Immune cell signaling: a novel mechanistic model reveals new therapeutic targets

Trends in Pharmacological Sciences

Volumn 27, Issue 10, 2006, Pages 518-524

  Sigalov, Alexander B ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; CELL SURFACE RECEPTOR; FC RECEPTOR; GLYCOPROTEIN GP 41; GLYCOPROTEIN VI; HYBRID PROTEIN; MULTICHAIN IMMUNE RECOGNITION RECEPTOR; NEF PROTEIN; OLIGOMER; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

ANTIGEN RECOGNITION; ARTICLE; DRUG DESIGN; DRUG TARGETING; ENZYME PHOSPHORYLATION; ENZYME SUBUNIT; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IMMUNOCOMPETENT CELL; LIGAND BINDING; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; SIGNAL TRANSDUCTION; VIRUS INFECTION;

ANIMALS; HIV INFECTIONS; HUMANS; LIGANDS; MODELS, IMMUNOLOGICAL; RECEPTORS, IMMUNOLOGIC; SIGNAL TRANSDUCTION;

EID: 33748551761     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2006.08.004     Document Type: Article

References (39)

1. Manolios N., et al. Transmembrane helical interactions and the assembly of the T cell receptor complex. Science 249 (1990) 274-277
2. Call M.E., et al. The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 111 (2002) 967-979
3. Michnoff C.H., et al. Mutations within the NH2-terminal transmembrane domain of membrane immunoglobulin (Ig) M alters Igα and Igβ association and signal transduction. J. Biol. Chem. 269 (1994) 24237-24244
4. Daeron M. Fc receptor biology. Annu. Rev. Immunol. 15 (1997) 203-234
5. Borrego F., et al. Structure and function of major histocompatibility complex (MHC) class I specific receptors expressed on human natural killer (NK) cells. Mol. Immunol. 38 (2002) 637-660
6. Biassoni R., et al. Human natural killer cell activating receptors. Mol. Immunol. 37 (2000) 1015-1024
7. Moroi M., and Jung S.M. Platelet glycoprotein VI: its structure and function. Thromb. Res. 114 (2004) 221-233
8. Sigalov A., et al. Homooligomerization of the cytoplasmic domain of the T cell receptor ζ chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry 43 (2004) 2049-2061
9. Sigalov A.B. Multichain immune recognition receptor signaling: different players, same game?. Trends Immunol. 25 (2004) 583-589
10. Sigalov A. Multi-chain immune recognition receptors: spatial organization and signal transduction. Semin. Immunol. 17 (2005) 51-64
11. Arkin M. Protein-protein interactions and cancer: small molecules going in for the kill. Curr. Opin. Chem. Biol. 9 (2005) 317-324
12. Pecht I., et al. Rotational dynamics of the Fcε receptor on mast cells monitored by specific monoclonal antibodies and IgE. Biochemistry 30 (1991) 3450-3458
13. Rudolph M.G., and Wilson I.A. The specificity of TCR/pMHC interaction. Curr. Opin. Immunol. 14 (2002) 52-65
14. Posner R.G., et al. Interaction of a monoclonal IgE-specific antibody with cell-surface IgE-FcεRI: characterization of equilibrium binding and secretory response. Biochemistry 43 (2004) 11352-11360
15. Patrick S.M., et al. Dependence of T cell activation on area of contact and density of a ligand-coated surface. J. Immunol. Methods 241 (2000) 97-108
16. Pitcher L.A., et al. The CD3 γε/δε signaling module provides normal T cell functions in the absence of the TCR ζ immunoreceptor tyrosine-based activation motifs. Eur. J. Immunol. 35 (2005) 3643-3654
17. Wilson B.S., et al. Distinct functions of the FcεR1 γ and β subunits in the control of FcεR1-mediated tyrosine kinase activation and signaling responses in RBL-2H3 mast cells. J. Biol. Chem. 270 (1995) 4013-4022
18. La Gruta N.L., et al. Architectural changes in the TCR:CD3 complex induced by MHC:peptide ligation. J. Immunol. 172 (2004) 3662-3669
19. Kim J.H., et al. Independent trafficking of Ig-α/Ig-β and μ-heavy chain is facilitated by dissociation of the B cell antigen receptor complex. J. Immunol. 175 (2005) 147-154
20. Asai K., et al. Distinct aggregation of β- and γ-chains of the high-affinity IgE receptor on cross-linking. J. Histochem. Cytochem. 48 (2000) 1705-1716
21. Risueno R.M., et al. Ligand-induced conformational change in the T-cell receptor associated with productive immune synapses. Blood 106 (2005) 601-608
22. Dustin M.L. A dynamic view of the immunological synapse. Semin. Immunol. 17 (2005) 400-410
23. Krummel M.F., et al. Differential clustering of CD4 and CD3ζ during T cell recognition. Science 289 (2000) 1349-1352
24. Quintana F.J., et al. HIV-1 fusion peptide targets the TCR and inhibits antigen-specific T cell activation. J. Clin. Invest. 115 (2005) 2149-2158
25. Wang X.M., et al. T-cell antigen receptor peptides inhibit signal transduction within the membrane bilayer. Clin. Immunol. 105 (2002) 199-207
26. Yamasaki S., et al. Mechanistic basis of pre-T cell receptor-mediated autonomous signaling critical for thymocyte development. Nat. Immunol. 7 (2006) 67-75
27. Draberova L., et al. Signaling assemblies formed in mast cells activated via Fcε receptor I dimers. Eur. J. Immunol. 34 (2004) 2209-2219
28. Loregian A., and Palu G. Disruption of protein-protein interactions: towards new targets for chemotherapy. J. Cell. Physiol. 204 (2005) 750-762
29. Enk A.H., and Knop J. T cell receptor mimic peptides and their potential application in T-cell-mediated disease. Int. Arch. Allergy Immunol. 123 (2000) 275-281
30. Ali M., et al. Hydrophobic transmembrane-peptide lipid conjugations enhance membrane binding and functional activity in T-cells. Bioconjug. Chem. 16 (2005) 1556-1563
31. Amon, M.A. et al. Lipidation and glycosylation of a T cell antigen receptor (TCR) transmembrane hydrophobic peptide dramatically enhances in vitro and in vivo function. Biochim. Biophys. Acta. (in press)
32. Bennasroune A., et al. Transmembrane peptides as inhibitors of ErbB receptor signaling. Mol. Biol. Cell 15 (2004) 3464-3474
33. Siegel R.M., et al. SPOTS: signaling protein oligomeric transduction structures are early mediators of death receptor-induced apoptosis at the plasma membrane. J. Cell Biol. 167 (2004) 735-744
34. + T cell depletion. J. Clin. Immunol. 21 (2001) 218-226
35. Schrager J.A., and Marsh J.W. HIV-1 Nef increases T cell activation in a stimulus-dependent manner. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8167-8172
36. + T lymphocytes by the Nef protein of HIV-1. J. Leukoc. Biol. 79 (2006) 616-627
37. Simmons A., et al. Nef triggers a transcriptional program in T cells imitating single-signal T cell activation and inducing HIV virulence mediators. Immunity 14 (2001) 763-777
38. Swigut T., et al. Cooperative interactions of simian immunodeficiency virus Nef, AP-2, and CD3-ζ mediate the selective induction of T-cell receptor-CD3 endocytosis. J. Virol. 77 (2003) 8116-8126
39. Schamel W.W., et al. Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response. J. Exp. Med. 202 (2005) 493-503