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Volumn 159, Issue 4, 2002, Pages 625-635

Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells

Author keywords

CD63; Dextran; Synaptotagmin VII; TIR FM; VAMP7

Indexed keywords

BIOLOGICAL MARKER; CALCIMYCIN; CALCIUM; FLUORESCENT DYE; HYBRID PROTEIN; IONOPHORE;

EID: 0037175388     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.200208154     Document Type: Article
Times cited : (297)

References (40)
  • 2
    • 0036330559 scopus 로고    scopus 로고
    • Lysosomes and the plasma membrane: Trypanosomes reveal a secret relationship
    • Andrews, N.W. 2002. Lysosomes and the plasma membrane: trypanosomes reveal a secret relationship. J. Cell Biol. 158:389-394.
    • (2002) J. Cell Biol , vol.158 , pp. 389-394
    • Andrews, N.W.1
  • 3
    • 0019494948 scopus 로고
    • Cell-substrate contacts illuminated by total internal reflection fluorescence
    • Axelrod, D. 1981. Cell-substrate contacts illuminated by total internal reflection fluorescence. J. Cell Biol. 89:141-145.
    • (1981) J. Cell Biol , vol.89 , pp. 141-145
    • Axelrod, D.1
  • 4
    • 0034744582 scopus 로고    scopus 로고
    • The pilus-induced Ca2+ flux triggers lysosome exocytosis and increases the amount of Lampl accessible to Neisseria IgA1 protease
    • Ayala, B.P., B. Vasquez, S. Clary, J.A. Tainer, K. Rodland, and M. So. 2001. The pilus-induced Ca2+ flux triggers lysosome exocytosis and increases the amount of Lampl accessible to Neisseria IgA1 protease. Cell Microbiol. 3:265-275.
    • (2001) Cell Microbiol , vol.3 , pp. 265-275
    • Ayala, B.P.1    Vasquez, B.2    Clary, S.3    Tainer, J.A.4    Rodland, K.5    So, M.6
  • 5
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero, P., L. Bittova, and S.R. Pfeffer. 2002. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J. Cell Biol. 156:511-518.
    • (2002) J. Cell Biol , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 6
    • 0018609332 scopus 로고
    • Ionomycin stimulates mast cell histamine secretion by forming a lipid-soluble calcium complex
    • Bennett, J.P., S. Cockcroft, and B.D. Gomperts. 1979. Ionomycin stimulates mast cell histamine secretion by forming a lipid-soluble calcium complex. Nature. 282:851-853.
    • (1979) Nature , vol.282 , pp. 851-853
    • Bennett, J.P.1    Cockcroft, S.2    Gomperts, B.D.3
  • 7
    • 0030984076 scopus 로고    scopus 로고
    • Kinesin- and myosin-driven steps of vesicle recruitment for Ca2 + - regulated exocytosis
    • Bi, G.Q., R.L. Morris, G. Liao, J.M. Alderton, J.M. Scholey, and R.A. Steinhardt. 1997. Kinesin- and myosin-driven steps of vesicle recruitment for Ca2 + - regulated exocytosis. J. Cell Biol. 138:999-1008.
    • (1997) J. Cell Biol , vol.138 , pp. 999-1008
    • Bi, G.Q.1    Morris, R.L.2    Liao, G.3    Alderton, J.M.4    Scholey, J.M.5    Steinhardt, R.A.6
  • 9
    • 0034927311 scopus 로고    scopus 로고
    • Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail
    • Blott, E.J., G. Bossi, R. Clark, M. Zvelebil, and G.M. Griffiths. 2001. Fas ligand is targeted to secretory lysosomes via a proline-rich domain in its cytoplasmic tail. J. Cell Sci. 114:2405-2416.
    • (2001) J. Cell Sci , vol.114 , pp. 2405-2416
    • Blott, E.J.1    Bossi, G.2    Clark, R.3    Zvelebil, M.4    Griffiths, G.M.5
  • 10
    • 0344352478 scopus 로고    scopus 로고
    • Oligopeptidase B-dependent signaling mediates host cell invasion by Trypanosoma cruzi
    • Caler, E.V., D.A. Vaena, P.A. Haynes, N.W. Andrews, and B.A. Burleigh. 1998. Oligopeptidase B-dependent signaling mediates host cell invasion by Trypanosoma cruzi. EMBO J. 17:4975-4986.
    • (1998) EMBO J , vol.17 , pp. 4975-4986
    • Caler, E.V.1    Vaena, D.A.2    Haynes, P.A.3    Andrews, N.W.4    Burleigh, B.A.5
  • 11
    • 0034441219 scopus 로고    scopus 로고
    • Dual role of signaling pathways leading to Ca(2+) and cyclic AMP elevation in host cell invasion by Trypanosoma cruzi
    • Caler, E.V., R.E. Morty, B.A. Burleigh, and N.W. Andrews. 2000. Dual role of signaling pathways leading to Ca(2+) and cyclic AMP elevation in host cell invasion by Trypanosoma cruzi. Infect. Immun. 68:6602-6610.
    • (2000) Infect. Immun , vol.68 , pp. 6602-6610
    • Caler, E.V.1    Morty, R.E.2    Burleigh, B.A.3    Andrews, N.W.4
  • 12
    • 0030003892 scopus 로고    scopus 로고
    • A biosynthetic regulated secretory pathway in constitutive secretory cells
    • Chavez, R.A., S.G. Miller, and H.P. Moore. 1996. A biosynthetic regulated secretory pathway in constitutive secretory cells. J. Cell Biol. 133:1177-1191.
    • (1996) J. Cell Biol , vol.133 , pp. 1177-1191
    • Chavez, R.A.1    Miller, S.G.2    Moore, H.P.3
  • 13
    • 0029764204 scopus 로고    scopus 로고
    • Ca2+ triggers massive exocytosis in Chinese hamster ovary cells
    • Coorssen, J.R., H. Schmitt, and W. Almers. 1996. Ca2+ triggers massive exocytosis in Chinese hamster ovary cells. EMBO J. 15:3787-3791.
    • (1996) EMBO J , vol.15 , pp. 3787-3791
    • Coorssen, J.R.1    Schmitt, H.2    Almers, W.3
  • 14
    • 0032101320 scopus 로고    scopus 로고
    • Endocytotic formation of vesicles and other membranous structures induced by Ca2+ and axolemmal injury
    • Eddleman, C.S., M.L. Ballinger, M.E. Smyers, H.M. Fishman, and G.D. Bittner. 1998. Endocytotic formation of vesicles and other membranous structures induced by Ca2+ and axolemmal injury. J. Neurosci. 18:4029-4041.
    • (1998) J. Neurosci , vol.18 , pp. 4029-4041
    • Eddleman, C.S.1    Ballinger, M.L.2    Smyers, M.E.3    Fishman, H.M.4    Bittner, G.D.5
  • 15
    • 0028971377 scopus 로고
    • IgG-induced Ca2+ oscillations in differentiated U937 cells; a study using laser scanning confocal microscopy and co-loaded fluo-3 and fura-red fluorescent probes
    • Floto, R.A., M.P. Mahaut-Smith, B. Somasundaram, and J.M. Allen. 1995. IgG-induced Ca2+ oscillations in differentiated U937 cells; a study using laser scanning confocal microscopy and co-loaded fluo-3 and fura-red fluorescent probes. Cell Calcium. 18:377-389.
    • (1995) Cell Calcium , vol.18 , pp. 377-389
    • Floto, R.A.1    Mahaut-Smith, M.P.2    Somasundaram, B.3    Allen, J.M.4
  • 16
    • 0029792020 scopus 로고    scopus 로고
    • Recombinant apoaequorin acting as a pseudo-luciferase reports micromolar changes in the endoplasmic reticulum free Ca2+ of intact cells
    • Kendall, J.M., M.N. Badminton, G.B. Sala-Newby, A.K. Campbell, and C.M. Rembold. 1996. Recombinant apoaequorin acting as a pseudo-luciferase reports micromolar changes in the endoplasmic reticulum free Ca2+ of intact cells. Biochem. J. 318:383-387.
    • (1996) Biochem. J , vol.318 , pp. 383-387
    • Kendall, J.M.1    Badminton, M.N.2    Sala-Newby, G.B.3    Campbell, A.K.4    Rembold, C.M.5
  • 18
    • 0035196362 scopus 로고    scopus 로고
    • Insulin-regulated release from the endosomal recycling compartment is regulated by budding of specialized vesicles
    • Lampson, M.A., J. Schmoranzer, A. Zeigerer, S.M. Simon, and T.E. McGraw. 2001. Insulin-regulated release from the endosomal recycling compartment is regulated by budding of specialized vesicles. Mol. Biol. Cell. 12:3489-3501.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3489-3501
    • Lampson, M.A.1    Schmoranzer, J.2    Zeigerer, A.3    Simon, S.M.4    McGraw, T.E.5
  • 19
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis, J., J.M. McCaffery, A. Miyawaki, M.G. Farquhar, and R.Y. Tsien. 1998. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. USA. 95:6803-6808.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 20
    • 0033579720 scopus 로고    scopus 로고
    • Dense-cored vesicles, smooth endoplasmic reticulum, and mitochondria are closely associated with non-specialized parts of plasma membrane of nerve terminals: Implications for exocytosis and calcium buffering by intraterminal organelles
    • Lysakowski, A., H. Figueras, S.D. Price, and Y.Y. Peng. 1999. Dense-cored vesicles, smooth endoplasmic reticulum, and mitochondria are closely associated with non-specialized parts of plasma membrane of nerve terminals: implications for exocytosis and calcium buffering by intraterminal organelles. J. Comp. Neurol. 403:378-390.
    • (1999) J. Comp. Neurol , vol.403 , pp. 378-390
    • Lysakowski, A.1    Figueras, H.2    Price, S.D.3    Peng, Y.Y.4
  • 21
    • 0035490904 scopus 로고    scopus 로고
    • The melanosome: Membrane dynamics in black and white
    • Marks, M.S., and M.C. Seabra. 2001. The melanosome: membrane dynamics in black and white. Nat. Rev. Mol. Cell Biol. 2:738-748.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 738-748
    • Marks, M.S.1    Seabra, M.C.2
  • 23
    • 0030985763 scopus 로고    scopus 로고
    • Loss, restoration, and maintenance of plasma membrane integrity
    • McNeil, P.L., and R.A. Steinhardt. 1997. Loss, restoration, and maintenance of plasma membrane integrity. J. Cell Biol. 137:1-4.
    • (1997) J. Cell Biol , vol.137 , pp. 1-4
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 25
    • 0035151221 scopus 로고    scopus 로고
    • Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules
    • Nagamatsu, S., Y. Nakamichi, T. Watanabe, S. Matsushima, S. Yamaguchi, J. Ni, E. Itagaki, and H. Ishida. 2001. Localization of cellubrevin-related peptide, endobrevin, in the early endosome in pancreatic beta cells and its physiological function in exo-endocytosis of secretory granules. J. Cell Sci. 114:219-227.
    • (2001) J. Cell Sci , vol.114 , pp. 219-227
    • Nagamatsu, S.1    Nakamichi, Y.2    Watanabe, T.3    Matsushima, S.4    Yamaguchi, S.5    Ni, J.6    Itagaki, E.7    Ishida, H.8
  • 26
    • 0035186848 scopus 로고    scopus 로고
    • Three-dimensional high voltage electron microscopy of thick biological specimens
    • Nagata, T. 2001. Three-dimensional high voltage electron microscopy of thick biological specimens. Micron. 32:387-404.
    • (2001) Micron , vol.32 , pp. 387-404
    • Nagata, T.1
  • 27
    • 0026612701 scopus 로고
    • Thrombin-induced Ca2+ mobilization in vascular smooth muscle utilizes a slowly ribosylating pertussis toxin-sensitive G protein. Evidence for the involvement of a G protein in inositol trisphosphate-dependent Ca2+ release
    • Neylon, C.B., A. Nickashin, P.J. Little, V.A. Tkachuk, and A. Bobik. 1992. Thrombin-induced Ca2+ mobilization in vascular smooth muscle utilizes a slowly ribosylating pertussis toxin-sensitive G protein. Evidence for the involvement of a G protein in inositol trisphosphate-dependent Ca2+ release. J. Biol. Chem. 267:7295-7302.
    • (1992) J. Biol. Chem , vol.267 , pp. 7295-7302
    • Neylon, C.B.1    Nickashin, A.2    Little, P.J.3    Tkachuk, V.A.4    Bobik, A.5
  • 28
    • 0029666286 scopus 로고    scopus 로고
    • Ca2 +-dependent exocytotic pathways in Chinese hamster ovary fibroblasts revealed by a caged-Ca2 + compound
    • Ninomiya, Y., T. Kishimoto, Y. Miyashita, and H. Kasai. 1996. Ca2 +-dependent exocytotic pathways in Chinese hamster ovary fibroblasts revealed by a caged-Ca2 + compound. J. Biol. Chem. 271:17751-17754.
    • (1996) J. Biol. Chem , vol.271 , pp. 17751-17754
    • Ninomiya, Y.1    Kishimoto, T.2    Miyashita, Y.3    Kasai, H.4
  • 29
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade, G.E. 1975. Intracellular aspects of the process of protein secretion. Science. 189:347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 30
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes
    • Reddy, A., E.V. Caler, and N.W. Andrews. 2001. Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes. Cell. 106:157-169.
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 32
    • 0030615262 scopus 로고    scopus 로고
    • Lysosomes behave as Ca2 +-regulated exocytic vesicles in fibroblasts and epithelial cells
    • Rodriguez, A., P. Webster, J. Ortego, and N.W. Andrews. 1997. Lysosomes behave as Ca2 +-regulated exocytic vesicles in fibroblasts and epithelial cells. J. Cell Biol. 137:93-104.
    • (1997) J. Cell Biol , vol.137 , pp. 93-104
    • Rodriguez, A.1    Webster, P.2    Ortego, J.3    Andrews, N.W.4
  • 33
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection fluorescence microscopy
    • Schmoranzer, J., M. Goulian, D. Axelrod, and S.M. Simon. 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
  • 35
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt, R.A., G. Bi, and J.M. Alderton. 1994. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science. 263:390-393.
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 36
    • 0033523774 scopus 로고    scopus 로고
    • Regulated secretion from hemopoietic cells
    • Stinchcombe, J.C., and G.M. Griffiths. 1999. Regulated secretion from hemopoietic cells. J. Cell Biol. 147:1-6.
    • (1999) J. Cell Biol , vol.147 , pp. 1-6
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 37
    • 0033067513 scopus 로고    scopus 로고
    • The mechanism of facilitated cell membrane resealing
    • Togo, T., J.M. Alderton, G.Q. Bi, and R.A. Steinhardt. 1999. The mechanism of facilitated cell membrane resealing. J. CellSci. 112:719-731.
    • (1999) J. CellSci , vol.112 , pp. 719-731
    • Togo, T.1    Alderton, J.M.2    Bi, G.Q.3    Steinhardt, R.A.4
  • 39
    • 0027426683 scopus 로고
    • Early responses in mitogenic signaling, bombesin induced protein phosphorylations in Swiss 3T3 cells
    • Van Lint, J., P. Agostinis, W. Merlevede, and J.R. Vandenheede. 1993. Early responses in mitogenic signaling, bombesin induced protein phosphorylations in Swiss 3T3 cells. Adv. Enzyme Regul. 33:143-155.
    • (1993) Adv. Enzyme Regul , vol.33 , pp. 143-155
    • Van Lint, J.1    Agostinis, P.2    Merlevede, W.3    Vandenheede, J.R.4


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