Structural Basis for the Interaction between Focal Adhesion Kinase and CD4

Journal of Molecular Biology

Volumn 375, Issue 5, 2008, Pages 1320-1328

  Garron, Marie Line ^a,b   Arthos, James ^c   Guichou, Jean François ^a,b   McNally, Jonathan ^c   Cicala, Claudia ^c   Arold, Stefan T ^a,b  

^a INSERM   (France)

^b CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^c NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

CD4; focal adhesion kinase; gp120; HIV; Nef

Indexed keywords

CD4 ANTIGEN; FOCAL ADHESION KINASE; NEF PROTEIN; PROTEIN KINASE LCK;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTALLOGRAPHY; ENDOCYTOSIS; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; T LYMPHOCYTE;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 37549055113     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.040     Document Type: Article

References (40)

1. Mitra S.K., and Schlaepfer D.D. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18 (2006) 516-523
2. Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., and Arold S.T. Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain. Structure 11 (2003) 1207-1217
3. Brown M.C., Perrotta J.A., and Turner C.E. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell Biol. 135 (1996) 1109-1123
4. Gao G., Prutzman K.C., King M.L., Scheswohl D.M., DeRose E.F., London R.E., et al. NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model. J. Biol. Chem. 279 (2004) 8441-8451
5. Hagel M., George E.L., Kim A., Tamimi R., Opitz S.L., Turner C.E., et al. The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 22 (2002) 901-915
6. Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D., and Guan J.L. Interaction of focal adhesion kinase with cytoskeletal protein talin. J. Biol. Chem. 270 (1995) 16995-16999
7. Cicala C., Arthos J., Ruiz M., Vaccarezza M., Rubbert A., Riva A., et al. Induction of phosphorylation and intracellular association of CC chemokine receptor 5 and focal adhesion kinase in primary human CD4+ T cells by macrophage-tropic HIV envelope. J. Immunol. 163 (1999) 420-426
8. Cicala C., Arthos J., Rubbert A., Selig S., Wildt K., Cohen O.J., and Fauci A.S. HIV-1 envelope induces activation of caspase-3 and cleavage of focal adhesion kinase in primary human CD4(+) T cells. Proc. Natl Acad. Sci. USA 97 (2000) 1178-1183
9. Berg N.N., and Ostergaard H.L. T cell receptor engagement induces tyrosine phosphorylation of FAK and Pyk2 and their association with Lck. J. Immunol. 159 (1997) 1753-1757
10. Ostergaard H.L., Lou O., Arendt C.W., and Berg N.N. Paxillin phosphorylation and association with Lck and Pyk2 in anti-CD3- or anti-CD45-stimulated T cells. J. Biol. Chem. 273 (1998) 5692-5696
11. Kim P.W., Sun Z.Y., Blacklow S.C., Wagner G., and Eck M.J. A zinc clasp structure tethers Lck to T cell coreceptors CD4 and CD8. Science 301 (2003) 1725-1728
12. Craig H.M., Pandori M.W., and Guatelli J.C. Interaction of HIV-1 Nef with the cellular dileucine-based sorting pathway is required for CD4 down-regulation and optimal viral infectivity. Proc. Natl Acad. Sci. USA 95 (1998) 11229-11234
13. Izard T., and Vonrhein C. Structural basis for amplifying vinculin activation by talin. J. Biol. Chem. 279 (2004) 27667-27678
14. Stove V., Van de Walle I., Naessens E., Coene E., Stove C., Plum J., and Verhasselt B. Human immunodeficiency virus Nef induces rapid internalization of the T-cell coreceptor CD8alphabeta. J. Virol. 79 (2005) 11422-11433
15. Swigut T., Shohdy N., and Skowronski J. Mechanism for down-regulation of CD28 by Nef. EMBO J. 20 (2001) 1593-1604
16. Schmalzigaug R., Garron M.L., Roseman J.T., Xing Y., Davidson C.E., Arold S.T., and Premont R.T. GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillin. Cell. Signalling 19 (2007) 1733-1744
17. Feng S., Chen J.K., Yu H., Simon J.A., and Schreiber S.L. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266 (1994) 1241-1247
18. Grzesiek S., Stahl S.J., Wingfield P.T., and Bax A. The CD4 determinant for downregulation by HIV-1 Nef directly binds to Nef. Mapping of the Nef binding surface by NMR. Biochemistry 35 (1996) 10256-10261
19. Sleckman B.P., Shin J., Igras V.E., Collins T.L., Strominger J.L., and Burakoff S.J. Disruption of the CD4-p56lck complex is required for rapid internalization of CD4. Proc. Natl Acad. Sci. USA 89 (1992) 7566-7570
20. Shin J., Doyle C., Yang Z., Kappes D., and Strominger J.L. Structural features of the cytoplasmic region of CD4 required for internalization. EMBO J. 9 (1990) 425-434
21. Juszczak R.J., Turchin H., Truneh A., Culp J., and Kassis S. Effect of human immunodeficiency virus gp120 glycoprotein on the association of the protein tyrosine kinase p56lck with CD4 in human T lymphocytes. J. Biol. Chem. 266 (1991) 11176-11183
22. Cooley M.A., Broome J.M., Ohngemach C., Romer L.H., and Schaller M.D. Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase. Mol. Biol. Cell 11 (2000) 3247-3263
23. Arold S.T., Ulmer T.S., Mulhern T.D., Werner J.M., Ladbury J.E., Campbell I.D., and Noble M.E. The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases. J. Biol. Chem. 276 (2001) 17199-17205
24. Rapoport I., Chen Y.C., Cupers P., Shoelson S.E., and Kirchhausen T. Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17 (1998) 2148-2155
25. Arold S.T., Hoellerer M.K., and Noble M.E. The structural basis of localization and signaling by the focal adhesion targeting domain. Structure 10 (2002) 319-327
26. Arthos J., Rubbert A., Rabin R.L., Cicala C., Machado E., Wildt K., et al. CCR5 signal transduction in macrophages by human immunodeficiency virus and simian immunodeficiency virus envelopes. J. Virol. 74 (2000) 6418-6424
27. Cicala C., Arthos J., Selig S.M., Dennis Jr. G., Hosack D.A., Van Ryk D., et al. HIV envelope induces a cascade of cell signals in non-proliferating target cells that favor virus replication. Proc. Natl Acad. Sci. USA 99 (2002) 9380-9385
28. Cicala C., Arthos J., Censoplano N., Cruz C., Chung E., Martinelli E., et al. HIV-1 gp120 induces NFAT nuclear translocation in resting CD4+ T-cells. Virology 345 (2006) 105-114
29. Weissman D., Rabin R.L., Arthos J., Rubbert A., Dybul M., Swofford R., et al. Macrophage-tropic HIV and SIV envelope proteins induce a signal through the CCR5 chemokine receptor. Nature 389 (1997) 981-985
30. Preusser A., Briese L., and Willbold D. Presence of a helix in human CD4 cytoplasmic domain promotes binding to HIV-1 Nef protein. Biochem. Biophys. Res. Commun. 292 (2002) 734-740
31. Dutartre H., Harris M., Olive D., and Collette Y. The human immunodeficiency virus type 1 Nef protein binds the Src-related tyrosine kinase Lck SH2 domain through a novel phosphotyrosine independent mechanism. Virology 247 (1998) 200-211
32. Trible R.P., Emert-Sedlak L., and Smithgall T.E. HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction. J. Biol. Chem. 281 (2006) 27029-27038
33. Lusso P. HIV and the chemokine system: 10 years later. EMBO J. 25 (2006) 447-456
34. Wildum S., Schindler M., Munch J., and Kirchhoff F. Contribution of Vpu, Env, and Nef to CD4 down-modulation and resistance of human immunodeficiency virus type 1-infected T cells to superinfection. J. Virol. 80 (2006) 8047-8059
35. CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
36. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D: Biol. Crystallogr. 54 (1998) 905-921
37. Lamzin V.S., and Wilson K.S. Automated refinement of protein models. Acta Crystallogr., Sect. D: Biol. Crystallogr. 49 (1993) 129-147
38. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60 (2004) 2126-2132
39. Doria-Rose N.A., Learn G.H., Rodrigo A.G., Nickle D.C., Li F., Mahalanabis M., et al. Human immunodeficiency virus type 1 subtype B ancestral envelope protein is functional and elicits neutralizing antibodies in rabbits similar to those elicited by a circulating subtype B envelope. J. Virol. 79 (2005) 11214-11224
40. Arthos J., Deen K.C., Chaikin M.A., Fornwald J.A., Sathe G., Sattentau Q.J., et al. Identification of the residues in human CD4 critical for the binding of HIV. Cell 57 (1989) 469-481