메뉴 건너뛰기




Volumn 393, Issue 1-2, 2012, Pages 77-84

Protection from Clostridium difficile toxin B-catalysed Rac1/Cdc42 glucosylation by tauroursodeoxycholic acid-induced Rac1/Cdc42 phosphorylation

Author keywords

Actin cytoskeleton; Akt kinase; Bile acid; Cytopathic effect

Indexed keywords

BILE ACID; CLOSTRIDIUM DIFFICILE TOXIN B; PROTEIN CDC42; PROTEIN KINASE B; RAC1 PROTEIN; RHO FACTOR; TAUROURSODEOXYCHOLIC ACID;

EID: 84856197124     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC-2011-198     Document Type: Article
Times cited : (22)

References (29)
  • 1
    • 77957833800 scopus 로고    scopus 로고
    • The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane
    • Berndt, N., Yang, H., Trinczek, B., Betzi, S., Zhang, Z., Wu, B., Lawrence, N.J., Pellecchia, M., Schonbrunn, E., Cheng, J.Q., et al. (2010). The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane. Cell Death Differ. 17, 1795-1804.
    • (2010) Cell Death Differ. , vol.17 , pp. 1795-1804
    • Berndt, N.1    Yang, H.2    Trinczek, B.3    Betzi, S.4    Zhang, Z.5    Wu, B.6    Lawrence, N.J.7    Pellecchia, M.8    Schonbrunn, E.9    Cheng, J.Q.10
  • 2
    • 32944455840 scopus 로고    scopus 로고
    • Conjugated bile acids promote ERK1/2 and AKT activation via a pertussis toxin-sensitive mechanism in murine and human hepatocytes
    • DOI 10.1002/hep.20942
    • Dent, P., Fang, Y., Gupta, S., Studer, E., Mitchell, C., Spiegel, S., and Hylemon, P.B. (2005). Conjugated bile acids promote ERK1/2 and AKT activation via a pertussis toxin-sensitive mechanism in murine and human hepatocytes. Hepatology 42, 1291-1299. (Pubitemid 43260031)
    • (2005) Hepatology , vol.42 , Issue.6 , pp. 1291-1299
    • Dent, P.1    Fang, Y.2    Gupta, S.3    Studer, E.4    Mitchell, G.5    Spiegel, S.6    Hylemon, P.B.7
  • 3
    • 18544379580 scopus 로고    scopus 로고
    • Actin polymerization machinery: The finish line of signaling networks, the starting point of cellular movement
    • DOI 10.1007/s00018-004-4472-6
    • Disanza, A., Steffen, A., Hertzog, M., Frittoli, E., Rottner, K., and Scita, G. (2005). Actin polymerization machinery: the finish line of signaling networks, the starting point of cellular movement. Cell Mol. Life Sci. 62, 955-970. (Pubitemid 40655613)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.9 , pp. 955-970
    • Disanza, A.1    Steffen, A.2    Hertzog, M.3    Frittoli, E.4    Rottner, K.5    Scita, G.6
  • 4
    • 64349095054 scopus 로고    scopus 로고
    • Killing of rat basophilic leukemia cells by lethal toxin from Clostridium sordellii : critical role of phosphatidylinositide 3'-OH kinase/Akt signaling
    • Dreger, S.C., Schulz, F., Huelsenbeck, J., Gerhard, R., Hofmann, F., Just, I., and Genth, H. (2009). Killing of rat basophilic leukemia cells by lethal toxin from Clostridium sordellii : critical role of phosphatidylinositide 3'-OH kinase/Akt signaling. Biochemistry 48, 1785-1792.
    • (2009) Biochemistry , vol.48 , pp. 1785-1792
    • Dreger, S.C.1    Schulz, F.2    Huelsenbeck, J.3    Gerhard, R.4    Hofmann, F.5    Just, I.6    Genth, H.7
  • 5
    • 34548472183 scopus 로고    scopus 로고
    • Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity
    • DOI 10.1074/jbc.M703062200
    • Egerer, M., Giesemann, T., Jank, T., Satchell, K.J., and Aktories, K. (2007). Auto-catalytic cleavage of Clostridium difficile toxins A and B depends on cysteine protease activity. J. Biol. Chem. 282, 25314-25321. (Pubitemid 47372781)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25314-25321
    • Egerer, M.1    Giesemann, T.2    Jank, T.3    Fullner Satchell, K.J.4    Aktories, K.5
  • 6
    • 0037805583 scopus 로고    scopus 로고
    • Serine phosphorylation negatively regulates RhoA in vivo
    • DOI 10.1074/jbc.M213066200
    • Ellerbroek, S.M., Wennerberg, K., and Burridge, K. (2003). Serine phosphorylation negatively regulates RhoA in vivo. J. Biol. Chem. 278, 19023-19031. (Pubitemid 36799287)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 19023-19031
    • Ellerbroek, S.M.1    Wennerberg, K.2    Burridge, K.3
  • 7
    • 0030582768 scopus 로고    scopus 로고
    • Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii
    • DOI 10.1006/bbrc.1996.1812
    • Genth, H., Hofmann, F., Selzer, J., Rex, G., Aktories, K., and Just, I. (1996). Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii. Biochem. Biophys. Res. Commun. 229, 370-374. (Pubitemid 27029039)
    • (1996) Biochemical and Biophysical Research Communications , vol.229 , Issue.2 , pp. 370-374
    • Genth, H.1    Hofmann, F.2    Selzer, J.3    Rex, G.4    Aktories, K.5    Just, I.6
  • 8
    • 0033976505 scopus 로고    scopus 로고
    • New method to generate enzymatically deficient Clostridium difficile toxin B as an antigen for immunization
    • DOI 10.1128/IAI.68.3.1094-1101.2000
    • Genth, H., Selzer, J., Busch, C., Dumbach, J., Hofmann, F., Aktories, K., and Just, I. (2000). New method to generate enzymatically deficient Clostridium difficile toxin B as an antigen for immunization. Infect. Immun. 68, 1094-1101. (Pubitemid 30108496)
    • (2000) Infection and Immunity , vol.68 , Issue.3 , pp. 1094-1101
    • Genth, H.1    Selzer, J.2    Busch, C.3    Dumbach, J.4    Hofmann, F.5    Aktories, K.6    Just, I.7
  • 9
    • 33646942752 scopus 로고    scopus 로고
    • Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B
    • DOI 10.1016/j.febslet.2006.04.100, PII S0014579306006314
    • Genth, H., Huelsenbeck, J., Hartmann, B., Hofmann, F., Just, I., and Gerhard, R. (2006). Cellular stability of Rho-GTPases glucosylated by Clostridium difficile toxin B. FEBS Lett. 580, 3565-3569. (Pubitemid 43795899)
    • (2006) FEBS Letters , vol.580 , Issue.14 , pp. 3565-3569
    • Genth, H.1    Huelsenbeck, J.2    Hartmann, B.3    Hofmann, F.4    Just, I.5    Gerhard, R.6
  • 10
    • 39649088950 scopus 로고    scopus 로고
    • Clostridium difficile toxins: More than mere inhibitors of Rho proteins
    • Genth, H., Dreger, S.C., Huelsenbeck, J., and Just, I. (2008). Clostridium difficile toxins: more than mere inhibitors of Rho proteins. Int. J. Biochem. Cell Biol. 40, 592-597.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 592-597
    • Genth, H.1    Dreger, S.C.2    Huelsenbeck, J.3    Just, I.4
  • 11
    • 0142135588 scopus 로고    scopus 로고
    • Glucosylation of Ras by Clostridium sordellii Lethal Toxin: Consequences for Effector Loop Conformations Observed by NMR Spectroscopy
    • DOI 10.1021/bi034529v
    • Geyer, M., Wilde, C., Selzer, J., Aktories, K., and Kalbitzer, H.R. (2003). Glucosylation of Ras by Clostridium sordellii lethal toxin: consequences for effector loop conformations observed by NMR spectroscopy. Biochemistry 42, 11951-11959. (Pubitemid 37280645)
    • (2003) Biochemistry , vol.42 , Issue.41 , pp. 11951-11959
    • Geyer, M.1    Wilde, C.2    Selzer, J.3    Aktories, K.4    Kalbitzer, H.R.5
  • 12
    • 3543117821 scopus 로고    scopus 로고
    • The development of phosphatidylinositol ether lipid analogues as inhibitors of the serine/threonine kinase, Akt
    • DOI 10.1517/13543784.13.7.787
    • Gills, J.J. and Dennis, P.A. (2004). The development of phosphatidylinositol ether lipid analogues as inhibitors of the serine/ threonine kinase, Akt. Expert Opin. Investig. Drugs 13, 787-797. (Pubitemid 39028931)
    • (2004) Expert Opinion on Investigational Drugs , vol.13 , Issue.7 , pp. 787-797
    • Gills, J.J.1    Dennis, P.A.2
  • 13
    • 84954358174 scopus 로고    scopus 로고
    • Prevention of the cytopathic effect induced by Clostridium difficile Toxin B by active Rac1
    • Halabi-Cabezon, I., Huelsenbeck, J., May, M., Ladwein, M., Rottner, K., Just, I., and Genth, H. (2008). Prevention of the cytopathic effect induced by Clostridium difficile Toxin B by active Rac1. FEBS Lett. 582, 3751-3756.
    • (2008) FEBS Lett. , vol.582 , pp. 3751-3756
    • Halabi-Cabezon, I.1    Huelsenbeck, J.2    May, M.3    Ladwein, M.4    Rottner, K.5    Just, I.6    Genth, H.7
  • 14
    • 70350222202 scopus 로고    scopus 로고
    • Inhibition of cytokinesis by Clostridium difficile toxin B and cytotoxic necrotizing factors - Reinforcing the critical role of RhoA in cytokinesis
    • Huelsenbeck, S.C., May, M., Schmidt, G., and Genth, H. (2009). Inhibition of cytokinesis by Clostridium difficile toxin B and cytotoxic necrotizing factors - reinforcing the critical role of RhoA in cytokinesis. Cell Motil. Cytoskeleton 66, 967-975.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 967-975
    • Huelsenbeck, S.C.1    May, M.2    Schmidt, G.3    Genth, H.4
  • 15
    • 36849050145 scopus 로고    scopus 로고
    • Clostridium difficile glucosyltransferase toxin B-essential amino acids for substrate binding
    • DOI 10.1074/jbc.M703138200
    • Jank, T., Giesemann, T., and Aktories, K. (2007). Clostridium difficile glucosyltransferase toxin B - essential amino acids for substrate binding. J. Biol. Chem. 282, 35222-35231. (Pubitemid 350232434)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 35222-35231
    • Jank, T.1    Giesemann, T.2    Aktories, K.3
  • 17
    • 0034614606 scopus 로고    scopus 로고
    • Akt protein kinase inhibits Rac1-GTP binding through phosphorylation at serine 71 of Rac1
    • DOI 10.1074/jbc.275.1.423
    • Kwon, T., Kwon, D.Y., Chun, J., Kim, J.H., and Kang, S.S. (2000). Akt protein kinase inhibits Rac1-GTP binding through phosphorylation at serine 71 of Rac1. J. Biol. Chem. 275, 423-428. (Pubitemid 30039001)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 423-428
    • Kwon, T.1    Kwon, D.Y.2    Chun, J.3    Kim, J.H.4    Kang, S.S.5
  • 18
    • 0030040750 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes
    • Lang, P., Gesbert, F., Delespine-Carmagnat, M., Stancou, R., Pouchelet, M., and Bertoglio, J. (1996). Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. EMBO J. 15, 510-519. (Pubitemid 26044564)
    • (1996) EMBO Journal , vol.15 , Issue.3 , pp. 510-519
    • Lang, P.1    Gesbert, F.2    Delespine-Carmagnat, M.3    Stancou, R.4    Pouchelet, M.5    Bertoglio, J.6
  • 19
    • 78649357145 scopus 로고    scopus 로고
    • Rational design of inhibitors and activity-based probes targeting Clostridium difficile virulence factor TcdB
    • Puri, A.W., Lupardus, P.J., Deu, E., Albrow, V.E., Garcia, K.C., Bogyo, M., and Shen, A. (2010). Rational design of inhibitors and activity-based probes targeting Clostridium difficile virulence factor TcdB. Chem. Biol. 17, 1201-1211.
    • (2010) Chem. Biol. , vol.17 , pp. 1201-1211
    • Puri, A.W.1    Lupardus, P.J.2    Deu, E.3    Albrow, V.E.4    Garcia, K.C.5    Bogyo, M.6    Shen, A.7
  • 21
    • 72749094547 scopus 로고    scopus 로고
    • Serine-71 phosphorylation of Rac1/Cdc42 diminishes the pathogenic effect of Clostridium difficile toxin A
    • Schoentaube, J., Olling, A., Tatge, H., Just, I., and Gerhard, R. (2009). Serine-71 phosphorylation of Rac1/Cdc42 diminishes the pathogenic effect of Clostridium difficile toxin A. Cell Microbiol. 11, 1816-1826.
    • (2009) Cell Microbiol. , vol.11 , pp. 1816-1826
    • Schoentaube, J.1    Olling, A.2    Tatge, H.3    Just, I.4    Gerhard, R.5
  • 22
    • 70349439436 scopus 로고    scopus 로고
    • Prevention of Clostridium sordellii lethal toxin-induced apoptotic cell death by tauroursodeoxycholic acid
    • Schulz, F., Just, I., and Genth, H. (2009). Prevention of Clostridium sordellii lethal toxin-induced apoptotic cell death by tauroursodeoxycholic acid. Biochemistry 48, 9002-9010.
    • (2009) Biochemistry , vol.48 , pp. 9002-9010
    • Schulz, F.1    Just, I.2    Genth, H.3
  • 23
    • 0032515914 scopus 로고    scopus 로고
    • Glucosylation and ADP ribosylation of Rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling
    • DOI 10.1021/bi972592c
    • Sehr, P., Joseph, G., Genth, H., Just, I., Pick, E., and Aktories, K. (1998). Glucosylation and ADP-ribosylation of Rho proteins - effects on nucleotide binding, GTPase activity, and effector-coupling. Biochemistry 37, 5296-5304. (Pubitemid 28176531)
    • (1998) Biochemistry , vol.37 , Issue.15 , pp. 5296-5304
    • Sehr, P.1    Joseph, G.2    Genth, H.3    Just, I.4    Pick, E.5    Aktories, K.6
  • 24
    • 0029823945 scopus 로고    scopus 로고
    • Clostridium novyi α-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins
    • DOI 10.1074/jbc.271.41.25173
    • Selzer, J., Hofmann, F., Rex, G., Wilm, M., Mann, M., Just, I., and Aktories, K. (1996). Clostridium novyi α-toxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins. J. Biol. Chem. 271, 25173-25177. (Pubitemid 26337878)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25173-25177
    • Selzer, J.1    Hofmann, F.2    Rex, G.3    Wilm, M.4    Mann, M.5    Just, I.6    Aktories, K.7
  • 25
    • 34247181117 scopus 로고    scopus 로고
    • Game and players: Mitochondrial apoptosis and the therapeutic potential of ursodeoxycholic acid
    • Sola, S., Aranha, M.M., Steer, C.J., and Rodrigues, C.M. (2007). Game and players: mitochondrial apoptosis and the therapeutic potential of ursodeoxycholic acid. Curr. Issues Mol. Biol. 9, 123-138. (Pubitemid 46614349)
    • (2007) Current Issues in Molecular Biology , vol.9 , Issue.2 , pp. 123-138
    • Sola, S.1    Aranha, M.M.2    Steer, C.J.3    Rodrigues, C.M.P.4
  • 26
    • 79551522234 scopus 로고    scopus 로고
    • Current status of nonantibiotic and adjunct therapies for Clostridium difficile infection
    • Suwantarat, N. and Bobak, D.A. (2011). Current status of nonantibiotic and adjunct therapies for Clostridium difficile infection. Curr. Infect. Dis. Rep. 13, 21-27.
    • (2011) Curr. Infect. Dis. Rep. , vol.13 , pp. 21-27
    • Suwantarat, N.1    Bobak, D.A.2
  • 27
    • 0034283341 scopus 로고    scopus 로고
    • Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin
    • Vetter, I.R., Hofmann, F., Wohlgemuth, S., Herrmann, C., and Just, I. (2000). Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin. J. Mol. Biol. 301, 1091-1095.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1091-1095
    • Vetter, I.R.1    Hofmann, F.2    Wohlgemuth, S.3    Herrmann, C.4    Just, I.5
  • 28
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • DOI 10.1128/CMR.18.2.247-263.2005
    • Voth, D.E. and Ballard, J. (2005). Clostridium difficile toxins: mechanism of action and role in disease. Clin. Microbiol. Rev. 18, 247-263. (Pubitemid 40548293)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 29
    • 0034595678 scopus 로고    scopus 로고
    • Recognition of RhoA by Clostridium botulinum C3 exoenzyme
    • DOI 10.1074/jbc.M910362199
    • Wilde, C., Genth, H., Aktories, K., and Just I. (2000). Recognition of RhoA by Clostridium botulinum C3 exoenzyme. J. Biol. Chem. 275, 16478-16483. (Pubitemid 30398869)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16478-16483
    • Wilde, C.1    Genth, H.2    Aktories, K.3    Just, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.