Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth

Science

Volumn 333, Issue 6039, 2011, Pages 228-233

  Wild, Philipp ^a   Farhan, Hesso ^b   McEwan, David G ^a   Wagner, Sebastian ^c   Rogov, Vladimir V ^d,e   Brady, Nathan R ^f   Richter, Benjamin ^a   Korac, Jelena ^g   Waidmann, Oliver ^a   Choudhary, Chunaram ^c   Dötsch, Volker ^d   Bumann, Dirk ^b   Dikic, Ivan ^a,g  

^a GOETHE UNIVERSITY MEDICAL SCHOOL   (Germany)

^b UNIVERSITY OF BASEL   (Switzerland)

^c University of Copenhagen   (Denmark)

^d GOETHE UNIVERSITY   (Germany)

^e INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^f GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^g UNIVERSITY OF SPLIT   (Croatia)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; OPTINEURIN; PROTEIN KINASE; TANK BINDING KINASE 1; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

BACTERIUM; CHEMICAL BINDING; ENZYME ACTIVITY; EXPERIMENTAL STUDY; GROWTH RATE; MEMBRANE; PROTEIN;

ARTICLE; AUTOPHAGY; BACTERIAL GROWTH; BINDING AFFINITY; CELL PROLIFERATION; CONTROLLED STUDY; CYTOSOL; GROWTH INHIBITION; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SALMONELLA; SALMONELLA ENTERICA; SALMONELLA TYPHIMURIUM;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AUTOPHAGY; CELL LINE, TUMOR; CYTOSOL; HELA CELLS; HUMANS; IMMUNITY, INNATE; MICROTUBULE-ASSOCIATED PROTEINS; MODELS, BIOLOGICAL; NUCLEAR PROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN-SERINE-THREONINE KINASES; RNA INTERFERENCE; SALMONELLA TYPHIMURIUM; TRANSCRIPTION FACTOR TFIIIA; UBIQUITIN;

BACTERIA (MICROORGANISMS); SALMONELLA; SALMONELLA ENTERICA;

EID: 79960804104     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1205405     Document Type: Article

References (27)

1. H. Nakatogawa, K. Suzuki, Y. Kamada, Y. Ohsumi, Nat. Rev. Mol. Cell Biol. 10, 458 (2009).
2. Z. Yang, D. J. Klionsky, Curr. Opin. Cell Biol. 22, 124 (2010).
3. B. Levine, N. Mizushima, H. W. Virgin, Nature 469, 323 (2011).
4. V. Deretic, Curr. Opin. Cell Biol. 22, 252 (2010).
5. V. Kirkin, D. G. McEwan, I. Novak, I. Dikic, Mol. Cell 34, 259 (2009).
6. C. Kraft, M. Peter, K. Hofmann, Nat. Cell Biol. 12, 836 (2010).
7. D. G. McEwan, I. Dikic, Trends Cell Biol. 21, 195 (2011).
8. I. Novak et al., EMBO Rep. 11, 45 (2010).
9. V. Kirkin et al., Mol. Cell 33, 505 (2009).
10. Materials and methods are available as supporting material on Science Online.
11. S. Pankiv et al., J. Biol. Chem. 282, 24131 (2007).
12. C. Behrends, M. E. Sowa, S. P. Gygi, J. W. Harper, Nature 466, 68 (2010).
13. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; D, Asp; E, Glu; F, Phe; G, Gly; I, Ile; and S, Ser.
14. S. Wagner et al., Oncogene 27, 3739 (2008).
15. S. Morton, L. Hesson, M. Peggie, P. Cohen, FEBS Lett. 582, 997 (2008).
16. K. Clark, L. Plater, M. Peggie, P. Cohen, J. Biol. Chem. 284, 14136 (2009).
17. A. L. Radtke, L. M. Delbridge, S. Balachandran, G. N. Barber, M. X. O'Riordan, PLoS Pathog. 3, e29 (2007).
18. T. L. Thurston, G. Ryzhakov, S. Bloor, N. von Muhlinen, F. Randow, Nat. Immunol. 10, 1215 (2009).
19. L. A. Knodler et al., Proc. Natl. Acad. Sci. U.S.A. 107, 17733 (2010).
20. A. J. Perrin, X. Jiang, C. L. Birmingham, N. S. So, J. H. Brumell, Curr. Biol. 14, 806 (2004).
21. C. R. Beuzón et al., EMBO J. 19, 3235 (2000).
22. Y. T. Zheng et al., J. Immunol. 183, 5909 (2009).
23. M. Cemma, P. K. Kim, J. H. Brumell, Autophagy 7, 341 (2011).
24. P. Stehmeier, S. Muller, Mol. Cell 33, 400 (2009).
25. H. Jiang, D. Cheng, W. Liu, J. Peng, J. Feng, Biochem. Biophys. Res. Commun. 395, 471 (2010).
26. S. J. Cherra 3rd et al., J. Cell Biol. 190, 533 (2010).
27. F. Ikeda, N. Crosetto, I. Dikic, Cell 143, 677 (2010).