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Volumn 17, Issue 18, 1998, Pages 5298-5308

The Golgi apparatus is an inositol 1,4,5-trisphosphate-sensitive Ca2+ store, with functional properties distinct from those of the endoplasmic reticulum

Author keywords

Ca2+ store; Golgi apparatus; Inositol 1,4,5 trisphosphate

Indexed keywords

CALCIUM ION; CALRETICULIN; HISTAMINE; INOSITOL 1,4,5 TRISPHOSPHATE; PHOTOPROTEIN;

EID: 0032530396     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.18.5298     Document Type: Article
Times cited : (389)

References (40)
  • 1
    • 0027097849 scopus 로고
    • The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • Antebi, A. and Fink, G.R. (1992) The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell. 3, 633-654.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 2
    • 0030069359 scopus 로고    scopus 로고
    • Prosomatostatin processing in permeabilized cells. Calcium is required for prohormone cleavage but not formation of nascent secretory vesicles
    • Austin, C.D. and Shields, D. (1996) Prosomatostatin processing in permeabilized cells. Calcium is required for prohormone cleavage but not formation of nascent secretory vesicles. J. Biol. Chem., 271, 1194-1199.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1194-1199
    • Austin, C.D.1    Shields, D.2
  • 3
    • 0030613252 scopus 로고    scopus 로고
    • 2+] in the endoplasmic reticulum and cytoplasm of intact HeLa cells: A comparative study
    • 2+] in the endoplasmic reticulum and cytoplasm of intact HeLa cells: a comparative study. J. Biol. Chem., 272, 27694-27699.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27694-27699
    • Barrero, M.J.1    Montero, M.2    Alvarez, J.3
  • 8
    • 0025975040 scopus 로고
    • The calcium pumping ATPase of the plasma membrane
    • Carafoli, E. (1991) The calcium pumping ATPase of the plasma membrane. Annu. Rev. Physiol., 53, 531-547.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 531-547
    • Carafoli, E.1
  • 9
    • 0028131971 scopus 로고
    • Transport via the regulated secretory pathway in semi-intact PC12 cells: Role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II
    • Carnell, L. and Moore, H.P. (1994) Transport via the regulated secretory pathway in semi-intact PC12 cells: role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II. J. Cell Biol., 127, 693-705.
    • (1994) J. Cell Biol. , vol.127 , pp. 693-705
    • Carnell, L.1    Moore, H.P.2
  • 10
    • 0019395366 scopus 로고
    • 2+-pumping ATPase of heart sarcolemma. Characterization, calmodulin dependence, and partial purification
    • 2+-pumping ATPase of heart sarcolemma. Characterization, calmodulin dependence, and partial purification. J. Biol. Chem., 256, 3263-3270.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3263-3270
    • Caroni, P.1    Carafoli, E.2
  • 11
    • 0028239365 scopus 로고
    • Imaging of total intracellular calcium and calcium influx and efflux in individual resting and stimulated tumor mast cells using ion microscopy
    • Chandra, S., Fewtrell, C., Millard, P.J., Sandison, D.R., Webb, W.W. and Morrison, G.H. (1994) Imaging of total intracellular calcium and calcium influx and efflux in individual resting and stimulated tumor mast cells using ion microscopy. J. Biol. Chem., 269, 15186-15194.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15186-15194
    • Chandra, S.1    Fewtrell, C.2    Millard, P.J.3    Sandison, D.R.4    Webb, W.W.5    Morrison, G.H.6
  • 13
    • 0028890152 scopus 로고
    • 2+)-ATPase and inositol 1,4,5-trisphosphate receptor in human platelet membranes
    • 2+)-ATPase and inositol 1,4,5-trisphosphate receptor in human platelet membranes. Cell Calcium, 17, 65-70.
    • (1995) Cell Calcium , vol.17 , pp. 65-70
    • Dean, W.L.1    Quinton, T.M.2
  • 14
    • 0030016030 scopus 로고    scopus 로고
    • 2+ depletion on the synthesis, phosphorylation and secretion of caseins in lactating mammary epithelial cells
    • 2+ depletion on the synthesis, phosphorylation and secretion of caseins in lactating mammary epithelial cells. Biochem. J., 317, 487-493.
    • (1996) Biochem. J. , vol.317 , pp. 487-493
    • Duncan, J.S.1    Burgoyne, R.D.2
  • 15
    • 0024004720 scopus 로고
    • Purification of a RAS-responsive adenyl-cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method
    • Field, J., Nikawa, J., Broeck, D., MacDonald, B., Rodgers, L., Wilson, I.A., Lerner, R.A. and Wigler, M. (1988) Purification of a RAS-responsive adenyl-cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. Mol. Cell. Biol., 8, 2159-2165.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2159-2165
    • Field, J.1    Nikawa, J.2    Broeck, D.3    MacDonald, B.4    Rodgers, L.5    Wilson, I.A.6    Lerner, R.A.7    Wigler, M.8
  • 17
    • 0029034566 scopus 로고
    • Spatial distribution and quantitation of free lumenal [Ca] within the InsP3-sensitive internal store of individual BHK-21 cells: Ion dependence of InsP3-induced Ca release and reloading
    • Hofer, A.M., Schlue, W.-R., Curci, S. and Machen, T.E. (1995) Spatial distribution and quantitation of free lumenal [Ca] within the InsP3-sensitive internal store of individual BHK-21 cells: ion dependence of InsP3-induced Ca release and reloading. FASEB J., 9, 788-798.
    • (1995) FASEB J. , vol.9 , pp. 788-798
    • Hofer, A.M.1    Schlue, W.-R.2    Curci, S.3    Machen, T.E.4
  • 21
    • 0001307877 scopus 로고    scopus 로고
    • Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor
    • Kim, J.H., Lingwood, C.A., Williams, D.B., Furuya, W., Manolson, M.F. and Grinstein, S. (1996) Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor. J. Cell Biol., 134, 1387-1399.
    • (1996) J. Cell Biol. , vol.134 , pp. 1387-1399
    • Kim, J.H.1    Lingwood, C.A.2    Williams, D.B.3    Furuya, W.4    Manolson, M.F.5    Grinstein, S.6
  • 22
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K.H. and Michalak, M. (1997) Calreticulin. Cell, 88, 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.H.1    Michalak, M.2
  • 24
    • 0027172770 scopus 로고
    • Mutational analysis of the Golgi retention signal of bovine
    • Masibay, A.S., Balaji, P.V., Boeggeman, E.E. and Qasba, P.K. (1993) Mutational analysis of the Golgi retention signal of bovine. J. Biol. Chem., 268, 9908-9916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9908-9916
    • Masibay, A.S.1    Balaji, P.V.2    Boeggeman, E.E.3    Qasba, P.K.4
  • 30
    • 0020961054 scopus 로고
    • Immunocytochemical localization of alpha-D-mannosidase II in the Golgi apparatus of rat liver
    • Novikoff, P.M., Tulsiani, D.R., Touster, O., Yam, A. and Novikoff, A.B. (1983) Immunocytochemical localization of alpha-D-mannosidase II in the Golgi apparatus of rat liver. Proc. Natl Acad. Sci. USA, 80, 4364-4368.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 4364-4368
    • Novikoff, P.M.1    Tulsiani, D.R.2    Touster, O.3    Yam, A.4    Novikoff, A.B.5
  • 31
    • 0030250996 scopus 로고    scopus 로고
    • 2+ be released from secretory granules or synaptic vesicles?
    • 2+ be released from secretory granules or synaptic vesicles? Trends Neurosci., 19, 411-413.
    • (1996) Trends Neurosci. , vol.19 , pp. 411-413
    • Petersen, O.H.1
  • 32
    • 0030982434 scopus 로고    scopus 로고
    • High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system
    • Pezzati, R., Bossi, M., Podini, P. Meldolesi, J. and Grohovaz, F. (1997) High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Mol. Biol. Cell, 8, 1501-1512.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1501-1512
    • Pezzati, R.1    Bossi, M.2    Podini, P.3    Meldolesi, J.4    Grohovaz, F.5
  • 36
    • 0030087711 scopus 로고    scopus 로고
    • Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo
    • Rizzuto, R., Brini, M., De Giorgi, F., Rossi, R., Heim, R., Tsien, R.Y. and Pozzan, T. (1996) Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo. Curr. Biol., 6, 183-188.
    • (1996) Curr. Biol. , vol.6 , pp. 183-188
    • Rizzuto, R.1    Brini, M.2    De Giorgi, F.3    Rossi, R.4    Heim, R.5    Tsien, R.Y.6    Pozzan, T.7
  • 39
    • 0024326031 scopus 로고
    • Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles
    • Van, P.N., Peter, F. and Soling, H.D. (1989) Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. No indication for calsequestrin-like proteins in inositol 1,4,5-trisphosphate-sensitive calcium sequestering rat liver vesicles. J. Biol. Clin., 264, 17494-17501.
    • (1989) J. Biol. Clin. , vol.264 , pp. 17494-17501
    • Van, P.N.1    Peter, F.2    Soling, H.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.