Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A

FEBS Letters

Volumn 581, Issue 1, 2007, Pages 65-70

  Seo, Min Duk ^a   Park, Sung Jean ^a   Kim, Hyun Jung ^a   Lee, Bong Jin ^a  

^a Tumor Microenvironment Global Core Research Center   (South Korea)

Author keywords

BCR signaling; EBV; LMP2A; NMR; PY motif; WW domain

Indexed keywords

ASPARTIC ACID; B LYMPHOCYTE RECEPTOR; GLUTAMINE; GLYCINE; LATENT MEMBRANE PROTEIN 2; LATENT MEMBRANE PROTEIN 2A; TRYPTOPHAN; TYROSINE; UBIQUITIN PROTEIN LIGASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; EPSTEIN BARR VIRUS; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

AMINO ACID MOTIFS; HERPESVIRUS 4, HUMAN; HUMANS; MOLECULAR MIMICRY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ANTIGEN, B-CELL; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP; UBIQUITIN-PROTEIN LIGASES; VIRAL MATRIX PROTEINS; VIRUS LATENCY;

HUMAN HERPESVIRUS 4;

EID: 33845622516     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.11.078     Document Type: Article

References (29)

1. Masucci M.G., and Ernberg I. Epstein-Barr virus: adaptation to a life within the immune system. Trends Microbiol 2 (1994) 125-130
2. Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., and Kieff E. Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases. Immunity 2 (1995) 155-166
3. Miller C.L., Lee J.H., Kieff E., Burkhardt A.L., Bolen J.B., and Longnecker R. Epstein-Barr virus protein LMP2A regulates reactivation from latency by negatively regulating tyrosine kinases involved in sIg-mediated signal transduction. Infect. Agents Dis. 3 (1994) 128-136
4. Miller C.L., Lee J.H., Kieff E., and Longnecker R. An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking. Proc Natl. Acad. Sci. USA 91 (1994) 772-776
5. Miller C.L., Longnecker R., and Kieff E. Epstein-Barr virus latent membrane protein 2A blocks calcium mobilization in B lymphocytes. J. Virol. 67 (1993) 3087-3094
6. Caldwell R.G., Wilson J.B., Anderson S.J., and Longnecker R. Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signals. Immunity 9 (1998) 405-411
7. DeFranco A.L. The complexity of signaling pathways activated by the BCR. Curr. Opin. Immunol. 9 (1997) 296-308
8. Fruehling S., and Longnecker R. The immunoreceptor tyrosine-based activation motif of Epstein-Barr virus LMP2A is essential for blocking BCR-mediated signal transduction. Virology 235 (1997) 241-251
9. Fruehling S., Swart R., Dolwick K.M., Kremmer E., and Longnecker R. Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latency. J. Virol. 72 (1998) 7796-7806
10. Longnecker R., and Kieff E. A second Epstein-Barr virus membrane protein (LMP2) is expressed in latent infection and colocalizes with LMP1. J. Virol. 64 (1990) 2319-2326
11. Longnecker R., Druker B., Roberts T.M., and Kieff E. An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase. J. Virol. 65 (1991) 3681-3692
12. Scholle F., Longnecker R., and Raab-Traub N. Analysis of the phosphorylation status of Epstein-Barr virus LMP2A in epithelial cells. Virology 291 (2001) 208-214
13. Ikeda M., Ikeda A., Longan L.C., and Longnecker R. The Epstein-Barr virus latent membrane protein 2A PY motif recruits WW domain-containing ubiquitin-protein ligases. Virology 268 (2000) 178-191
14. Winberg G., Matskova L., Chen F., Plant P., Rotin D., Gish G., Ingham R., Ernberg I., and Pawson T. Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases. Mol. Cell. Biol. 20 (2000) 8526-8535
15. Ikeda M., Ikeda A., and Longnecker R. PY motifs of Epstein-Barr virus LMP2A regulate protein stability and phosphorylation of LMP2A-associated proteins. J. Virol. 75 (2001) 5711-5718
16. Park S.J., Seo M.D., Lee S.K., Ikeda M., Longnecker R., and Lee B.J. Expression and characterization of N-terminal domain of Epstein-Barr virus latent membrane protein 2A in Escherichia coli. Protein Exp. Purif. 41 (2005) 9-17
17. 15N NMR relaxation. Biochemistry 33 (1994) 5984-6003
18. Jeon Y.H., Yamazaki T., Otomo T., Ishihama A., and Kyogoku Y. Flexible linker in the RNA polymerase α subunit facilitates the independent motion of the C-terminal activator contact domain. J. Mol. Biol. 267 (1997) 953-962
19. Wishart D.S., and Nip A.M. Protein chemical shift analysis: a practical guide. Biochem. Cell. Biol. 76 (1998) 153-163
20. Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
21. Busson P., Edwards R.H., Tursz T., and Raab-Traub N. Sequence polymorphism in the Epstein-Barr virus latent membrane protein (LMP)-2 gene. J. Gen. Virol. 76 (1995) 139-145
22. Franken M., Annis B., Ali A.N., and Wang F. 5′ coding and regulatory region sequence divergence with conserved function of the Epstein-Barr virus LMP2A homolog in herpesvirus papio. J. Virol. 69 (1995) 8011-8019
23. Macias M.J., Hyvonen M., Baraldi E., Schultz J., Sudol M., Saraste M., and Oschkinat H. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382 (1996) 646-649
24. Ranganathan R., Lu K.P., Hunter T., and Noel J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89 (1997) 875-886
25. Sudol M. Structure and function of the WW domain. Prog. Biophys. Mol. Biol. 65 (1996) 113-132
26. Harvey K.F., and Kumar S. Nedd4-like proteins: an emerging family of ubiquitin-protein ligases implicated in diverse cellular functions. Trends Cell Biol. 9 (1999) 166-169
27. Bork P., and Sudol M. The WW domain, A signaling site in dystrophin. Trends Biochem. Sci. 19 (1994) 531-553
28. Kanelis V., Rotin D., and Forman-Kay J.D. Solution structure of a Nedd4 WW domain-ENaC peptide complex. Nat. Struct. Biol. 8 (2001) 407-412
29. Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337 (2004) 635-645