메뉴 건너뛰기




Volumn 5, Issue 1, 2014, Pages

AMPylation is critical for Rab1 localization to vacuoles containing Legionella pneumophila

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; BACTERIAL PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN ANKX; PROTEIN DRRA; PROTEIN LEPB; RAB PROTEIN; UNCLASSIFIED DRUG;

EID: 84903363940     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01035-13     Document Type: Article
Times cited : (45)

References (39)
  • 2
    • 0017662282 scopus 로고
    • Legionnaires' disease: Isolation of a bacterium and demonstration of its role in other respiratory disease
    • McDade JE, Shepard CC, Fraser DW, Tsai TR, Redus MA, Dowdle WR. 1977. Legionnaires' disease: isolation of a bacterium and demonstration of its role in other respiratory disease. N. Engl. J. Med. 297:1197-1203. http:// dx.doi.org/10.1056/NEJM197712012972202.
    • (1977) N. Engl. J. Med. , vol.297 , pp. 1197-1203
    • McDade, J.E.1    Shepard, C.C.2    Fraser, D.W.3    Tsai, T.R.4    Redus, M.A.5    Dowdle, W.R.6
  • 3
    • 0032539674 scopus 로고    scopus 로고
    • Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome
    • Segal G, Purcell M, Shuman HA. 1998. Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome. Proc. Natl. Acad. Sci. U. S. A. 95: 1669-1674. http://dx.doi.org/10.1073/pnas.95.4.1669.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1669-1674
    • Segal, G.1    Purcell, M.2    Shuman, H.A.3
  • 4
    • 0032488861 scopus 로고    scopus 로고
    • Conjugative transfer by the virulence system of Legionella pneumophila
    • Vogel JP, Andrews HL, Wong SK, Isberg RR. 1998. Conjugative transfer by the virulence system of Legionella pneumophila. Science 279:873-876. http://dx.doi.org/10.1126/science.279.5352.873.
    • (1998) Science , vol.279 , pp. 873-876
    • Vogel, J.P.1    Andrews, H.L.2    Wong, S.K.3    Isberg, R.R.4
  • 5
    • 59849094765 scopus 로고    scopus 로고
    • Legionella pneumophila Dot/Icm translocated substrates: A sum of parts
    • Ensminger AW, Isberg RR. 2009. Legionella pneumophila Dot/Icm translocated substrates: a sum of parts. Curr. Opin. Microbiol. 12:67-73. http://dx.doi.org/10.1016/j.mib.2008.12.004.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 67-73
    • Ensminger, A.W.1    Isberg, R.R.2
  • 6
    • 0020591330 scopus 로고
    • Formation of a novel phagosome by the Legionnaires' disease bacterium (Legionella pneumophila) in human monocytes
    • Horwitz MA. 1983. Formation of a novel phagosome by the Legionnaires' disease bacterium (Legionella pneumophila) in human monocytes. J. Exp. Med. 158:1319-1331. http://dx.doi.org/10.1084/jem.158.4.1319.
    • (1983) J. Exp. Med. , vol.158 , pp. 1319-1331
    • Horwitz, M.A.1
  • 7
    • 0027472133 scopus 로고
    • Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila
    • Berger KH, Isberg RR. 1993. Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila. Mol. Microbiol. 7:7-19. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01092.x.
    • (1993) Mol. Microbiol. , vol.7 , pp. 7-19
    • Berger, K.H.1    Isberg, R.R.2
  • 8
    • 0029155737 scopus 로고
    • Association of Legionella pneumophila with the macrophage endoplasmic reticulum
    • Swanson MS, Isberg RR. 1995. Association of Legionella pneumophila with the macrophage endoplasmic reticulum. Infect. Immun. 63: 3609-3620.
    • (1995) Infect. Immun. , vol.63 , pp. 3609-3620
    • Swanson, M.S.1    Isberg, R.R.2
  • 9
    • 0031971194 scopus 로고    scopus 로고
    • Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake
    • Roy CR, Berger KH, Isberg RR. 1998. Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake. Mol. Microbiol. 28:663-674. http:// dx.doi.org/10.1046/j.1365-2958.1998.00841.x.
    • (1998) Mol. Microbiol. , vol.28 , pp. 663-674
    • Roy, C.R.1    Berger, K.H.2    Isberg, R.R.3
  • 10
    • 0035691622 scopus 로고    scopus 로고
    • How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: Implications for conversion of plasma membrane to the ER membrane
    • Tilney LG, Harb OS, Connelly PS, Robinson CG, Roy CR. 2001. How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane. J. Cell Sci. 114:4637-4650.
    • (2001) J. Cell Sci. , vol.114 , pp. 4637-4650
    • Tilney, L.G.1    Harb, O.S.2    Connelly, P.S.3    Robinson, C.G.4    Roy, C.R.5
  • 11
    • 0036903907 scopus 로고    scopus 로고
    • Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites
    • Kagan JC, Roy CR. 2002. Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Nat. Cell Biol. 4:945-954. http://dx.doi.org/10.1038/ncb883.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 945-954
    • Kagan, J.C.1    Roy, C.R.2
  • 12
    • 2142758690 scopus 로고    scopus 로고
    • Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system
    • Derré I, Isberg RR. 2004. Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system. Infect. Immun. 72:3048-3053. http://dx.doi.org/10.1128/ IAI.72.5.3048-3053.2004.
    • (2004) Infect. Immun. , vol.72 , pp. 3048-3053
    • Derré, I.1    Isberg, R.R.2
  • 13
    • 2442537071 scopus 로고    scopus 로고
    • Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle
    • Kagan JC, Stein MP, Pypaert M, Roy CR. 2004. Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle. J. Exp. Med. 199:1201-1211. http://dx.doi.org/10.1084/jem.20031706.
    • (2004) J. Exp. Med. , vol.199 , pp. 1201-1211
    • Kagan, J.C.1    Stein, M.P.2    Pypaert, M.3    Roy, C.R.4
  • 14
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • Nagai H, Kagan JC, Zhu X, Kahn RA, Roy CR. 2002. A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science 295:679-682. http://dx.doi.org/10.1126/science.1067025.
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 15
  • 16
    • 84889234826 scopus 로고    scopus 로고
    • Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila
    • Machner MP, Isberg RR. 2006. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev. Cell 11:47-56. http://dx.doi.org/10.1016/j.devcel.2006.05.013.
    • (2006) Dev. Cell , vol.11 , pp. 47-56
    • McHner, M.P.1    Isberg, R.R.2
  • 17
    • 33748172869 scopus 로고    scopus 로고
    • The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor
    • Murata T, Delprato A, Ingmundson A, Toomre DK, Lambright DG, Roy CR. 2006. The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nat. Cell Biol. 8:971-977. http://dx.doi.org/10.1038/ncb1463.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 971-977
    • Murata, T.1    Delprato, A.2    Ingmundson, A.3    Toomre, D.K.4    Lambright, D.G.5    Roy, C.R.6
  • 18
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • Ingmundson A, Delprato A, Lambright DG, Roy CR. 2007. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450: 365-369. http://dx.doi.org/10.1038/nature06336.
    • (2007) Nature , vol.450 , pp. 365-369
    • Ingmundson, A.1    Delprato, A.2    Lambright, D.G.3    Roy, C.R.4
  • 19
    • 84889234796 scopus 로고    scopus 로고
    • A bifunctional bacterial protein links GDI displacement to Rab1 activation
    • Machner MP, Isberg RR. 2007. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318:974-977. http://dx.doi.org/ 10.1126/science.1149121.
    • (2007) Science , vol.318 , pp. 974-977
    • McHner, M.P.1    Isberg, R.R.2
  • 20
    • 84855988874 scopus 로고    scopus 로고
    • The Legionella pneumophila effector DrrA is sufficient to stimulate SNARE-dependent membrane fusion
    • Arasaki K, Toomre DK, Roy CR. 2012. The Legionella pneumophila effector DrrA is sufficient to stimulate SNARE-dependent membrane fusion. Cell Host Microbe 11:46-57. http://dx.doi.org/10.1016/ j.chom.2011.11.009.
    • (2012) Cell Host Microbe , vol.11 , pp. 46-57
    • Arasaki, K.1    Toomre, D.K.2    Roy, C.R.3
  • 21
    • 84870229212 scopus 로고    scopus 로고
    • The role of Rab GTPases in the transport of vacuoles containing Legionella pneumophila and Coxiella burnetii
    • Hardiman CA, McDonough JA, Newton HJ, Roy CR. 2012. The role of Rab GTPases in the transport of vacuoles containing Legionella pneumophila and Coxiella burnetii. Biochem. Soc. Trans. 40:1353-1359. http:// dx.doi.org/10.1042/BST20120167.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1353-1359
    • Hardiman, C.A.1    McDonough, J.A.2    Newton, H.J.3    Roy, C.R.4
  • 22
    • 79960699136 scopus 로고    scopus 로고
    • De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
    • Neunuebel MR, Chen Y, Gaspar AH, Backlund PS, Jr, Yergey A, Machner MP. 2011. De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila. Science 333:453-456. http:// dx.doi.org/10.1126/science.1207193.
    • (2011) Science , vol.333 , pp. 453-456
    • Neunuebel, M.R.1    Chen, Y.2    Gaspar, A.H.3    Backlund Jr., P.S.4    Yergey, A.5    McHner, M.P.6
  • 23
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Müller MP, Peters H, Blümer J, Blankenfeldt W, Goody RS, Itzen A. 2010. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329:946-949. http://dx.doi.org/10.1126/ science.1192276.
    • (2010) Science , vol.329 , pp. 946-949
    • Müller, M.P.1    Peters, H.2    Blümer, J.3    Blankenfeldt, W.4    Goody, R.S.5    Itzen, A.6
  • 24
    • 80052399642 scopus 로고    scopus 로고
    • Modulation of Rab GTPase function by a protein phosphocholine transferase
    • Mukherjee S, Liu X, Arasaki K, McDonough J, Galán JE, Roy CR. 2011. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477:103-106. http://dx.doi.org/10.1038/nature10335.
    • (2011) Nature , vol.477 , pp. 103-106
    • Mukherjee, S.1    Liu, X.2    Arasaki, K.3    McDonough, J.4    Galán, J.E.5    Roy, C.R.6
  • 25
    • 79960929331 scopus 로고    scopus 로고
    • Legionella pneumophila SidD is a deAMPylase that modifies Rab1
    • Tan Y, Luo ZQ. 2011. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 475:506-509. http://dx.doi.org/10.1038/ nature10307.
    • (2011) Nature , vol.475 , pp. 506-509
    • Tan, Y.1    Luo, Z.Q.2
  • 26
    • 8444243363 scopus 로고    scopus 로고
    • Targeting Rab GTPases to distinct membrane compartments
    • Pfeffer S, Aivazian D. 2004. Targeting Rab GTPases to distinct membrane compartments. Nat. Rev. Mol. Cell Biol. 5:886-896. http://dx.doi.org/ 10.1038/nrm1500.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 886-896
    • Pfeffer, S.1    Aivazian, D.2
  • 27
    • 84855504174 scopus 로고    scopus 로고
    • Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination
    • Tan Y, Arnold RJ, Luo ZQ. 2011. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc. Natl. Acad. Sci. U. S. A. 108:21212-21217. http://dx.doi.org/10.1073/ pnas.1114023109.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 21212-21217
    • Tan, Y.1    Arnold, R.J.2    Luo, Z.Q.3
  • 28
    • 84863399784 scopus 로고    scopus 로고
    • Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins
    • Goody PR, Heller K, Oesterlin LK, Müller MP, Itzen A, Goody RS. 2012. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J. 31:1774-1784. http://dx.doi.org/ 10.1038/emboj.2012.16.
    • (2012) EMBO J. , vol.31 , pp. 1774-1784
    • Goody, P.R.1    Heller, K.2    Oesterlin, L.K.3    Müller, M.P.4    Itzen, A.5    Goody, R.S.6
  • 29
    • 72449132474 scopus 로고    scopus 로고
    • RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity
    • Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A. 2009. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol. Cell 36:1060-1072. http:// dx.doi.org/10.1016/j.molcel.2009.11.014.
    • (2009) Mol. Cell , vol.36 , pp. 1060-1072
    • Schoebel, S.1    Oesterlin, L.K.2    Blankenfeldt, W.3    Goody, R.S.4    Itzen, A.5
  • 30
    • 77955057137 scopus 로고    scopus 로고
    • High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA
    • Schoebel S, Blankenfeldt W, Goody RS, Itzen A. 2010. High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO Rep. 11:598-604. http://dx.doi.org/10.1038/ embor.2010.97.
    • (2010) EMBO Rep. , vol.11 , pp. 598-604
    • Schoebel, S.1    Blankenfeldt, W.2    Goody, R.S.3    Itzen, A.4
  • 31
    • 77949498580 scopus 로고    scopus 로고
    • Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA
    • Zhu Y, Hu L, Zhou Y, Yao Q, Liu L, Shao F. 2010. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proc. Natl. Acad. Sci. U. S. A. 107:4699-4704. http:// dx.doi.org/10.1073/pnas.0914231107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 4699-4704
    • Zhu, Y.1    Hu, L.2    Zhou, Y.3    Yao, Q.4    Liu, L.5    Shao, F.6
  • 32
    • 75049083763 scopus 로고    scopus 로고
    • Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA
    • Suh HY, Lee DW, Lee KH, Ku B, Choi SJ, Woo JS, Kim YG, Oh BH. 2010. Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA. EMBO J. 29:496-504. http:// dx.doi.org/10.1038/emboj.2009.347.
    • (2010) EMBO J. , vol.29 , pp. 496-504
    • Suh, H.Y.1    Lee, D.W.2    Lee, K.H.3    Ku, B.4    Choi, S.J.5    Woo, J.S.6    Kim, Y.G.7    Oh, B.H.8
  • 33
    • 84859564863 scopus 로고    scopus 로고
    • Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor
    • Oesterlin LK, Goody RS, Itzen A. 2012. Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proc. Natl. Acad. Sci. U. S. A. 109:5621-5626. http://dx.doi.org/ 10.1073/pnas.1121161109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 5621-5626
    • Oesterlin, L.K.1    Goody, R.S.2    Itzen, A.3
  • 34
    • 84867421460 scopus 로고    scopus 로고
    • Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1
    • Muller MP, Shkumatov AV, Oesterlin LK, Schoebel S, Goody PR, Goody RS, Itzen A. 2012. Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1. J. Biol. Chem. 287:35036-35046. http://dx.doi.org/10.1074/jbc.M112.396861.
    • (2012) J. Biol. Chem. , vol.287 , pp. 35036-35046
    • Muller, M.P.1    Shkumatov, A.V.2    Oesterlin, L.K.3    Schoebel, S.4    Goody, P.R.5    Goody, R.S.6    Itzen, A.7
  • 35
    • 46249111623 scopus 로고    scopus 로고
    • Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors
    • Pan X, Lührmann A, Satoh A, Laskowski-Arce MA, Roy CR. 2008. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320:1651-1654. http://dx.doi.org/10.1126/ science.1158160.
    • (2008) Science , vol.320 , pp. 1651-1654
    • Pan, X.1    Lührmann, A.2    Satoh, A.3    Laskowski-Arce, M.A.4    Roy, C.R.5
  • 37
    • 34948874261 scopus 로고    scopus 로고
    • Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
    • Haas AK, Yoshimura S, Stephens DJ, Preisinger C, Fuchs E, Barr FA. 2007. Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells. J. Cell Sci. 120:2997-3010. http://dx.doi.org/10.1242/jcs.014225.
    • (2007) J. Cell Sci. , vol.120 , pp. 2997-3010
    • Haas, A.K.1    Yoshimura, S.2    Stephens, D.J.3    Preisinger, C.4    Fuchs, E.5    Barr, F.A.6
  • 39
    • 32344443060 scopus 로고    scopus 로고
    • Analysis of Rab1 recruitment to vacuoles containing Legionella pneumophila
    • Kagan JC, Murata T, Roy CR. 2005. Analysis of Rab1 recruitment to vacuoles containing Legionella pneumophila. Methods Enzymol. 403: 71-81. http://dx.doi.org/10.1016/S0076-6879(05)03007-7.
    • (2005) Methods Enzymol. , vol.403 , pp. 71-81
    • Kagan, J.C.1    Murata, T.2    Roy, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.