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Volumn 475, Issue 7357, 2011, Pages 506-509

Legionella pneumophila SidD is a deAMPylase that modifies Rab1

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RAB PROTEIN;

EID: 79960929331     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10307     Document Type: Article
Times cited : (194)

References (29)
  • 1
    • 59849094765 scopus 로고    scopus 로고
    • Legionella pneumophila Dot/Icm translocated substrates: A sum of parts
    • Ensminger, A. W. & Isberg, R. R. Legionella pneumophila Dot/Icm translocated substrates: a sum of parts. Curr. Opin. Microbiol. 12, 67-73 (2009).
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 67-73
    • Ensminger, A.W.1    Isberg, R.R.2
  • 2
    • 84889234826 scopus 로고    scopus 로고
    • Targeting of Host Rab GTPase Function by the Intravacuolar Pathogen Legionella pneumophila
    • DOI 10.1016/j.devcel.2006.05.013, PII S1534580706002541
    • Machner, M. P. & Isberg, R. R. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev. Cell 11, 47-56 (2006). (Pubitemid 43960806)
    • (2006) Developmental Cell , vol.11 , Issue.1 , pp. 47-56
    • Machner, M.P.1    Isberg, R.R.2
  • 4
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • Muller, M. P. et al. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329, 946-949 (2010).
    • (2010) Science , vol.329 , pp. 946-949
    • Muller, M.P.1
  • 5
    • 57649149094 scopus 로고    scopus 로고
    • The Legionella pneumophila replication vacuole: makingacosynicheinsidehostcells
    • Isberg, R. R., O'Connor, T. J. & Heidtman,M. The Legionella pneumophila replication vacuole:makingacosynicheinsidehostcells.NatureRev. Microbiol.7,13-24(2009).
    • (2009) NatureRev.Microbiol. , vol.7 , pp. 13-24
    • Isberg, R.R.1    O'Connor, T.J.2    Heidtman, M.3
  • 6
    • 78651234971 scopus 로고    scopus 로고
    • Legionella metaeffector exploits host proteasome to temporally regulate cognate effector
    • Kubori, T., Shinzawa, N., Kanuka, H. & Nagai, H. Legionella metaeffector exploits host proteasome to temporally regulate cognate effector. PLoS Pathog. 6, e1001216 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Kubori, T.1    Shinzawa, N.2    Kanuka, H.3    Nagai, H.4
  • 7
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • DOI 10.1038/nature06336, PII NATURE06336
    • Ingmundson, A., Delprato, A., Lambright, D. G. & Roy, C. R. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450, 365-369 (2007). (Pubitemid 350126758)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 365-369
    • Ingmundson, A.1    Delprato, A.2    Lambright, D.G.3    Roy, C.R.4
  • 8
    • 63649139064 scopus 로고    scopus 로고
    • The fic domain: Regulation of cell signaling by adenylylation
    • Worby, C. A. et al. The fic domain: regulation of cell signaling by adenylylation. Mol. Cell 34, 93-103 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 93-103
    • Worby, C.A.1
  • 9
    • 67149136177 scopus 로고    scopus 로고
    • Fido a novel AMPylation domain common to Fic Doc, and AvrB
    • Kinch, L. N., Yarbrough, M. L., Orth, K. & Grishin, N. V. Fido, a novel AMPylation domain common to Fic, Doc, and AvrB. PLoS ONE 4, e5818 (2009).
    • (2009) PLoS ONE , vol.4
    • Kinch, L.N.1    Yarbrough, M.L.2    Orth, K.3    Grishin, N.V.4
  • 10
    • 46249111623 scopus 로고    scopus 로고
    • Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors
    • DOI 10.1126/science.1158160
    • Pan, X., Luhrmann, A., Satoh, A., Laskowski-Arce, M. A. & Roy, C. R. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320, 1651-1654 (2008). (Pubitemid 351931257)
    • (2008) Science , vol.320 , Issue.5883 , pp. 1651-1654
    • Pan, X.1    Luhrmann, A.2    Satoh, A.3    Laskowski-Arce, M.A.4    Roy, C.R.5
  • 11
    • 41949084350 scopus 로고    scopus 로고
    • Lgt: A family of cytotoxic glucosyltransferases produced by Legionella pneumophila
    • DOI 10.1128/JB.01798-07
    • Belyi, Y., Tabakova, I., Stahl, M. & Aktories, K. Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila. J. Bacteriol. 190, 3026-3035 (2008). (Pubitemid 351508203)
    • (2008) Journal of Bacteriology , vol.190 , Issue.8 , pp. 3026-3035
    • Belyi, Y.1    Tabakova, I.2    Stahl, M.3    Aktories, K.4
  • 12
    • 65549084822 scopus 로고    scopus 로고
    • Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response
    • Shen, X. et al. Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response. Cell. Microbiol. 11, 911-926 (2009).
    • (2009) Cell. Microbiol. , vol.11 , pp. 911-926
    • Shen, X.1
  • 15
    • 66149098151 scopus 로고    scopus 로고
    • Bacterial FIC proteins AMP up infection
    • Roy, C. R. & Mukherjee, S. Bacterial FIC proteins AMP up infection. Sci. Signal. 2, pe14 (2009).
    • (2009) Sci. Signal. , vol.2
    • Roy, C.R.1    Mukherjee, S.2
  • 16
    • 64149084796 scopus 로고    scopus 로고
    • Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila
    • Brombacher, E. et al. Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila. J. Biol. Chem. 284, 4846-4856 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 4846-4856
    • Brombacher, E.1
  • 17
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMMcomparison
    • Soding, J. Protein homology detection by HMM-HMMcomparison. Bioinformatics 21, 951-960 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 18
    • 34249827271 scopus 로고    scopus 로고
    • Structure of Streptococcus agalactiae serine/threonine phosphatase: The subdomain conformation is coupled to the binding of a third metal ion
    • DOI 10.1111/j.1742-4658.2007.05845.x
    • Rantanen, M. K., Lehtio, L., Rajagopal, L., Rubens, C. E. & Goldman, A. Structure of Streptococcus agalactiae serine/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion. FEBS J. 274, 3128-3137 (2007). (Pubitemid 46849094)
    • (2007) FEBS Journal , vol.274 , Issue.12 , pp. 3128-3137
    • Rantanen, M.K.1    Lehtio, L.2    Rajagopal, L.3    Rubens, C.E.4    Goldman, A.5
  • 19
    • 38349115371 scopus 로고    scopus 로고
    • Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: A flexible flap subdomain controls access to the catalytic site
    • Schlicker, C. et al. Structural analysis of the PP2C phosphatase tPphA from Thermosynechococcus elongatus: a flexible flap subdomain controls access to the catalytic site. J. Mol. Biol. 376, 570-581 (2008).
    • (2008) J. Mol. Biol. , vol.376 , pp. 570-581
    • Schlicker, C.1
  • 20
    • 3142585284 scopus 로고    scopus 로고
    • Controlling the location and activation of Rab GTPases
    • DOI 10.1016/j.ceb.2004.06.014, PII S0955067404000833
    • Seabra, M. C. & Wasmeier, C. Controlling the location and activation of Rab GTPases. Curr. Opin. Cell Biol. 16, 451-457 (2004). (Pubitemid 38903152)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 451-457
    • Seabra, M.C.1    Wasmeier, C.2
  • 22
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough, M. L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269-272 (2009).
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1
  • 23
    • 79952403625 scopus 로고    scopus 로고
    • Comprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila
    • Zhu, W. et al. Comprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila. PLoS ONE 6, e17638 (2011).
    • (2011) PLoS ONE , vol.6
    • Zhu, W.1
  • 24
    • 0027472133 scopus 로고
    • Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila
    • DOI 10.1111/j.1365-2958.1993.tb01092.x
    • Berger, K. H. & Isberg, R. R. Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila. Mol. Microbiol. 7, 7-19 (1993). (Pubitemid 23011091)
    • (1993) Molecular Microbiology , vol.7 , Issue.1 , pp. 7-19
    • Berger, K.H.1    Isberg, R.R.2
  • 25
    • 0038349211 scopus 로고    scopus 로고
    • The Legionella pneumophila LidA protein: A translocated substrate of the Dot/lcm system associated with maintenance of bacterial integrity
    • DOI 10.1046/j.1365-2958.2003.03400.x
    • Conover, G. M., Derre, I., Vogel, J. P. & Isberg, R. R. The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity. Mol. Microbiol. 48, 305-321 (2003). (Pubitemid 36819070)
    • (2003) Molecular Microbiology , vol.48 , Issue.2 , pp. 305-321
    • Conover, G.M.1    Derre, I.2    Vogel, J.P.3    Isberg, R.R.4
  • 26
    • 48249135525 scopus 로고    scopus 로고
    • Anin vivo gene deletion systemfor determining temporal requirement of bacterial virulence factors
    • Liu, Y., Gao, P.,Banga, S.&Luo, Z. Q.Anin vivo gene deletion systemfor determining temporal requirement of bacterial virulence factors. Proc. Natl Acad. Sci. USA 105, 9385-9390 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9385-9390
    • Liu, Y.1    Gao, P.2    Banga, S.3    Luo, Z.Q.4
  • 27
    • 0029670585 scopus 로고    scopus 로고
    • Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1D of Saccharomyces cerevisiae
    • Fan, H. Y., Cheng, K. K. & Klein, H. L. Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1D of Saccharomyces cerevisiae. Genetics 142, 749-759 (1996).
    • (1996) Genetics , vol.142 , pp. 749-759
    • Fan, H.Y.1    Cheng, K.K.2    Klein, H.L.3
  • 28
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., Schiestl, R. H., Willems, A. R. & Woods, R. A. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 11, 355-360 (1995).
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 29
    • 77950378868 scopus 로고    scopus 로고
    • Inhibition of host vacuolar H1-ATPase activity by a Legionella pneumophila effector
    • Xu, L. et al. Inhibition of host vacuolar H1-ATPase activity by a Legionella pneumophila effector. PLoS Pathog. 6, e1000822 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Xu, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.