Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry

Science

Volumn 337, Issue 6100, 2012, Pages 1348-1352

  Herzog, Franz ^a   Kahraman, Abdullah ^a   Boehringer, Daniel ^a   Mak, Raymond ^a   Bracher, Andreas ^c   Walzthoeni, Thomas ^a   Leitner, Alexander ^a   Beck, Martin ^b   Hartl, Franz Ulrich ^c   Ban, Nenad ^a   Malmström, Lars ^a   Aebersold, Ruedi ^a  

^a ETH ZURICH   (Switzerland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CHAPERONIN CONTAINING TCP1; PHOSPHOPROTEIN PHOSPHATASE 2A;

AMINO ACID; CELL ORGANELLE; ENZYME ACTIVITY; MASS SPECTROMETRY; PROTEIN; SPATIAL ANALYSIS; TOPOLOGY;

ARTICLE; CELL FUNCTION; CROSS LINKING; HUMAN; MASS SPECTROMETRY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 84866095385     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1221483     Document Type: Article

References (38)

1. F. Alber et al., Nature 450, 695 (2007).
2. P. Aloy, R. B. Russell, Nat. Rev. Mol. Cell Biol. 7, 188 (2006).
3. A. Leitner et al., Mol. Cell. Proteomics 9, 1634 (2010).
4. H. Zhang et al., Mol. Cell. Proteomics 8, 409 (2009).
5. Z. A. Chen et al., EMBO J. 29, 717 (2010).
6. S. Jennebach, F. Herzog, R. Aebersold, P. Cramer, Nucleic Acids Res. 40, 5591 (2012).
7. K. Lasker et al., Proc. Natl. Acad. Sci. U.S.A. 109, 1380 (2012).
8. M. A. Lauber, J. P. Reilly, Anal. Chem. 82, 7736 (2010).
9. V. Janssens, J. Goris, Biochem. J. 353, 417 (2001).
10. G. B. Moorhead, L. Trinkle-Mulcahy, A.Ulke-Lemée, Nat. Rev. Mol. Cell Biol. 8, 234 (2007).
11. Y. Shi, Cell 139, 468 (2009).
12. C. Wurzenberger, D. W. Gerlich, Nat. Rev. Mol. Cell Biol. 12, 469 (2011).
13. D. M. Virshup, S. Shenolikar, Mol. Cell 33, 537 (2009).
14. M. Goudreault et al., Mol. Cell. Proteomics 8, 157 (2009).
15. J. R. Hutchins et al., Science 328, 593 (2010).
16. Materials and methods are available as supplementary materials on Science Online.
17. A. Leitner et al., Mol. Cell. Proteomics 11, M111.014126 (2012).
18. O. Rinner et al., Nat. Methods 5, 315 (2008).
19. A. Wepf, T. Glatter, A. Schmidt, R. Aebersold, M. Gstaiger, Nat. Methods 6, 203 (2009).
20. Y. Xu et al., Cell 127, 1239 (2006).
21. M. Kong, D. Ditsworth, T. Lindsten, C. B. Thompson, Mol. Cell 36, 51 (2009).
22. T. D. Prickett, D. L. Brautigan, J. Biol. Chem. 279, 38912 (2004).
23. M. LeNoue-Newton et al., J. Biol. Chem. 286, 17665 (2011).
24. H. Wang, X. Wang, Y. Jiang, Mol. Biol. Cell 14, 4342 (2003).
25. P. Bradley, D. Baker, Proteins 65, 922 (2006).
26. J. J. Gray et al., J. Mol. Biol. 331, 281 (2003).
27. X. Yan, R. Habedanck, E. A. Nigg, Mol. Biol. Cell 17, 634 (2006).
28. T. S. Kitajima et al., Nature 441, 46 (2006).
29. C. G. Riedel et al., Nature 441, 53 (2006).
30. Z. Xu et al., Mol. Cell 35, 426 (2009).
31. S. Muto et al., Proc. Natl. Acad. Sci. U.S.A. 104, 4285 (2007).
32. Y. Cong et al., EMBO J. 31, 720 (2012).
33. N. Kalisman, C. M. Adams, M. Levitt, Proc. Natl. Acad. Sci. U.S.A. 109, 2884 (2012).
34. A. Leitner et al., Structure 20, 814 (2012).
35. I. G. Muñoz et al., Nat. Struct. Mol. Biol. 18, 14 (2011).
36. L. Chen, P. B. Sigler, Cell 99, 757 (1999).
37. D. K. Clare et al., Cell 149, 113 (2012).
38. F. Alber et al., Nature 450, 683 (2007).