413 scopus 로고    scopus 로고
    • Multiple and diverse exocytosis in wild-type and defective PC12 cells
    • Kasai, H. et al. Multiple and diverse exocytosis in wild-type and defective PC12 cells. Proc. Natl. Acad. Sci. USA 96, 945-949 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 945-949
    • Kasai, H.1
  • 6
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • Andrews, N. W. Regulated secretion of conventional lysosomes. Trends Cell. Biol. 10, 316-321 (2000).
    • (2000) Trends Cell. Biol. , vol.10 , pp. 316-321
    • Andrews, N.W.1
  • 7
    • 0026745079 scopus 로고
    • Differential expression of markers and activities in a group of PC12 nerve cell clones
    • Clementi, E., Racchetti, G., Zacchetti, D., Panzeri, M. C. & Meldolesi, J. Differential expression of markers and activities in a group of PC12 nerve cell clones. Eur. J. Neurosci. 4, 944-953 (1992).
    • (1992) Eur. J. Neurosci. , vol.4 , pp. 944-953
    • Clementi, E.1    Racchetti, G.2    Zacchetti, D.3    Panzeri, M.C.4    Meldolesi, J.5
  • 8
    • 0035802119 scopus 로고    scopus 로고
    • Protein kinase B phosphorylates AHNAK and regulates its subcellular localization
    • Sussman, J., Stokoe, D., Ossina, N. & Shtivelmann, E. Protein kinase B phosphorylates AHNAK and regulates its subcellular localization. J. Cell Biol. 154, 1019-1030 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 1019-1030
    • Sussman, J.1    Stokoe, D.2    Ossina, N.3    Shtivelmann, E.4
  • 9
    • 0036296502 scopus 로고    scopus 로고
    • Identification of AHNAK as a novel autoantigen in systemic lupus erythematosus
    • Sköldberg, F. et al. Identification of AHNAK as a novel autoantigen in systemic lupus erythematosus. Biochem. Biophys. Res. Commun. 291, 951-958 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 951-958
    • Sköldberg, F.1
  • 10
    • 0027464086 scopus 로고
    • The human gene AHNAK encodes a large phosphoprotein located primarily in the nucleus
    • Shtivelman, E. & Bishop, J. M. The human gene AHNAK encodes a large phosphoprotein located primarily in the nucleus. J. Cell Biol. 120, 625-630 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 625-630
    • Shtivelman, E.1    Bishop, J.M.2
  • 11
    • 0034846497 scopus 로고    scopus 로고
    • Late endosomes: Sorting and partitioning in multivesicular bodies
    • Piper, R. C. & Luzio, J. P. Late endosomes: sorting and partitioning in multivesicular bodies. Traffic 2, 612-621 (2001).
    • (2001) Traffic , vol.2 , pp. 612-621
    • Piper, R.C.1    Luzio, J.P.2
  • 12
    • 0034909532 scopus 로고    scopus 로고
    • A Glut4-veside marker protein, insulin-responsive aminopeptidase, is localized in a novel vesicular compartment in PC12 cells
    • Thoidis, G. & Kandrov, K. V. A Glut4-veside marker protein, insulin-responsive aminopeptidase, is localized in a novel vesicular compartment in PC12 cells. Traffic 2, 577-587 (2001).
    • (2001) Traffic , vol.2 , pp. 577-587
    • Thoidis, G.1    Kandrov, K.V.2
  • 13
    • 0030696255 scopus 로고    scopus 로고
    • Targeting of green fluorescent protein to neuroendocrine secretary granules: A new tool for real time studies of regulated protein secretion
    • Kaether, C., Salm, T., Glombik M., Almers, W. & Gerdes, H. H. Targeting of green fluorescent protein to neuroendocrine secretary granules: a new tool for real time studies of regulated protein secretion. Eur. J. Cell Biol. 74, 133-142 (1997).
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 133-142
    • Kaether, C.1    Salm, T.2    Glombik, M.3    Almers, W.4    Gerdes, H.H.5
  • 14
    • 0033214345 scopus 로고    scopus 로고
    • Neurosecretory cells without neurosecretion: Evidence of an independently regulated trait of the cell phenotype
    • Malosio, M. L. et al. Neurosecretory cells without neurosecretion: evidence of an independently regulated trait of the cell phenotype. J. Physiol. (Lond.) 520, 43-52 (1999).
    • (1999) J. Physiol. (Lond.) , vol.520 , pp. 43-52
    • Malosio, M.L.1
  • 15
    • 0034733663 scopus 로고    scopus 로고
    • Nitric oxide inhibits the tumor necrosis factor alpha-regulated endocytosis of human dendritic cells in a cyclic GMP-dependent way
    • Paolucci, P., Rovere, P., De Nadai, C., Manfredi, A. A. & Clementi, E. Nitric oxide inhibits the tumor necrosis factor alpha-regulated endocytosis of human dendritic cells in a cyclic GMP-dependent way. J. Biol. Chem. 275, 19638-19644 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 19638-19644
    • Paolucci, P.1    Rovere, P.2    De Nadai, C.3    Manfredi, A.A.4    Clementi, E.5
  • 16
    • 0035025267 scopus 로고    scopus 로고
    • Coping with the inevitable: How cells repair a torn surface membrane
    • McNeil, P. L. & Terasaki, M. Coping with the inevitable: how cells repair a torn surface membrane. Nature Cell Biol. 3, E124-E129 (2001).
    • (2001) Nature Cell Biol. , vol.3
    • McNeil, P.L.1    Terasaki, M.2
  • 18
    • 0027279290 scopus 로고
    • Desmoyokin, a 280 kDa keratinocyte plasma membrane-associated protein, is homologous to the protein encoded by human gene AHNAK
    • Hashimoto, T. et al. Desmoyokin, a 280 kDa keratinocyte plasma membrane-associated protein, is homologous to the protein encoded by human gene AHNAK J. Cell Sci. 105, 275-286 (1993).
    • (1993) J. Cell Sci. , vol.105 , pp. 275-286
    • Hashimoto, T.1
  • 19
    • 0034106013 scopus 로고    scopus 로고
    • C-terminus of desmoyokin-AHNAK protein is responsible for its translocation between the nucleus and cytoplasm
    • Nie, Z., Ning, W., Amagai, M. & Hashimoto, T. C-terminus of desmoyokin-AHNAK protein is responsible for its translocation between the nucleus and cytoplasm. J. Invest. Dermatol, 114, 1044-1049 (2000).
    • (2000) J. Invest. Dermatol. , vol.114 , pp. 1044-1049
    • Nie, Z.1    Ning, W.2    Amagai, M.3    Hashimoto, T.4
  • 20
    • 0028969494 scopus 로고
    • Regulation of translocation of the desmoyokin-AHNAK protein to the plasma membrane in keratinocytes by protein kinase C
    • Hashimoto, T., Gamou, S., Shimizu, N., Kitajima, Y. & Nishikawa, T. Regulation of translocation of the desmoyokin-AHNAK protein to the plasma membrane in keratinocytes by protein kinase C. Exp. Cell Res. 217, 258-266 (1995).
    • (1995) Exp. Cell Res. , vol.217 , pp. 258-266
    • Hashimoto, T.1    Gamou, S.2    Shimizu, N.3    Kitajima, Y.4    Nishikawa, T.5
  • 21
    • 0032765048 scopus 로고    scopus 로고
    • Signalling from β-adrenoreceptor to L-type calcium channel: Identification of a novel cardiac protein kinase A target possessing similarities to AHNAK
    • Haase, H. et al. Signalling from β-adrenoreceptor to L-type calcium channel: identification of a novel cardiac protein kinase A target possessing similarities to AHNAK. FASEB J. 113, 2161-2172 (1999).
    • (1999) FASEB J. , vol.113 , pp. 2161-2172
    • Haase, H.1
  • 22
    • 0040313465 scopus 로고    scopus 로고
    • AHNAK, a protein that binds and activates phospholipase C-γ1 in the presence of arachidonic acid
    • Sekiya, F., Bae, Y. S., Jhon, D. Y., Hwang, S. C. & Rhee, S. G. AHNAK, a protein that binds and activates phospholipase C-γ1 in the presence of arachidonic acid. J. Biol. Chem. 274, 13900-13907 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13900-13907
    • Sekiya, F.1    Bae, Y.S.2    Jhon, D.Y.3    Hwang, S.C.4    Rhee, S.G.5
  • 23
    • 0035968275 scopus 로고    scopus 로고
    • The giant protein AHNAK is a specific target for the calcium- and zinc-binding S100B protein
    • Gentil, B. J. et al. The giant protein AHNAK is a specific target for the calcium- and zinc-binding S100B protein. J. Biol. Chem. 276, 23253-23261 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23253-23261
    • Gentil, B.J.1
  • 24
    • 0035132869 scopus 로고    scopus 로고
    • Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons
    • Lu, W. et al. Activation of synaptic NMDA receptors induces membrane insertion of new AMPA receptors and LTP in cultured hippocampal neurons. Neuron 29, 243-254 (2001).
    • (2001) Neuron , vol.29 , pp. 243-254
    • Lu, W.1
  • 25
    • 0033003216 scopus 로고    scopus 로고
    • Modulation of vasopressin-elicited water transport by trafficking of aquaporin2-containing vesicles
    • Ward, D. T., Hammond, T. G. & Harris, H. W. Modulation of vasopressin-elicited water transport by trafficking of aquaporin2-containing vesicles. Annu. Rev. Physiol. 61, 683-697 (1999).
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 683-697
    • Ward, D.T.1    Hammond, T.G.2    Harris, H.W.3
  • 26
    • 0035958981 scopus 로고    scopus 로고
    • 2+ in insulin-stimulated glucose transport in 3T3-L1 cells
    • 2+ in insulin-stimulated glucose transport in 3T3-L1 cells. J. Biol. Chem. 276, 27816-27824 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27816-27824
    • Whitehead, J.P.1
  • 27
    • 0035106864 scopus 로고    scopus 로고
    • GLUT4-at the cross roads between membrane trafficking and signal transduction
    • Simpson, F.., Whitehead, J. P. & James, D. E. GLUT4-at the cross roads between membrane trafficking and signal transduction. Traffic 2, 2-11 (2001).
    • (2001) Traffic , vol.2 , pp. 2-11
    • Simpson, F.1    Whitehead, J.P.2    James, D.E.3
  • 28
    • 0033543660 scopus 로고    scopus 로고
    • +-ATPast redistribution to the apical membrane in rat renal inner medullary collecting duct cells
    • +-ATPast redistribution to the apical membrane in rat renal inner medullary collecting duct cells. J. Biol. Chem. 274, 26518-26522 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 26518-26522
    • Banerjee, A.1    Shih, T.2    Alexander, E.A.3    Schwartz, J.H.4
  • 30
    • 0023159083 scopus 로고
    • Gradual and stepwise changes in the membrane capacitance of rat peritoneal mast cells
    • Almers, W. & Neher, E. Gradual and stepwise changes in the membrane capacitance of rat peritoneal mast cells. J. Physiol. (Lond) 386, 205-217 (1987).
    • (1987) J. Physiol. (Lond) , vol.386 , pp. 205-217
    • Almers, W.1    Neher, E.2
  • 31
    • 0000647430 scopus 로고    scopus 로고
    • Two types of exocytosis observed in single, rat pancreatic acinar cells
    • (in the press)
    • Thomas, P. et al. Two types of exocytosis observed in single, rat pancreatic acinar cells. J. Physiol. (Lond.) (in the press).
    • J. Physiol. (Lond.)
    • Thomas, P.1
  • 32
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu, T., Binz, T., Niemann, H. & Neher, E. Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nature Neurosci 1, 192-200 (1998).
    • (1998) Nature Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 33
    • 0033571899 scopus 로고    scopus 로고
    • Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)-VAMP7 in neuronal cells: Evidence for a novel membrane compartment
    • Coco, S. et al. Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)-VAMP7 in neuronal cells: evidence for a novel membrane compartment. J. Neurosci. 19, 9803-9812 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 9803-9812
    • Coco, S.1
  • 34
    • 0032578457 scopus 로고    scopus 로고
    • v-SNARE-dependent secretion is required for phagocytosis
    • Hackam, D. J. et al. v-SNARE-dependent secretion is required for phagocytosis. Proc. Natl Acad. Sci. USA 95, 11691-11696 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11691-11696
    • Hackam, D.J.1
  • 35
    • 0034192575 scopus 로고    scopus 로고
    • Quo vadis: Polarized membrane recycling in motility and phagocytosis
    • Mellman, I. Quo vadis: polarized membrane recycling in motility and phagocytosis. J. Cell Biol. 49, 529-530 (2000).
    • (2000) J. Cell Biol. , vol.49 , pp. 529-530
    • Mellman, I.1
  • 36
    • 0028014529 scopus 로고
    • Cell membrane resealing by vesicular mechanism similar to neurotransmitter release
    • Steinhardt, R. A., Bi, G. & Alderton, J. M. Cell membrane resealing by vesicular mechanism similar to neurotransmitter release. Science 263, 390-393 (1994).
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 37
    • 0033067513 scopus 로고    scopus 로고
    • The mechanism of facilitated cell membrane resealing
    • Togo, T., Alderton, J. M., Bi, G. O. & Steinhardt, R. A. The mechanism of facilitated cell membrane resealing. J. Cell Sci. 112, 719-731 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 719-731
    • Togo, T.1    Alderton, J.M.2    Bi, G.O.3    Steinhardt, R.A.4
  • 38
  • 39
    • 0032865299 scopus 로고    scopus 로고
    • Neurite extension occurs in the absence of regulated exocytosis in PC12 subclones
    • Leoni, C. et al. Neurite extension occurs in the absence of regulated exocytosis in PC12 subclones. Mol. Biol. Cell 10, 2919-2931 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2919-2931
    • Leoni, C.1
  • 40
    • 0030936274 scopus 로고    scopus 로고
    • Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transferrin receptor
    • Schmidt, A., Hannah, M. J. & Huttner, W. B. Synaptic-like microvesicles of neuroendocrine cells originate from a novel compartment that is continuous with the plasma membrane and devoid of transferrin receptor. J. Cell Biol, 137, 445-458 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 445-458
    • Schmidt, A.1    Hannah, M.J.2    Huttner, W.B.3
  • 41
    • 0017769048 scopus 로고
    • Antibodies to major histocompatibility antigens produced by hybrid cell lines
    • Galfré, G., Howe, S. C., Milstein, C., Butcher, G. W. & Howard, J. C. Antibodies to major histocompatibility antigens produced by hybrid cell lines. Nature 266, 550-552 (1977).
    • (1977) Nature , vol.266 , pp. 550-552
    • Galfré, G.1    Howe, S.C.2    Milstein, C.3    Butcher, G.W.4    Howard, J.C.5
  • 42
    • 0034625085 scopus 로고    scopus 로고
    • Rapid regulated dense-core vesicle exocytosis requires the CAPS protein
    • Rupnik, M. et al. Rapid regulated dense-core vesicle exocytosis requires the CAPS protein. Proc. Natl Acad. Sci. USA 97, 5627-5632 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5627-5632
    • Rupnik, M.1
  • 43
    • 0030812756 scopus 로고    scopus 로고
    • Overexpression of calsequestrin in L6 myoblasts: Formation of endoplasmic reticulum subdomains and their evolution into discrete vacuoles where aggregates of the protein are specifically accumulated
    • Gatti, G., Podini, P. & Meldolesi, J. Overexpression of calsequestrin in L6 myoblasts: formation of endoplasmic reticulum subdomains and their evolution into discrete vacuoles where aggregates of the protein are specifically accumulated. Mol. Biol. Cell 8, 1789-1803 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1789-1803
    • Gatti, G.1    Podini, P.2    Meldolesi, J.3
  • 44
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M. et al. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469 (1996).
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1
  • 45
    • 0026725397 scopus 로고
    • Electroporation in 'intracellular' buffer increases cell survival
    • Van den Hoff, M. J. B., Moorman, A. F. M. & Lamers, W. H. Electroporation in 'intracellular' buffer increases cell survival. Nucleic Acids Res. 20, 2902 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2902
    • Van den Hoff, M.J.B.1    Moorman, A.F.M.2    Lamers, W.H.3


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