A systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2

Cellular Signalling

Volumn 26, Issue 6, 2014, Pages 1243-1257

  Nicholson, Judith ^a,b   Scherl, Alex ^c   Way, Luke ^a   Blackburn, Elizabeth A ^a   Walkinshaw, Malcolm D ^a   Ball, Kathryn L ^a   Hupp, Ted R ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

CypB; Interactome; Linear motifs; MDM2; Proteomics

Indexed keywords

CYCLOPHILIN B; NUTLIN 3; PROTEIN MDM2; CYCLOPHILIN; IMIDAZOLE DERIVATIVE; MDM2 PROTEIN, HUMAN; PIPERAZINE DERIVATIVE; PROTEIN BINDING;

ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; IN VIVO STUDY; LIGAND BINDING; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEOMICS; AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; BINDING COMPETITION; CHEMICAL STRUCTURE; CONSENSUS SEQUENCE; MCF 7 CELL LINE; METABOLISM; MOLECULAR GENETICS; PROTEIN DENATURATION; PROTEIN DOMAIN;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING, COMPETITIVE; CONSENSUS SEQUENCE; CYCLOPHILINS; HUMANS; IMIDAZOLES; MCF-7 CELLS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PIPERAZINES; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN INTERACTION MAPPING; PROTEIN INTERACTION MAPS; PROTO-ONCOGENE PROTEINS C-MDM2;

EID: 84895947285     PISSN: 08986568     EISSN: 18733913     Source Type: Journal    
DOI: 10.1016/j.cellsig.2014.02.011     Document Type: Article

References (66)

1. Tate S., Larsen B., Bonner R., Gingras A.C. J. Proteomics. 2013, 81:91-101.
2. Zhang Q.C., Petrey D., Deng L., Qiang L., Shi Y., Thu C.A., Bisikirska B., Lefebvre C., Accili D., Hunter T., Maniatis T., Califano A., Honig B. Nature 2012, 490:556-560.
3. Schlecht U., Miranda M., Suresh S., Davis R.W., St Onge R.P. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:9213-9218.
4. Saha S., Dazard J.E., Xu H., Ewing R.M. J. Proteome Res. 2012, 11:4476-4487.
5. Tompa P. Nat. Chem. Biol. 2012, 8:597-600.
6. Jubb H., Higueruelo A.P., Winter A., Blundell T.L. Trends Pharmacol. Sci. 2012, 33:241-248.
7. Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R., Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 2007, 316:1160-1166.
8. Santamaria A., Wang B., Elowe S., Malik R., Zhang F., Bauer M., Schmidt A., Sillje H.H., Korner R., Nigg E.A. Mol. Cell. Proteomics 2011, 10. (M110 004457).
9. von Kriegsheim A., Baiocchi D., Birtwistle M., Sumpton D., Bienvenut W., Morrice N., Yamada K., Lamond A., Kalna G., Orton R., Gilbert D., Kolch W. Nat. Cell Biol. 2009, 11:1458-1464.
10. Deshaies R.J., Joazeiro C.A. Annu. Rev. Biochem. 2009, 78:399-434.
11. Maslon M.M., Hupp T.R. Trends Cell Biol. 2010, 20:542-555.
12. Chen J., Wu X., Lin J., Levine A.J. Mol. Cell. Biol. 1996, 16:2445-2452.
13. Honda R., Tanaka H., Yasuda H. FEBS Lett. 1997, 420:25-27.
14. Deisenroth C., Zhang Y. Oncogene 2010, 29:4253-4260.
15. Candeias M.M., Malbert-Colas L., Powell D.J., Daskalogianni C., Maslon M.M., Naski N., Bourougaa K., Calvo F., Fahraeus R. Nat. Cell Biol. 2008, 10:1098-1105.
16. Wawrzynow B., Zylicz A., Wallace M., Hupp T., Zylicz M. J. Biol. Chem. 2007, 282:32603-32612.
17. Powers E.T., Morimoto R.I., Dillin A., Kelly J.W., Balch W.E. Annu. Rev. Biochem. 2009, 78:959-991.
18. Nicholson J., Neelagandan K., Huart A.S., Ball K., Molloy M.P., Hupp T. J. Proteome Res. 2012, 11:5464-5478.
19. Burch L., Shimizu H., Smith A., Patterson C., Hupp T.R. J. Mol. Biol. 2004, 337:129-145.
20. Neduva V., Linding R., Su-Angrand I., Stark A., de Masi F., Gibson T.J., Lewis J., Serrano L., Russell R.B. PLoS Biol. 2005, 3:e405.
21. Neduva V., Russell R.B. FEBS Lett. 2005, 579:3342-3345.
22. Shimizu H., Burch L.R., Smith A.J., Dornan D., Wallace M., Ball K.L., Hupp T.R. J. Biol. Chem. 2002, 277:28446-28458.
23. Wallace M., Worrall E., Pettersson S., Hupp T.R., Ball K.L. Mol. Cell 2006, 23:251-263.
24. Hegyi H., Buday L., Tompa P. PLoS Comput. Biol. 2009, 5:e1000552.
25. Bottger A., Bottger V., Sparks A., Liu W.L., Howard S.F., Lane D.P. Curr. Biol. 1997, 7:860-869.
26. Liu W.L., Midgley C., Stephen C., Saville M., Lane D.P. J. Mol. Biol. 2001, 313:711-731.
27. Pazgier M., Liu M., Zou G., Yuan W., Li C., Li J., Monbo J., Zella D., Tarasov S.G., Lu W. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:4665-4670.
28. Phan J., Li Z., Kasprzak A., Li B., Sebti S., Guida W., Schonbrunn E., Chen J. J. Biol. Chem. 2010, 285:2174-2183.
29. Joseph T.L., Madhumalar A., Brown C.J., Lane D.P., Verma C.S. Cell Cycle 2010, 9:1167-1181.
30. Vassilev L.T., Vu B.T., Graves B., Carvajal D., Podlaski F., Filipovic Z., Kong N., Kammlott U., Lukacs C., Klein C., Fotouhi N., Liu E.A. Science 2004, 303:844-848.
31. Ray-Coquard I., Blay J.Y., Italiano A., Le Cesne A., Penel N., Zhi J., Heil F., Rueger R., Graves B., Ding M., Geho D., Middleton S.A., Vassilev L.T., Nichols G.L., Bui B.N. Lancet Oncol. 2012, 13:1133-1140.
32. Kurokawa M., Kim J., Geradts J., Matsuura K., Liu L., Ran X., Xia W., Ribar T.J., Henao R., Dewhirst M.W., Kim W.J., Lucas J.E., Wang S., Spector N.L., Kornbluth S. Sci. Signal. 2013, 6:ra32.
33. Yao X., Freas A., Ramirez J., Demirev P.A., Fenselau C. Anal. Chem. 2001, 73:2836-2842.
34. van Leeuwen I.M., Higgins M., Campbell J., Brown C.J., McCarthy A.R., Pirrie L., Westwood N.J., Lain S. Cell Cycle 2011, 10:1590-1598.
35. Panchaud A., Scherl A., Shaffer S.A., von Haller P.D., Kulasekara H.D., Miller S.I., Goodlett D.R. Anal. Chem. 2009, 81:6481-6488.
36. Worrall E.G., Worrall L., Blackburn E., Walkinshaw M., Hupp T.R. J. Mol. Biol. 2010, 398:414-428.
37. Kitagawa M., Aonuma M., Lee S.H., Fukutake S., McCormick F. Oncogene 2008, 27:5303-5314.
38. Pettersson S., Sczaniecka M., McLaren L., Russell F., Gladstone K., Hupp T., Wallace M. Biochem. J. 2013, 450:523-536.
39. Huart A.S., MacLaine N.J., Narayan V., Hupp T.R. PLoS One 2012, 7:e43391.
40. Pettersson S., Kelleher M., Pion E., Wallace M., Ball K.L. Biochem. J. 2009, 418:575-585.
41. Hernychova L., Man P., Verma C., Nicholson J., Sharma C.A., Ruckova E., Teo J.Y., Ball K., Vojtesek B., Hupp T.R. Proteomics 2013, 13:2512-2525.
42. Poyurovsky M.V., Katz C., Laptenko O., Beckerman R., Lokshin M., Ahn J., Byeon I.-J.L., Gabizon R., Mattia M., Zupnick A., Brown L.M., Friedler A., Prives C. Nat. Struct. Mol. Biol. 2010, 17:982-989.
43. Panchaud A., Jung S., Shaffer S.A., Aitchison J.D., Goodlett D.R. Anal. Chem. 2011, 83:2250-2257.
44. Mayo L.D., Turchi J.J., Berberich S.J. Cancer Res. 1997, 57:5013-5016.
45. Banks D., Wu M., Higa L.A., Gavrilova N., Quan J., Ye T., Kobayashi R., Sun H., Zhang H. Cell Cycle 2006, 5:1719-1729.
46. Dobbs T.A., Tainer J.A., Lees-Miller S.P. DNA Repair 2010, 9:1307-1314.
47. De Castro E., Sigrist C.J.A., Gattiker A., Bulliard V., Langendijk-Genevaux P.S., Gasteiger E., Bairoch A., Hulo N. Nucleic Acids Res. 2006, 34:362-365.
48. Boularan C., Scott M.G., Bourougaa K., Bellal M., Esteve E., Thuret A., Benmerah A., Tramier M., Coppey-Moisan M., Labbe-Jullie C., Fahraeus R., Marullo S. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:18061-18066.
49. Zhu Y., Poyurovsky M.V., Li Y., Biderman L., Stahl J., Jacq X., Prives C. Mol. Cell 2009, 35:316-326.
50. Henikoff S., Henikoff J.G., Alford W.J., Pietrokovski S. Gene 1995, 163:GC17-GC26.
51. Cummings M.D., Farnum M.A., Nelen M.I. J. Biomol. Screen. 2006, 11:854-863.
52. Choi J.W., Schroeder M.A., Sarkaria J.N., Bram R.J. Cancer Res. 2014, 74:484-496.
53. Clausson C.M., Allalou A., Weibrecht I., Mahmoudi S., Farnebo M., Landegren U., Wahlby C., Soderberg O. Nat. Methods 2011, 8:892-893.
54. Worrall E.G., Wawrzynow B., Worrall L., Walkinshaw M., Ball K.L., Hupp T.R. J. Chem. Biol. 2009, 2:113-129.
55. Li C., Pazgier M., Yuan W., Liu M., Wei G., Lu W.Y., Lu W. J. Mol. Biol. 2010, 398:200-213.
56. Uhrinova S., Uhrin D., Powers H., Watt K., Zheleva D., Fischer P., McInnes C., Barlow P.N. J. Mol. Biol. 2005, 350:587-598.
57. McCoy M.A., Gesell J.J., Senior M.M., Wyss D.F. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:1645-1648.
58. Davey N.E., Van Roey K., Weatheritt R.J., Toedt G., Uyar B., Altenberg B., Budd A., Diella F., Dinkel H., Gibson T.J. Mol. Biosyst. 2012, 8:268-281.
59. Leung G.C., Ho C.S., Blasutig I.M., Murphy J.M., Sicheri F. FEBS Lett. 2007, 581:77-83.
60. Chen Y.C., Aguan K., Yang C.W., Wang Y.T., Pal N.R., Chung I.F. PLoS One 2011, 6:e20025.
61. Fuxreiter M., Tompa P., Simon I. Bioinformatics 2007, 23:950-956.
62. Fuxreiter M. Mol. Biosyst. 2012, 8:168-177.
63. Dyson H.J., Wright P.E. Curr. Opin. Struct. Biol. 2002, 12:54-60.
64. ElSawy K.M., Verma C.S., Joseph T.L., Lane D.P., Twarock R., Caves L.S. Cell Cycle 2013, 12:394-404.
65. Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K. J. Biol. Chem. 2010, 285:35551-35557.
66. Lobley A., Swindells M.B., Orengo C.A., Jones D.T. PLoS Comput. Biol. 2007, 3:e162.