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Volumn 7, Issue 3, 1996, Pages 397-408

Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilized mast cells, as a Rac/RhoGDI complex

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CYTOSOL PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); N ACETYL BETA GLUCOSAMINIDASE; STREPTOLYSIN O; UNCLASSIFIED DRUG;

EID: 0029876343     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.3.397     Document Type: Article
Times cited : (52)

References (53)
  • 1
    • 0028299331 scopus 로고
    • rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane
    • rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane. Biochem. J. 298, 585-591.
    • (1994) Biochem. J. , vol.298 , pp. 585-591
    • Abo, A.1    Webb, M.R.2    Grogan, A.3    Segal, A.W.4
  • 2
    • 0025291478 scopus 로고
    • The stimulatory effect of calpactin (annexin II) on calcium-dependent exocytosis in chromaffin cells: Requirement for both the N-terminal and core domains of p36 and ATP
    • Ali, S.M , and Burgoyne, R.D. (1990). The stimulatory effect of calpactin (annexin II) on calcium-dependent exocytosis in chromaffin cells: requirement for both the N-terminal and core domains of p36 and ATP. Cell. Signalling 2, 265-276.
    • (1990) Cell. Signalling , vol.2 , pp. 265-276
    • Ali, S.M.1    Burgoyne, R.D.2
  • 3
    • 0025075352 scopus 로고
    • Exocytosis in mast cells by basic secretagogues: Evidence for direct activation of GTP-binding proteins
    • Aridor, M., Traub, L.M., and Sagi-Eisenberg, R. (1990). Exocytosis in mast cells by basic secretagogues: evidence for direct activation of GTP-binding proteins. J. Cell Biol. 111, 909-917.
    • (1990) J. Cell Biol. , vol.111 , pp. 909-917
    • Aridor, M.1    Traub, L.M.2    Sagi-Eisenberg, R.3
  • 5
    • 0022648103 scopus 로고
    • Two roles for guanine nucleotides in the stimulus secretion sequence of neutrophils
    • Barrowman, M.M., Cockcroft, S., and Gomperts, B.D (1986). Two roles for guanine nucleotides in the stimulus secretion sequence of neutrophils. Nature 319, 504-507.
    • (1986) Nature , vol.319 , pp. 504-507
    • Barrowman, M.M.1    Cockcroft, S.2    Gomperts, B.D.3
  • 6
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch, G.M., Bohl, B.P., and Chuang, T.H. (1994). Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269, 31674-31679.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 7
    • 0028987954 scopus 로고
    • Physiological effects of inverse agonists in transgenic mice with myocardial overexpression of the β-adrenoceptor
    • Bond, R.A., et al. (1995). Physiological effects of inverse agonists in transgenic mice with myocardial overexpression of the β-adrenoceptor. Nature 374, 272-276.
    • (1995) Nature , vol.374 , pp. 272-276
    • Bond, R.A.1
  • 8
    • 0027372389 scopus 로고
    • Neutrophil phospholipase D is activated by a membrane-associated rho family small molecular weight GTP-binding protein
    • Bowman, E.P., Uhlinger, D.J., and Lambeth, J.D. (1993). Neutrophil phospholipase D is activated by a membrane-associated rho family small molecular weight GTP-binding protein. J. Biol. Chem. 268, 21509-21512.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21509-21512
    • Bowman, E.P.1    Uhlinger, D.J.2    Lambeth, J.D.3
  • 9
    • 0028226187 scopus 로고
    • The GDP-bound form of the small G protein rac1 is a potent activator of the superoxide-forming NADPH oxidase of macrophages
    • Bromberg, Y., Shani, E., Joseph, G., Gorzalczany, Y., Sperling, O., and Pick, E. (1994). The GDP-bound form of the small G protein rac1 is a potent activator of the superoxide-forming NADPH oxidase of macrophages. J. Biol. Chem. 269, 7055-7058.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7055-7058
    • Bromberg, Y.1    Shani, E.2    Joseph, G.3    Gorzalczany, Y.4    Sperling, O.5    Pick, E.6
  • 12
    • 0024425981 scopus 로고
    • rac: A novel ras-related family of proteins that are botulinum toxin substrates
    • Didsbury, J., Weber, R.F., Bokoch, G.M., Evans, T., and Snyderman, R. (1989). rac: a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264, 16378-16382.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16378-16382
    • Didsbury, J.1    Weber, R.F.2    Bokoch, G.M.3    Evans, T.4    Snyderman, R.5
  • 13
    • 0016317358 scopus 로고
    • Studies on the role of calcium ions in the stimulation by adrenaline of amylase release from rat parotid
    • Dormer, R.L., and Ashcroft, S.J.H. (1974). Studies on the role of calcium ions in the stimulation by adrenaline of amylase release from rat parotid. Biochem. J. 144, 543-550.
    • (1974) Biochem. J. , vol.144 , pp. 543-550
    • Dormer, R.L.1    Ashcroft, S.J.H.2
  • 16
    • 0027031323 scopus 로고
    • Regulated exocytotic secretion from permeabilized cells
    • ed. J. Rothman, New York: Academic Press
    • Gomperts, B.D., and Tatham, P.E.R. (1992). Regulated exocytotic secretion from permeabilized cells. In: Methods in Enzymology, ed. J. Rothman, New York: Academic Press, 178-189.
    • (1992) Methods in Enzymology , pp. 178-189
    • Gomperts, B.D.1    Tatham, P.E.R.2
  • 17
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. (1994). Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10, 31-54.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 20
    • 0023374395 scopus 로고
    • 2+ and guanine nucleotides in exocytotic secretion from permeabilized mast cells
    • 2+ and guanine nucleotides in exocytotic secretion from permeabilized mast cells. J. Cell Biol. 105, 191-197.
    • (1987) J. Cell Biol. , vol.105 , pp. 191-197
    • Howell, T.W.1    Cockcroft, S.2    Gomperts, B.D.3
  • 22
    • 0025965647 scopus 로고
    • Regulation of binding of rhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor
    • Isomura, M., Kikuchi, A., Ohga, N., and Takai, Y. (1991). Regulation of binding of rhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor. Oncogene 6, 119-124.
    • (1991) Oncogene , vol.6 , pp. 119-124
    • Isomura, M.1    Kikuchi, A.2    Ohga, N.3    Takai, Y.4
  • 23
    • 0025874249 scopus 로고
    • Carboxyterminal isoprenylarion of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA
    • Kinsella, B.T., Erdman, R A., and Maltese, W.A. (1991). Carboxyterminal isoprenylarion of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J. Biol. Chem. 266, 9786-9794.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9786-9794
    • Kinsella, B.T.1    Erdman, R.A.2    Maltese, W.A.3
  • 24
    • 0020319190 scopus 로고
    • Calcium dependence of catecholamine release from bovine adrenal medullary cells after exposure to intense electric fields
    • Knight, D.E., and Baker, P.F. (1982). Calcium dependence of catecholamine release from bovine adrenal medullary cells after exposure to intense electric fields. J. Membr. Biol. 68, 107-140.
    • (1982) J. Membr. Biol. , vol.68 , pp. 107-140
    • Knight, D.E.1    Baker, P.F.2
  • 25
    • 0024388422 scopus 로고
    • Soluble proteins as modulators of the exocytotic reaction of permeabilized rat mast cells
    • Koffer, A., and Gomperts, B.D. (1989). Soluble proteins as modulators of the exocytotic reaction of permeabilized rat mast cells. J. Cell Sci. 94, 585-591.
    • (1989) J. Cell Sci. , vol.94 , pp. 585-591
    • Koffer, A.1    Gomperts, B.D.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0026445720 scopus 로고
    • 2+ is a modulator, in the exocytotic reaction of permeabilised rat mast cells
    • 2+ is a modulator, in the exocytotic reaction of permeabilised rat mast cells. Biochem. J. 288, 181-187.
    • (1992) Biochem. J. , vol.288 , pp. 181-187
    • Lillie, T.H.W.1    Gomperts, B.D.2
  • 28
    • 0027128724 scopus 로고
    • Nucleotides and divalent cations as effectors and modulators of exocytosis in permeabilised rat mast cells
    • Lillie, T.H.W., and Gomperts, B.D. (1992b). Nucleotides and divalent cations as effectors and modulators of exocytosis in permeabilised rat mast cells. Phil. Trans. Roy. Soc. Lond. B. 336, 25-34.
    • (1992) Phil. Trans. Roy. Soc. Lond. B. , vol.336 , pp. 25-34
    • Lillie, T.H.W.1    Gomperts, B.D.2
  • 29
    • 0025837076 scopus 로고
    • Techniques and concepts in exocytosis: Focus on mast cells
    • Lindau, M., and Gomperts, B.D. (1991). Techniques and concepts in exocytosis: focus on mast cells. Biochim. Biophys. Acta 1071, 429-471.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 429-471
    • Lindau, M.1    Gomperts, B.D.2
  • 30
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by cdc42 and rac1
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z., and Lim, L. (1994). A brain serine/threonine protein kinase activated by cdc42 and rac1. Nature 367, 40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 32
    • 0028231675 scopus 로고
    • Tetanus toxin and Clostridium perfringens enterotoxin as tools for the study of exocytosis
    • Matsuda, M., Okabe, T., Sugimoto, N., Senda, T., and Fujita, H. (1994). Tetanus toxin and Clostridium perfringens enterotoxin as tools for the study of exocytosis. Ann. NY Acad Sci 710, 94-106.
    • (1994) Ann. NY Acad Sci , vol.710 , pp. 94-106
    • Matsuda, M.1    Okabe, T.2    Sugimoto, N.3    Senda, T.4    Fujita, H.5
  • 33
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. (1987). Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 36
    • 0026726423 scopus 로고
    • Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells
    • Morgan, A., and Burgoyne, R.D. (1992). Interaction between protein kinase C and Exo1 (14-3-3 protein) and its relevance to exocytosis in permeabilized adrenal chromaffin cells. Biochem. J. 286, 807-811.
    • (1992) Biochem. J. , vol.286 , pp. 807-811
    • Morgan, A.1    Burgoyne, R.D.2
  • 37
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey, J.H. (1981). Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117, 307-310.
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 38
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie brilliant blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988). Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie brilliant blue G-250 and R-250. Electrophoresis 9, 255-262.
    • (1988) Electrophoresis , vol.9 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 40
    • 0028961293 scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia
    • Nobes, C.D., and Hall, A. (1995). Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 41
    • 0028070036 scopus 로고
    • Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins
    • Norman, J.C., Price, L.S., Ridley, A.J., Hall, A., and Koffer, A. (1994). Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins. J. Cell Biol. 126, 1005-1015.
    • (1994) J. Cell Biol. , vol.126 , pp. 1005-1015
    • Norman, J.C.1    Price, L.S.2    Ridley, A.J.3    Hall, A.4    Koffer, A.5
  • 42
    • 0025341908 scopus 로고
    • Intracellular application of GTP-5′-O-(3-thiotriphosphate) induces exocytotic granule fusion in guinea pig eosinophils
    • Nüsse, O., Lindau, M., Cromwell, O., Kay, A.B., and Gomperts, B.D. (1990) Intracellular application of GTP-5′-O-(3-thiotriphosphate) induces exocytotic granule fusion in guinea pig eosinophils. J. Exp. Med. 171, 775-786.
    • (1990) J. Exp. Med. , vol.171 , pp. 775-786
    • Nüsse, O.1    Lindau, M.2    Cromwell, O.3    Kay, A.B.4    Gomperts, B.D.5
  • 43
    • 0029139385 scopus 로고
    • Small GTPases, rac and rho, as regulators of secretion in mast cells
    • Price, L.S., Norman, J.C., Ridley, A.J., and Koffer, A. (1995). Small GTPases, rac and rho, as regulators of secretion in mast cells. Curr. Biol. 5, 68-73.
    • (1995) Curr. Biol. , vol.5 , pp. 68-73
    • Price, L.S.1    Norman, J.C.2    Ridley, A.J.3    Koffer, A.4
  • 44
    • 0027456952 scopus 로고
    • Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells
    • Roth, D., Morgan, A., and Burgoyne, R.D. (1993). Identification of a key domain in annexin and 14-3-3 proteins that stimulate calcium-dependent exocytosis in permeabilized adrenal chromaffin cells. FEBS Lett. 320, 207-210.
    • (1993) FEBS Lett. , vol.320 , pp. 207-210
    • Roth, D.1    Morgan, A.2    Burgoyne, R.D.3
  • 45
    • 0023245731 scopus 로고
    • Effects of ADP-ribosylation of GTP-binding protein by pertussis toxin on immunoglobulin E-dependent and -independent histamine release from mast cells and basophils
    • Saito, H., Okajima, F., Molski, T.F.P., Sha'afi, R.I., Ui, M., and Ishizaka, T. (1987). Effects of ADP-ribosylation of GTP-binding protein by pertussis toxin on immunoglobulin E-dependent and -independent histamine release from mast cells and basophils. J. Immunol. 138, 3927-3934.
    • (1987) J. Immunol. , vol.138 , pp. 3927-3934
    • Saito, H.1    Okajima, F.2    Molski, T.F.P.3    Sha'afi, R.I.4    Ui, M.5    Ishizaka, T.6
  • 46
    • 0023490531 scopus 로고
    • Loss of proteins from digitonin-permeabilized adrenal chromaffin cells essential for exocytosis
    • Sarafian, T., Aunis, D., and Bader, M. (1987). Loss of proteins from digitonin-permeabilized adrenal chromaffin cells essential for exocytosis. J. Biol. Chem. 262, 16671-16676.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16671-16676
    • Sarafian, T.1    Aunis, D.2    Bader, M.3
  • 47
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 48
    • 0027320755 scopus 로고
    • Correlation between secretion and phospholipase D activation in differentiated HL60 cells
    • Stutchfield, J., and Cockcroft, S. (1993). Correlation between secretion and phospholipase D activation in differentiated HL60 cells. Biochem. J. 293, 649-655.
    • (1993) Biochem. J. , vol.293 , pp. 649-655
    • Stutchfield, J.1    Cockcroft, S.2
  • 50
    • 0010328641 scopus 로고
    • Cell permeabilization
    • ed. K. Siddle and J.C Hutton Oxford, UK: IRL Press
    • Tatham, P.E.R., and Gomperts, B.D. (1990). Cell permeabilization In: Peptide Hormones - A Practical Approach, ed. K. Siddle and J.C Hutton Oxford, UK: IRL Press, 257-269.
    • (1990) Peptide Hormones - A Practical Approach , pp. 257-269
    • Tatham, P.E.R.1    Gomperts, B.D.2
  • 51
    • 0000663086 scopus 로고
    • Microscale alkylation with 4-vinylpyridine
    • Thomsen, J., and Bayne, S. (1988). Microscale alkylation with 4-vinylpyridine. J. Prot. Chem. 7, 295-296.
    • (1988) J. Prot. Chem. , vol.7 , pp. 295-296
    • Thomsen, J.1    Bayne, S.2
  • 52
    • 0027014517 scopus 로고
    • Dynamic changes in chromaffin cell cytoskeleton as prelude to exocytosis
    • Trifaro, J.M., Rodriguez-del-Castillo, A., and Vitale, M.L. (1992). Dynamic changes in chromaffin cell cytoskeleton as prelude to exocytosis. Mol. Neurobiol. 6, 339-358.
    • (1992) Mol. Neurobiol. , vol.6 , pp. 339-358
    • Trifaro, J.M.1    Rodriguez-del-Castillo, A.2    Vitale, M.L.3
  • 53
    • 0024385998 scopus 로고
    • Depletion of guanine nucleotides with mycophenolic acid suppresses IgE receptor-mediated degranulation in rat basophilic leukemia cells
    • Wilson, B.S., Deanin, G.G., Standefer, J C., Vanderjagt, D., and Oliver, J.M. (1989). Depletion of guanine nucleotides with mycophenolic acid suppresses IgE receptor-mediated degranulation in rat basophilic leukemia cells. J. Immunol. 143, 259-265.
    • (1989) J. Immunol. , vol.143 , pp. 259-265
    • Wilson, B.S.1    Deanin, G.G.2    Standefer, J.C.3    Vanderjagt, D.4    Oliver, J.M.5


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