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Volumn 108, Issue 44, 2011, Pages 17945-17950

Protein LidA from Legionella is a Rab GTPase supereffector

Author keywords

Adenylylation; Legionella containing vacuole; Vesicular trafficking

Indexed keywords

BACTERIAL PROTEIN; PROTEIN LIDA; RAB PROTEIN; UNCLASSIFIED DRUG;

EID: 81055145448     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1113133108     Document Type: Article
Times cited : (63)

References (37)
  • 1
    • 78751705518 scopus 로고    scopus 로고
    • GTPases involved in vesicular trafficking: Structures and mechanisms
    • Itzen A, Goody RS (2011) GTPases involved in vesicular trafficking: Structures and mechanisms. Semin Cell Dev Biol 22:48-56.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 48-56
    • Itzen, A.1    Goody, R.S.2
  • 2
    • 78751656754 scopus 로고    scopus 로고
    • Role of Rab GTPases in membrane traffic and cell physiology
    • Novick PJ, Hutagalung AH (2011) Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev 91:119-149.
    • (2011) Physiol Rev , vol.91 , pp. 119-149
    • Novick, P.J.1    Hutagalung, A.H.2
  • 3
    • 57649149094 scopus 로고    scopus 로고
    • The Legionella pneumophila replication vacuole: Making a cosy niche inside host cells
    • Isberg RR, O'Connor TJ, Heidtman M (2008) The Legionella pneumophila replication vacuole: Making a cosy niche inside host cells. Nat Rev Microbiol 7:13-24.
    • (2008) Nat Rev Microbiol , vol.7 , pp. 13-24
    • Isberg, R.R.1    O'Connor, T.J.2    Heidtman, M.3
  • 6
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion
    • DOI 10.1126/science.289.5478.444
    • Allan BB, Moyer BD, Balch WE (2000) Rab1 recruitment of p115 into a cis-SNARE complex: Programming budding COPII vesicles for fusion. Science 289:444-448. (Pubitemid 30490455)
    • (2000) Science , vol.289 , Issue.5478 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 7
    • 0035024551 scopus 로고    scopus 로고
    • Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering
    • DOI 10.1034/j.1600-0854.2001.1o007.x
    • Moyer BD, Allan BB, Balch WE (2001) Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering. Traffic 2:268-276. (Pubitemid 32487557)
    • (2001) Traffic , vol.2 , Issue.4 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 8
    • 0037455546 scopus 로고    scopus 로고
    • The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation
    • DOI 10.1083/jcb.200207045
    • Diao A, Rahman D, Pappin DJC, Lucocq J, Lowe M (2003) The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J Cell Biol 160:201-212. (Pubitemid 36254954)
    • (2003) Journal of Cell Biology , vol.160 , Issue.2 , pp. 201-212
    • Diao, A.1    Rahman, D.2    Pappin, D.J.C.3    Lucocq, J.4    Lowe, M.5
  • 9
    • 0013086419 scopus 로고    scopus 로고
    • Golgin-84 is a rab1 binding partner involved in Golgi structure
    • Satoh A, Wang Y, Malsam J, Beard MB, Warren G (2003) Golgin-84 is a Rab1 binding partner involved in Golgi structure. Traffic 4:153-161. (Pubitemid 36621708)
    • (2003) Traffic , vol.4 , Issue.3 , pp. 153-161
    • Satoh, A.1    Wang, Y.2    Malsam, J.3    Beard, M.B.4    Warren, G.5
  • 10
    • 79955000748 scopus 로고    scopus 로고
    • A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1
    • Hou XM, et al. (2011) A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1. EMBO J 30:1659-1670.
    • (2011) EMBO J , vol.30 , pp. 1659-1670
    • Hou, X.M.1
  • 11
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • MüllerMP, et al. (2010) The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329:946-949.
    • (2010) Science , vol.329 , pp. 946-949
    • Müller, M.P.1
  • 12
    • 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 GM, Derre I, Vogel JP, Isberg RR (2003) The Legionella pneumophila LidA protein: A translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity. Mol Microbiol 48:305-321. (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
  • 13
    • 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. (2009) 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) J Biol Chem , vol.284 , pp. 4846-4856
    • Brombacher, E.1
  • 14
    • 21544441752 scopus 로고    scopus 로고
    • LidA, a translocated substrate of the Legionella pneumophila type IV secretion system, interferes with the early secretory pathway
    • DOI 10.1128/IAI.73.7.4370-4380.2005
    • Derre I, Isberg RR (2005) LidA, a translocated substrate of the Legionella pneumophila type IV secretion system, interferes with the early secretory pathway. Infect Immun 73:4370-4380. (Pubitemid 40923183)
    • (2005) Infection and Immunity , vol.73 , Issue.7 , pp. 4370-4380
    • Derre, I.1    Isberg, R.R.2
  • 15
    • 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 MP, Isberg RR (2006) Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev Cell 11:47-56. (Pubitemid 43960806)
    • (2006) Developmental Cell , vol.11 , Issue.1 , pp. 47-56
    • Machner, M.P.1    Isberg, R.R.2
  • 16
    • 58149181482 scopus 로고    scopus 로고
    • Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain
    • Recacha R, et al. (2009) Structural basis for recruitment of Rab6-interacting protein 1 to Golgi via a RUN domain. Structure 17:21-30.
    • (2009) Structure , vol.17 , pp. 21-30
    • Recacha, R.1
  • 17
    • 0035980002 scopus 로고    scopus 로고
    • Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal alpha -helix motifs
    • Wang X, Hu B, Zimmermann B, Kilimann MW (2001) Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal alpha -helix motifs. J Biol Chem 276:32480-32488.
    • (2001) J Biol Chem , vol.276 , pp. 32480-32488
    • Wang, X.1    Hu, B.2    Zimmermann, B.3    Kilimann, M.W.4
  • 18
    • 0033581022 scopus 로고    scopus 로고
    • Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3
    • Chung SH, Joberty G, Gelino EA, Macara IG, Holz RW(1999) Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3. J Biol Chem 274:18113-18120.
    • (1999) J Biol Chem , vol.274 , pp. 18113-18120
    • Chung, S.H.1    Joberty, G.2    Gelino, E.A.3    Macara, I.G.4    Holz, R.W.5
  • 19
    • 0029785081 scopus 로고    scopus 로고
    • Role of the Rab3A-binding domain in targeting of rabphilin-3A to vesicle membranes of PC12 cells
    • McKiernan CJ, Stabila PF, Macara IG (1996) Role of the Rab3A-binding domain in targeting of Rabphilin-3A to vesicle membranes of PC12 cells. Mol Cell Biol 16:4985-4995. (Pubitemid 26272153)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.9 , pp. 4985-4995
    • McKiernan, C.J.1    Stabila, P.F.2    Macara, I.G.3
  • 20
    • 33645110959 scopus 로고    scopus 로고
    • Distinct Rab27A binding affinities of Slp2-a and Slac2-a/melanophilin: Hierarchy of Rab27A effectors
    • Fukuda M (2006) Distinct Rab27A binding affinities of Slp2-a and Slac2-a/melanophilin: Hierarchy of Rab27A effectors. Biochem Biophys Res Commun 343:666-674.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 666-674
    • Fukuda, M.1
  • 21
    • 79960699136 scopus 로고    scopus 로고
    • De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
    • Neunuebel MR, et al. (2011) De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila. Science 333:453-456.
    • (2011) Science , vol.333 , pp. 453-456
    • Neunuebel, M.R.1
  • 22
    • 79960929331 scopus 로고    scopus 로고
    • Legionella pneumophila SidD is a deAMPylase that modifies Rab1
    • Tan YH, Luo ZQ (2011) Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 475:506-509.
    • (2011) Nature , vol.475 , pp. 506-509
    • Tan, Y.H.1    Luo, Z.Q.2
  • 23
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • DOI 10.1038/nature06336, PII NATURE06336
    • Ingmundson A, Delprato A, Lambright DG, Roy CR (2007) Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450:365-369. (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
  • 24
    • 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.
    • (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
  • 25
    • 77953809435 scopus 로고    scopus 로고
    • Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes
    • Wu YW, et al. (2010) Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes. Nat Chem Biol 6:534-540.
    • (2010) Nat Chem Biol , vol.6 , pp. 534-540
    • Wu, Y.W.1
  • 26
    • 0034898458 scopus 로고    scopus 로고
    • Organization of the Rab-GDI/CHM superfamily: The functional basis for choroideremia disease
    • DOI 10.1034/j.1600-0854.2001.20803.x
    • Alory C, Balch WE (2001) Organization of the Rab-GDI/CHM superfamily: The functional basis for choroideremia disease. Traffic 2:532-543. (Pubitemid 32725398)
    • (2001) Traffic , vol.2 , Issue.8 , pp. 532-543
    • Alory, C.1    Balch, W.E.2
  • 27
    • 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
    • DOI 10.1242/jcs.014225
    • Haas AK, et al. (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. (Pubitemid 47517083)
    • (2007) Journal of Cell Science , vol.120 , Issue.17 , pp. 2997-3010
    • Haas, A.K.1    Yoshimura, S.-I.2    Stephens, D.J.3    Preisinger, C.4    Fuchs, E.5    Barr, F.A.6
  • 28
    • 33746356908 scopus 로고    scopus 로고
    • TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
    • DOI 10.1038/nature04847, PII NATURE04847
    • Pan X, Eathiraj S, Munson M, Lambright DG (2006) TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature 442:303-306. (Pubitemid 44114905)
    • (2006) Nature , vol.442 , Issue.7100 , pp. 303-306
    • Pan, X.1    Eathiraj, S.2    Munson, M.3    Lambright, D.G.4
  • 29
    • 0033214775 scopus 로고    scopus 로고
    • Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases
    • DOI 10.1093/emboj/18.19.5216
    • Albert S, Will E, Gallwitz D (1999) Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases. EMBO J 18:5216-5225. (Pubitemid 29465572)
    • (1999) EMBO Journal , vol.18 , Issue.19 , pp. 5216-5225
    • Albert, S.1    Will, E.2    Gallwitz, D.3
  • 31
    • 28944445338 scopus 로고    scopus 로고
    • Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 A resolution
    • DOI 10.1016/j.jsb.2005.10.001, PII S104784770500225X
    • Bergbrede T, Pylypenko O, Rak A, Alexandrov K (2005) Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 A resolution. J Struct Biol 152:235-238. (Pubitemid 41785521)
    • (2005) Journal of Structural Biology , vol.152 , Issue.3 , pp. 235-238
    • Bergbrede, T.1    Pylypenko, O.2    Rak, A.3    Alexandrov, K.4
  • 32
    • 34247846396 scopus 로고    scopus 로고
    • A versatile ligation-independent cloning method suitable for high-throughput expression screening applications
    • Berrow NS, et al. (2007) A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Res 35:e45.
    • (2007) Nucleic Acids Res , vol.35
    • Berrow, N.S.1
  • 34
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 35
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66:213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1


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