메뉴 건너뛰기




Volumn 9, Issue 5, 1998, Pages 1053-1063

Induction of exocytosis from permeabilized mast cells by the guanosine triphosphatases RAC and Cdc42

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; GUANOSINE TRIPHOSPHATASE;

EID: 0031696158     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.5.1053     Document Type: Article
Times cited : (80)

References (50)
  • 1
    • 0028299331 scopus 로고
    • Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane
    • Abo, A., Webb, M.R., Grogan, A. and Segal, A.W. (1994), Activation of NADPH oxidase involves the dissociation of p21rac 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
    • 0027052911 scopus 로고
    • Post-translational processing of rac p21s is important both for their interaction with the GDP/GTP exchange proteins and for their activation of NADPH oxidase
    • Ando, S. et al. (1992). Post-translational processing of rac p21s is important both for their interaction with the GDP/GTP exchange proteins and for their activation of NADPH oxidase. J. Biol. Chem. 267, 25709-25713.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25709-25713
    • Ando, S.1
  • 5
    • 0025194791 scopus 로고
    • 2+-dependent lysosomal secretion in electropermeabilised human platelets
    • 2+-dependent lysosomal secretion in electropermeabilised human platelets. Eur. J. Biochem. 189, 647-655.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 647-655
    • Athayde, C.M.1    Scrutton, M.C.2
  • 6
    • 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
  • 7
    • 0027183815 scopus 로고
    • A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes
    • Bhakdi, S., Weller, U., Walev, I., Martin, E., Jonas, D., and Palmer, M. (1993). A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med. Microbiol. Immunol. 182, 167-175.
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 167-175
    • Bhakdi, S.1    Weller, U.2    Walev, I.3    Martin, E.4    Jonas, D.5    Palmer, M.6
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0023120078 scopus 로고
    • Ultrastructural demonstration of exocytosis in intact and saponin-permeabilized cultured bovine chromaffin cells
    • Brooks, J.C., and Carmichael, S.W. (1988). Ultrastructural demonstration of exocytosis in intact and saponin-permeabilized cultured bovine chromaffin cells. Am. J. Anat. 178, 85-89.
    • (1988) Am. J. Anat. , vol.178 , pp. 85-89
    • Brooks, J.C.1    Carmichael, S.W.2
  • 10
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P.D., Drechsel, D., and Hall, A. (1995). A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 12
    • 0025180735 scopus 로고
    • Isoprenylation of the low molecular mass GTP-binding proteins rac 1 and rac 2: Possible role in membrane localization
    • Didsbury, J.R., Uhing, R.J., and Snyderman, R. (1990). Isoprenylation of the low molecular mass GTP-binding proteins rac 1 and rac 2: possible role in membrane localization. Biochem. Biophys. Res. Commun. 171, 804-812.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 804-812
    • Didsbury, J.R.1    Uhing, R.J.2    Snyderman, R.3
  • 13
    • 0024425981 scopus 로고
    • rac. a novel ras-related family of proteins that are botulinum toxin substrates
    • Didsbury, J.R., 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.R.1    Weber, R.F.2    Bokoch, G.M.3    Evans, T.4    Snyderman, R.5
  • 14
    • 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
  • 15
    • 0021687960 scopus 로고
    • Capacitance measurements reveal stepwise fusion events in degranulating mast cells
    • Fernandez, J.M., Neher, E., and Gomperts, B.D. (1984). Capacitance measurements reveal stepwise fusion events in degranulating mast cells. Nature 312, 453-455.
    • (1984) Nature , vol.312 , pp. 453-455
    • Fernandez, J.M.1    Neher, E.2    Gomperts, B.D.3
  • 16
    • 0025195169 scopus 로고
    • E: A GTP-binding protein mediating exocytosis
    • E: a GTP-binding protein mediating exocytosis. Annu. Rev. Physiol. 52, 591-606.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 591-606
    • Gomperts, B.D.1
  • 18
    • 0027031323 scopus 로고
    • Regulated exocytotic secretion from permeabilized cells
    • Gomperts, B.D., and Tatham, P.E.R. (1992). Regulated exocytotic secretion from permeabilized cells. Methods Enzymol. 219, 178-189.
    • (1992) Methods Enzymol. , vol.219 , pp. 178-189
    • Gomperts, B.D.1    Tatham, P.E.R.2
  • 19
    • 0027467339 scopus 로고
    • Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase
    • Heyworth, P.G., Knaus, U.G., Xu, X., Uhlinger, D.J., Conroy, L., Bokoch, G.M., and Curnutte, J.T. (1993). Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase. Mol. Biol. Cell. 4, 261-269.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 261-269
    • Heyworth, P.G.1    Knaus, U.G.2    Xu, X.3    Uhlinger, D.J.4    Conroy, L.5    Bokoch, G.M.6    Curnutte, J.T.7
  • 21
    • 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. Membrane Biol. 68, 107-140.
    • (1982) J. Membrane Biol. , vol.68 , pp. 107-140
    • Knight, D.E.1    Baker, P.F.2
  • 22
    • 0024388422 scopus 로고
    • Soluble proteins as modulators of the exocytotic reaction of permeabilised rat mast cells
    • Koffer, A., and Gomperts, B.D. (1989). Soluble proteins as modulators of the exocytotic reaction of permeabilised 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
  • 23
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., Ahmed, S., Best, A., and Lim, L. (1995). The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell Biol. 15, 1942-1952.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 24
    • 0029779004 scopus 로고    scopus 로고
    • The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia
    • Kozma, R., Ahmed, S., Best, A., and Lim, L. (1996). The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia. Mol. Cell Biol. 16, 5069-5080.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5069-5080
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 25
    • 0027288743 scopus 로고
    • Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins
    • Kwong, C.H., Malech, H.L., Rotrosen, D., and Leto, T.L. (1993). Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry 32, 5711-5717.
    • (1993) Biochemistry , vol.32 , pp. 5711-5717
    • Kwong, C.H.1    Malech, H.L.2    Rotrosen, D.3    Leto, T.L.4
  • 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
    • 0030298138 scopus 로고    scopus 로고
    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
    • Lamarche, N., Tapon, N., Stowers, L., Burbelo, P.D., Aspenstrom, P., Bridges, T., Chant, J., and Hall, A. (1996). Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell 87, 519-529.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6    Chant, J.7    Hall, A.8
  • 28
    • 0029897366 scopus 로고    scopus 로고
    • Practical considerations regarding the use of streptolysin-O as a permeabilising agent for cells in the investigation of exocytosis
    • Larbi, K.Y., and Gomperts, B.D. (1996). Practical considerations regarding the use of streptolysin-O as a permeabilising agent for cells in the investigation of exocytosis. Biosci. Rep. 16, 11-21.
    • (1996) Biosci. Rep. , vol.16 , pp. 11-21
    • Larbi, K.Y.1    Gomperts, B.D.2
  • 29
    • 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
  • 30
    • 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
  • 31
    • 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
    • 0029803812 scopus 로고    scopus 로고
    • Rho-guanine nucleotide dissociation inhibitor protein (Rho-GDI) inhibits exocytosis in mast cells
    • Mariot, P., O'Sullivan, A.J., Brown, A.M., and Tatham, P.E.R. (1996). Rho-guanine nucleotide dissociation inhibitor protein (Rho-GDI) inhibits exocytosis in mast cells. EMBO J. 15, 6476-6482.
    • (1996) EMBO J. , vol.15 , pp. 6476-6482
    • Mariot, P.1    O'Sullivan, A.J.2    Brown, A.M.3    Tatham, P.E.R.4
  • 33
    • 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
  • 35
    • 0026705499 scopus 로고
    • Functional localization of an exocytosis-triggering G-protein in human cytotoxic T lymphocytes
    • Mittrucker, H., and Fleischer, B. (1992). Functional localization of an exocytosis-triggering G-protein in human cytotoxic T lymphocytes. Immunology 76, 610-615.
    • (1992) Immunology , vol.76 , pp. 610-615
    • Mittrucker, H.1    Fleischer, B.2
  • 36
    • 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
  • 37
    • 0029901614 scopus 로고    scopus 로고
    • Ultrastructural characterisation of tannic acid arrested degranulation of GTPgS stimulated guinea pig eosinophils
    • Newman, T.M., Tian, M., and Gomperts, B.D. (1996). Ultrastructural characterisation of tannic acid arrested degranulation of GTPgS stimulated guinea pig eosinophils. Eur. J. Cell Biol. 70, 209-220.
    • (1996) Eur. J. Cell Biol. , vol.70 , pp. 209-220
    • Newman, T.M.1    Tian, M.2    Gomperts, B.D.3
  • 39
    • 0025341908 scopus 로고
    • Intracellular application of GTP-5′-O-(3-thiotriphosphate) induces exocytotic granule fusion in guinea pig eosinophils
    • Nusse, 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
    • Nusse, O.1    Lindau, M.2    Cromwell, O.3    Kay, A.B.4    Gomperts, B.D.5
  • 40
    • 0029876343 scopus 로고    scopus 로고
    • Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilised mast cells, as a rac/rhoGDI complex
    • O'Sullivan, A.J., Brown, A.M., Freeman, H.N.M. and Gomperts, B.D. (1996), Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O permeabilised mast cells, as a rac/rhoGDI complex. Mol. Biol. Cell 7, 397-408.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 397-408
    • O'Sullivan, A.J.1    Brown, A.M.2    Freeman, H.N.M.3    Gomperts, B.D.4
  • 41
  • 42
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M.F., Ashworth, A., and Hall, A. (1995). An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 269, 1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 43
    • 0029665076 scopus 로고    scopus 로고
    • Inhibition of Fc∈RI-mediated activation of rat basophilic leukemia cells by Clostridium difficile toxin B (monoglucosyltransferase)
    • Prepens, U., Just, I., von Eichel-Streiber, C., and Aktories, K. (1996). Inhibition of Fc∈RI-mediated activation of rat basophilic leukemia cells by Clostridium difficile toxin B (monoglucosyltransferase). J. Biol. Chem. 271, 7324-7329.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7324-7329
    • Prepens, U.1    Just, I.2    Von Eichel-Streiber, C.3    Aktories, K.4
  • 44
    • 0028147401 scopus 로고
    • Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors
    • Quilliam, L.A., Kato, K., Rabun, K.M., Hisaka, M.M., Huff, S.Y., Campbell Burk, S., and Der, C.J. (1994). Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors. Mol. Cell. Biol. 14, 1113-1121.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1113-1121
    • Quilliam, L.A.1    Kato, K.2    Rabun, K.M.3    Hisaka, M.M.4    Huff, S.Y.5    Campbell Burk, S.6    Der, C.J.7
  • 45
    • 0029164774 scopus 로고
    • Purification of recombinant Rho/ Rac/G25K from Escherichia coli
    • Self, A.J., and Hall, A. (1995a). Purification of recombinant Rho/ Rac/G25K from Escherichia coli. Methods Enzymol. 256, 3-10.
    • (1995) Methods Enzymol. , vol.256 , pp. 3-10
    • Self, A.J.1    Hall, A.2
  • 46
    • 0029118307 scopus 로고
    • Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates
    • Self, A.J., and Hall, A. (1995b). Measurement of intrinsic nucleotide exchange and GTP hydrolysis rates. Methods Enzymol. 256, 67-76.
    • (1995) Methods Enzymol. , vol.256 , pp. 67-76
    • Self, A.J.1    Hall, A.2
  • 47
    • 0025686144 scopus 로고
    • Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): Identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42
    • Shinjo, K., Koland, J.G., Hart, M.J., Narasimhan, V., Johnson, D.I., Evans, T., and Cerione, R.A. (1990). Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc. Natl. Acad. Sci. USA 87, 9853-9857.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9853-9857
    • Shinjo, K.1    Koland, J.G.2    Hart, M.J.3    Narasimhan, V.4    Johnson, D.I.5    Evans, T.6    Cerione, R.A.7
  • 48
    • 0027952703 scopus 로고
    • Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility
    • Takaishi, K., Sasaki, T., Kato, M., Yamochi, W., Kuroda, S., Nakamura, T., Takeichi, M., and Takai, Y. (1994). Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility. Oncogene 9, 273-279.
    • (1994) Oncogene , vol.9 , pp. 273-279
    • Takaishi, K.1    Sasaki, T.2    Kato, M.3    Yamochi, W.4    Kuroda, S.5    Nakamura, T.6    Takeichi, M.7    Takai, Y.8
  • 49
    • 0010328641 scopus 로고
    • Cell permeabilisation
    • ed. K. Siddle and J.C. Hutton, Oxford, United Kingdom, IRL Press
    • Tatham, P.E.R., and Gomperts, B.D. (1990). Cell permeabilisation. In: Peptide Hormones - A Practical Approach, ed. K. Siddle and J.C. Hutton, Oxford, United Kingdom, IRL Press, 257-269.
    • (1990) Peptide Hormones - A Practical Approach , pp. 257-269
    • Tatham, P.E.R.1    Gomperts, B.D.2
  • 50
    • 0028842508 scopus 로고
    • Identification and molecular cloning of a p21cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets
    • Teo, M., Manser, E., and Lim, L. (1995). Identification and molecular cloning of a p21cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets. J. Biol. Chem. 270, 26690-26697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26690-26697
    • Teo, M.1    Manser, E.2    Lim, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.