Teaching Fido New ModiFICation Tricks

1. EngelP, GoepfertA, StangerFV, HarmsA, SchmidtA, et al. (2012) Adenylylation control by intra -⁠ or intermolecular active-site obstruction in Fic proteins. Nature 482 : 107–110.

2. MattooS, DurrantE, ChenMJ, XiaoJ, LazarCS, et al. (2011) Comparative analysis of Histophilus somni immunoglobulin-binding protein A (IbpA) with other fic domain-containing enzymes reveals differences in substrate and nucleotide specificities. J Biol Chem 286 : 32834–32842.

3. KinchLN, YarbroughML, OrthK, GrishinNV (2009) Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS ONE 4: e5818.

4. Garcia-PinoA, ZenkinN, LorisR (2014) The many faces of Fic: structural and functional aspects of Fic enzymes. Trends Biochem Sci 39 : 121–129.

5. YarbroughML, LiY, KinchLN, GrishinNV, BallHL, et al. (2009) AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323 : 269–272.

6. ItzenA, BlankenfeldtW, GoodyRS (2011) Adenylylation: renaissance of a forgotten post-translational modification. Trends Biochem Sci 36 : 221–228.

7. WooleryAR, LuongP, BrobergCA, OrthK (2010) AMPylation: Something Old is New Again. Front Microbiol 1 : 113.

8. StadtmanER (2001) The story of glutamine synthetase regulation. J Biol Chem 276 : 44357–44364.

9. HigaN, TomaC, KoizumiY, NakasoneN, NoharaT, et al. (2013) Vibrio parahaemolyticus effector proteins suppress inflammasome activation by interfering with host autophagy signaling. PLoS Pathog 9: e1003142.

10. XuH, YangJ, GaoW, LiL, LiP, et al. (2014) Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome. Nature E-pub ahead of print. doi:10.1038/nature13449

11. WorbyCA, MattooS, KrugerRP, CorbeilLB, KollerA, et al. (2009) The fic domain: regulation of cell signaling by adenylylation. Mol Cell 34 : 93–103.

12. ZekariasB, MattooS, WorbyC, LehmannJ, RosenbuschRF, et al. (2010) Histophilus somni IbpA DR2/Fic in virulence and immunoprotection at the natural host alveolar epithelial barrier. Infect Immun 78 : 1850–1858.

13. PulliainenAT, DehioC (2009) Bartonella henselae: subversion of vascular endothelial cell functions by translocated bacterial effector proteins. Int J Biochem Cell Biol 41 : 507–510.

14. PalaniveluDV, GoepfertA, MeuryM, GuyeP, DehioC, et al. (2011) Fic domain-catalyzed adenylylation: insight provided by the structural analysis of the type IV secretion system effector BepA. Protein Sci 20 : 492–499.

15. DehioC, SauderU, HiestandR (2004) Isolation of Bartonella schoenbuchensis from Lipoptena cervi, a blood-sucking arthropod causing deer ked dermatitis. J Clin Microbiol 42 : 5320–5323.

16. RahmanM, HamH, LiuX, SugiuraY, OrthK, et al. (2012) Visual neurotransmission in Drosophila requires expression of Fic in glial capitate projections. Nat Neurosci 15 : 871–875.

17. FengF, YangF, RongW, WuX, ZhangJ, et al. (2012) A Xanthomonas uridine 5′-monophosphate transferase inhibits plant immune kinases. Nature 485 : 114–118.

18. Castro-RoaD, Garcia-PinoA, De GieterS, van NulandNA, LorisR, et al. (2013) The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu. Nat Chem Biol 9 : 811–817.

19. CruzJW, RothenbacherFP, MaehigashiT, LaneWS, DunhamCM, et al. (2014) Doc toxin is a kinase that inactivates elongation factor Tu. J Biol Chem 289 : 7788–7798.

20. YamaguchiY, InouyeM (2011) Regulation of growth and death in Escherichia coli by toxin-antitoxin systems. Nat Rev Microbiol 9 : 779–790.

21. MaisonneuveE, GerdesK (2014) Molecular mechanisms underlying bacterial persisters. Cell 157 : 539–548.

22. PandeyDP, GerdesK (2005) Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res 33 : 966–976.

23. FieldsBS, BensonRF, BesserRE (2002) Legionella and Legionnaires' disease: 25 years of investigation. Clin Microbiol Rev 15 : 506–526.

24. NinioS, RoyCR (2007) Effector proteins translocated by Legionella pneumophila: strength in numbers. Trends Microbiol 15 : 372–380.

25. MukherjeeS, LiuX, ArasakiK, McDonoughJ, GalanJE, et al. (2011) Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477 : 103–106.

26. GoodyRS, ItzenA (2013) Modulation of small GTPases by legionella. Curr Top Microbiol Immunol 376 : 117–133.

27. CampanacciV, MukherjeeS, RoyCR, CherfilsJ (2013) Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain. EMBO J 32 : 1469–1477.

28. DesveauxD, SingerAU, WuAJ, McNultyBC, MusselwhiteL, et al. (2007) Type III effector activation via nucleotide binding, phosphorylation, and host target interaction. PLoS Pathog 3: e48.

29. AshfieldT, KeenNT, BuzzellRI, InnesRW (1995) Soybean resistance genes specific for different Pseudomonas syringae avirulence genes are allelic, or closely linked, at the RPG1 locus. Genetics 141 : 1597–1604.

30. CuiH, WangY, XueL, ChuJ, YanC, et al. (2010) Pseudomonas syringae effector protein AvrB perturbs Arabidopsis hormone signaling by activating MAP kinase 4. Cell Host Microbe 7 : 164–175.

31. LiuJ, ElmoreJM, LinZJ, CoakerG (2011) A receptor-like cytoplasmic kinase phosphorylates the host target RIN4, leading to the activation of a plant innate immune receptor. Cell Host Microbe 9 : 137–146.

32. AfzalAJ, KimJH, MackeyD (2013) The role of NOI-domain containing proteins in plant immune signaling. BMC Genomics 14 : 327.