Tetraspanins: Molecular organisers of the leukocyte surface

Trends in Immunology

Volumn 24, Issue 11, 2003, Pages 610-617

  Tarrant, Jacqueline M ^a   Robb, Lorraine ^a   Van Spriel, Annemiek B ^b   Wright, Mark D ^b  

^a WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b AUSTIN RESEARCH INSTITUTE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; TETRASPANIN;

ANTIGEN PRESENTATION; B LYMPHOCYTE; CELL FUNCTION; CELL MEMBRANE; CELL SURFACE; IMMUNE SYSTEM; IMMUNITY; LEUKOCYTE; NONHUMAN; PROTEIN INTERACTION; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION; T LYMPHOCYTE;

EID: 0242302578     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2003.09.011     Document Type: Review

References (73)

1. Wright M.D., Tomlison M.G. The ins and outs of the transmembrane 4 superfamily. Immunol. Today. 15:1994;588-594.
2. Wright M.D., et al. The L6 membrane proteins - a new four-transmembrane superfamily. Protein Sci. 9:2000;1594-1600.
3. Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 114:2001;4143-4151.
4. Stipp C.S., et al. Functional domains in tetraspanin proteins. Trends Biochem. Sci. 28:2003;106-112.
5. Kitadokoro K., et al. CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs. EMBO J. 20:2001;12-18.
6. Seigneuret M., et al. Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 276:2001;40055-40064.
7. Maecker H.T., et al. The tetraspanin superfamily: molecular facilitators. FASEB J. 11:1997;428-442.
8. Hemler M.E. Specific tetraspanin functions. J. Cell Biol. 155:2001;1103-1107.
9. Tai X.G., et al. CD9-mediated costimulation of TCR-triggered naïve T cells leads to activation followed by apoptosis. J. Immunol. 159:1997;3799-3807.
10. Engering A., Pieters J. Association of distinct tetraspanins with MHC class II molecules at different subcellular locations in human immature dendritic cells. Int. Immunol. 13:2001;127-134.
11. Shaw A.R., et al. Ectopic expression of human and feline CD9 in a human B cell line confers β1 integrin-dependent motility on fibronectin and laminin substrates and enhanced tyrosine phosphorylation. J. Biol. Chem. 270:1995;24092-24099.
12. Knobeloch K.P., et al. Targeted inactivation of the tetraspanin CD37 impairs T-cell-dependent B-cell response under suboptimal costimulatory conditions. Mol. Cell. Biol. 20:2000;5363-5369.
13. Olweus J., et al. CD53, a protein with four membrane-spanning domains, mediates signal transduction in human monocytes and B cells. J. Immunol. 151:1993;707-716.
14. Lagaudriere-Gesbert C., et al. Functional analysis of four tetraspans, CD9, CD53, CD81, and CD82, suggests a common role in costimulation, cell adhesion, and migration: only CD9 upregulates HB-EGF activity. Cell. Immunol. 182:1997;105-112.
15. Puls K.L., et al. CD53, a thymocyte selection marker whose induction requires a lower affinity TCR-MHC interaction than CD69, but is up-regulated with slower kinetics. Int. Immunol. 14:2002;249-258.
16. Cao L., et al. Anti-CD53 monoclonal antibody induced LFA-1/ICAM-1- dependent and -independent lymphocyte homotypic cell aggregation. Immunobiology. 197:1997;70-81.
17. Skubitz K.M., et al. CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils. J. Immunol. 157:1996;3617-3626.
18. Levy S., et al. CD81 (TAPA-1): a molecule involved in signal transduction and cell adhesion in the immune system. Annu. Rev. Immunol. 16:1998;89-109.
19. Maecker H.T., Levy S. Normal lymphocyte development but delayed humoral immune response in CD81-null mice. J. Exp. Med. 185:1997;1505-1510.
20. Miyazaki T., et al. Normal development but differentially altered proliferative responses of lymphocytes in mice lacking CD81. EMBO J. 16:1997;4217-4225.
21. Maecker H.T., et al. CD81 on B cells promotes interleukin 4 secretion and antibody production during T helper type 2 immune responses. Proc. Natl. Acad. Sci. U. S. A. 95:1998;2458-2462.
22. Behr S., Schriver F. Engaging CD19 or target of an antiproliferative antibody 1 on human B lymphocytes induces binding of B cells to the inerfollicular stroma of human tonsils via integrin α4/β1 and fibronectin. J. Exp. Med. 182:1995;1191-1199.
23. Todd S.C., et al. CD81 expressed on human thymocytes mediates integrin activation and interleukin 2-dependent proliferation. J. Exp. Med. 184:1996;2055-2060.
24. Shibagaki N., et al. Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation. Eur. J. Immunol. 29:1999;4081-4091.
25. Hammond C., et al. The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules. J. Immunol. 161:1998;3282-3291.
26. Yauch R.L., et al. Highly stoichiometric, stable, and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration. Mol. Biol. Cell. 9:1998;2751-2765.
27. Tarrant J.M., et al. The absence of Tssc6, a member of the tetraspanin superfamily, does not affect lymphoid development but enhances in vitro T-cell proliferative responses. Mol. Cell. Biol. 22:2002;5006-5018.
28. Boucheix C., Rubinstein E. Tetraspanins. Cell. Mol. Life Sci. 58:2001;1189-1205.
29. Yanez-Mo M., et al. Tetraspanins and intercellular interactions. Microcirculation. 8:2001;153-168.
30. Rubinstein E., et al. CD9, CD63, CD81, and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins. Eur. J. Immunol. 26:1996;2657-2665.
31. Claas C., et al. Evaluation of prototype TM4SF protein complexes and their relation to lipid rafts. J. Biol. Chem. 276:2001;7974-7984.
32. Yashiro-Ohtani Y., et al. Non-CD28 costimulatory molecules present in T cell rafts induce T cell costimulation by enhancing the association of TCR with rafts. J. Immunol. 164:2000;1251-1259.
33. Kropshofer H., et al. Tetraspan microdomains distinct from lipid rafts enrich select peptide-MHC class II complexes. Nat. Immunol. 3:2002;61-68.
34. Hakomori Si S.I. Inaugural Article: The glycosynapse. Proc. Natl. Acad. Sci. U. S. A. 99:(225):2002;232.
35. Szollosi J., et al. Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. J. Immunol. 157:1996;2939-2946.
36. Imai T., et al. Molecular analyses of the association of CD4 with two members of the transmembrane 4 superfamily, CD81 and CD82. J. Immunol. 155:1995;1229-1239.
37. Nakamura K., et al. Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diptheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J. Cell Biol. 129:1995;1691-1705.
38. Nichols T.C., et al. γ-glutamyl transpeptidase, an ecto-enzyme regulator of intracellular redox potential, is a component of TM4 signal transduction complexes. Eur. J. Immunol. 28:1998;4123-4129.
39. Berditchevski F., et al. A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. J. Biol. Chem. 272:1997;2595-2598.
40. Yauch R.L., Hemler M.E. Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphoinositide 4-kinase. Biochem. J. 351:2000;629-637.
41. Zhang X.A., et al. Transmembrane-4 superfamily proteins associate with activated protein kinase C (PKC) and link PKC to specific β1 integrins. J. Biol. Chem. 276:2001;25005-25013.
42. Carmo A.M., Wright M.D. Association of the transmembrane 4 superfamily molecule CD53 with a tyrosine phosphatase activity. Eur. J. Immunol. 25:1995;2090-2095.
43. Bell G.M., et al. The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. J. Exp. Med. 175:1992;527-536.
44. Toyo-oka K., et al. Association of a tetraspanin CD9 with CD5 on the T cell surface: role of particular transmembrane domains in the association. Int. Immunol. 11:1999;2043-2052.
45. Imai T., Yoshie I. C33 antigen and M38 antigen recognized by monoclonal antibodies inhibitory to syncitium formation by human T cell leukemia virus type 1 are both members of the transmembrane 4 superfamily and associate with each other and with CD4 or CD8 in T cells. J. Immunol. 151:1993;6470-6481.
46. Bradbury L.E., et al. The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules. J. Immunol. 149:1992;2841-2850.
47. Schick M.R., Levy S. The TAPA-1 molecule is associated on the surface of B cells with HLA-DR molecules. J. Immunol. 151:1993;4090-4097.
48. Angelisova P., et al. Association of four antigens of the tetraspans family (CD37, CD53, TAPA-1, and R2/C33) with MHC class II glycoproteins. Immunogenetics. 39:1994;249-256.
49. Charrin S., et al. EWI-2 is a new component of the tetraspanin web in hepatocytes and lymphoid cells. Biochem. J. 373:2003;409-421.
50. Hemler M.E., et al. Association of TM4SF proteins with integrins: relevance to cancer. Biochim. Biophys. Acta. 1287:1996;67-71.
51. Skubitz K.M., et al. CD63 associates with CD11/CD18 in large detergent-resistant complexes after translocation to the cell surface in human neutrophils. FEBS Lett. 469:2000;52-56.
52. VanCompernolle S.E., et al. Anti-CD81 activates LFA-1 on T cells and promotes T cell-B cell collaboration. Eur. J. Immunol. 31:2001;823-831.
53. Lagaudriere-Gesbert C., et al. The tetraspanin protein CD82 associates with both free HLA class I heavy chain and heterodimeric β2-microglobulin complexes. J. Immunol. 158:1997;2790-2797.
54. Kaji K., et al. Functional association of CD9 with the Fcγ receptors in macrophages. J. Immunol. 166:2001;3256-3265.
55. Anzai N., et al. C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors. Blood. 99:2002;4413-4421.
56. Lebel-Binay S., et al. CD82, member of the tetra-span-transmembrane protein family, is a costimulatory protein for T cell activation. J. Immunol. 155:1995;101-110.
57. Witherden D.A., et al. CD81 and CD28 costimulate T cells through distinct pathways. J. Immunol. 165:2000;1902-1909.
58. Tai X.G., et al. A role for CD9 molecules in T cell activation. J. Exp. Med. 184:1996;753-758.
59. Iwata S., et al. Distinctive signaling pathways through CD82 and β1 integrins in human T cells. Eur. J. Immunol. 32:2002;1328-1337.
60. Tsitsikov E.N., et al. Impaired CD19 expression and signaling, enhanced antibody response to type II T independent antigen and reduction of B-1 cells in CD81-deficient mice. Proc. Natl. Acad. Sci. U. S. A. 94:1997;10844-10849.
61. Le Naour F., et al. Severely reduced female fertility in CD9-deficient mice. Science. 287:2000;319-321.
62. Miyado K., et al. Requirement of CD9 on the egg plasma membrane for fertilization. Science. 287:2000;321-324.
63. Simons K., Toomre D. Lipid rafts and signal transduction. Nat. Rev. Mol. Cell Biol. 1:2000;31-39.
64. Delaguillaumie A., et al. Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes. J. Cell Sci. 115:2002;433-443.
65. Mittelbrunn M., et al. Cutting edge: dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC. J. Immunol. 169:2002;6691-6695.
66. Matsumoto A.K., et al. Functional dissection of the CD21/CD19/TAPA-1/Leu- 13 complex of B lymphocytes. J. Exp. Med. 178:1993;1407-1417.
67. Carter R.H., Fearon D.T. CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes. Science. 256:1992;105-107.
68. Oren R., et al. TAPA-1, the target of an antiproliferative antibody, defines a new family of transmembrane proteins. Mol. Cell. Biol. 10:1990;4007-4015.
69. Dykstra M., et al. Location is everything: lipid rafts and immune cell signaling. Annu. Rev. Immunol. 21:2003;457-481.
70. Maecker H.T., et al. Differential expression of murine CD81 highlighted by new anti-mouse CD81 monoclonal antibodies. Hybridoma. 19:2000;15-22.
71. Peters P.J., et al. Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature. 349:1991;669-676.
72. Thery C., et al. Exosomes: composition, biogenesis and function. Nat. Rev. Immunol. 2:2002;569-579.
73. Simonsen A., et al. The role of phosphoinositides in membrane transport. Curr. Opin. Cell Biol. 13:2001;485-492.