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5. References
P. S. LinsLey, Distinct roles for CD28 and cytotoxic T lymphocyte-associated molecule 4 receptor during T-cell activation. J. Exp. Med. 182, 289–292 (1995).
C. B. Thompson, Distinct roles for the costimulatory ligands B7-1 and B7-2 in T helper cell differentiation? Cell 81, 979–982 (1995).
J. Bluestone, New perspectives of CD28-B7 mediated T cell costimulation. Immunity 2, 555–559 (1995).
M. F. Bachmann et al., T cell responses are governed by avidity and co-stimulatory thresholds. Eur. J. Immunol. 26, 2017–2022 (1996).
E. A. Tivol et al., Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 3, 541–547 (1995).
P. Waterhouse et al., Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4. Science 270, 985–988 (1995).
C. E. Rudd and H. Schneider, Unifying concepts in CD28, ICOS and CTLA-4 coreceptor signaling. Nat Rev Immunol. 3, 544–556 (2003)
C. E. Rudd, J. M. Trevillyan, J. D. Dasgupta, L. L Wong and S. F. Schlossman, The CD4 receptor is complexed in detergent lysates to a protein tyrosine kinase (pp58) from human T lymphocytes. Proc. Natl. Acad. Sci. USA 85, 5190–5194 (1988).
A. Veillette, M. A. Bookman, E. M. Horak and J. B. Bolen, The CD4 and CD8 T cell surface antigens are associated with the internal tyrosine-protein kinase p56lck. Cell 55, 301–308 (1988).
A. Weiss, and R. D. Littman, Signal transduction by lymphocyte antigen receptors. Cell 76, 263–274 (1994).
E. M. Masteller, E. Chuang, A. C. Mullen, S. L. Reiner and C. B. Thompson, Structural analysis of CTLA-4 function in vivo. J. Immunol. 164, 5319–5327 (2000).
T. Pentcheva-Hoang, J. G. Egen, K. Wojnoonski and J. P. Allison, B7-1 and B7-2 selectively recruit CTLA-4 and CD28 to the immunological synapse. Immunity 21, 401–413 (2004).
E. Chuang et al., Regulation of cytotoxic T lymphocyte-associated molecule-4 by src kinases. J. Immunol. 162, 1270–1277 (1999).
K. M. Lee et al., Molecular basis of T cell inactivation by CTLA-4. Science 282, 2263–2266 (1998).
C. M. Cilio, M. R. Daws, A. Malashicheva, C. L. Sentman and D. Holmberg, Cytotoxic T lymphocyte antigen 4 is induced in the thymus upon in vivo activation and its blockade prevents anti-CD3-mediated depletion of thymocytes. J. Exp. Med. 188, 1239–1246 (1998).
L. E. M. Marengere et al., Regulation of T cell receptor signaling by tyrosine phosphatase Syp association with CTLA-4. Science 272, 1170–1173 (1996).
E. Chuang et al., The CD28 and CTLA-4 receptors associate with the serine/ threonine phosphatase PP2A. Immunity 13, 313–322 (2000).
M. Martin, H. Schneider, A. Azouz and C. E. Rudd, Cytotoxic T lymphocyte antigen 4 potently inhibits cell surface raft expression in its regulation of T cell function. J. Exp. Med. 194, 1675–1681 (2001).
S. Chikuma, J. B. Imboden and J. A. Bluestone, Negative regulation of T cell receptor-lipid raft interaction by cytotoxic T lymphocyte-associated antigen 4. J. Exp. Med. 197, 129–135 (2003).
P. J. Darlington et al., Surface cytotoxic T lymphocyte-associated antigen 4 partitions within lipid rafts and relocates to the immunological synapse under conditions of inhibition of T cell activation. J. Exp. Med. 195, 1337–1347 (2002).
A. Viola, S. Schroeder, Y. Sakakibara and A. Lanzavecchia, T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science 283, 680–682 (1999).
C. E. Rudd, M. Martin and H. Schneider, CTLA-4 negative signaling via lipid rafts: A new perspective. Sci. STKE. 2002(128), PE18 (2002).
F. Fallarino et al., Modulation of tryptophan catabolism by regulatory T cells. Nat. Immunol. 4, 1206–1212 (2003).
A. Boasso, J. P. Herbeuval, A. W. Hardy, C. Winkler and G. M. Shearer, Regulation of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA-synthetase by CTLA-4-Fc in human CD4+ T cells. Blood 105, 1574–1581 (2004).
L. Mellor et al., Cutting Edge: Induced indoleamine 2,3 dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion. J. Immunol. 171, 1652–1655 (2003).
E. K. Griffiths et al., Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap. Science 293, 2260–2263 (2001).
H. Wang et al., ADAP-SLP-76 binding differentially regulates supramolecular activation cluster (SMAC) formation relative to T cell-APC conjugation. J. Exp. Med. 200, 1063–1074 (2004).
H. Wang et al., SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates. Nat. Immunol. 4, 366–374 (2003).
E.-K. Jo, H. Wang and C. E Rudd, An essential role for SKAP-55 in LFA-1 clustering on T cells that cannot be substituted by SKAP-55R. J. Exp. Med. 201, 1733–1739 (2005).
J. L. Bos et al., The role of Rap1 in integrin-mediatedcell adhesion. Biochem. Soc. Trans. 31, 83–86 (2003).
K. Katagiri, M. Hattori, N. Minato and T. Kinashi, Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses. Mol. Cell. Biol. 22, 1001–1015 (2002).
K. Katagiri, A. Maeda, M. Shimonaka and T. Kinashi, RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nat. Immunol. 4, 741–748 (2003).
M. L. Dustin, P. M. Allen and A. S. Shaw, Environmental control of immunological synapse formation and duration. Trends Immunol. 22, 192–194 (2001).
A. Kupfer and H. Kupfer, Imaging immune cell interactions and functions: SMACs and the immunological synapse. Semin. Immunol. 15, 295–300 (2003).
E. Caron, Cellular functions of the Rap1 GTP-binding protein: a pattern emerges. J Cell Sci. 116, 435–440 (2003).
E. Sebzda, M. Bracke, T. Tugal, N. Hogg and D. A. Cantrell, Rap1A positively regulates T cells via integrin activation rather than inhibiting lymphocyte signaling. Nat. Immunol. 3, 251–258 (2002).
K. M. de Bruyn, S. Rangarajan, K. A. Reedquist, C. G. Figdoe and J. L. Bos, The small GTPase Rap1 is required for Mn (2+)-and antibody-induced LFA-1 and VLA-4-mediated cell adhesion. J. Biol. Chem. 277, 29468–29476 (2002).
K. Kinbara, L. E. Goldfinger, M. Hansen, F.-L. Chou and M. H. Ginsberg, RASGTPases: integrins’ friends or foes. Nat. Rev. Mol. Cell Biol. 4, 767–776 (2003).
L. S. Price and J. L. Bos, RAPL: taking the Rap in immunity. Nat. Immunol. 5, 1007–1008 (2004).
B. Franke, J. W. N. Akkerman and J. L. Bos, Rapid Ca2+-mediated activation of Rap1 in human platelets. EMBO J. 16, 252–259 (1997).
K. A. Reedquist and J. L. Bos, Costimulation through CD28 suppresses T cell receptor-dependent activation of the ras-like small GTPase Rap1 in human T lymphocytes. J. Biol. Chem. 273, 4944–4949 (1998).
T. Dillon, K. D. Carey, S. A. Wetzel, D. C. Parker and P. J. S. Stork, Regulation of the small GTPase Rap1 and extracellular signal-regulated kinases by the costimulatory molecule CTLA-4. Mol. Cell Biol. 25, 4117–4128 (2005).
J. Takagi and T. A. Springer, Integrin activation and structural rearrangement. Immunol. Rev. 186, 141–163 (2002).
N. Hogg et al., Mechanisms contributing to the activity of integrins on leukocytes. Immunol. Rev. 186, 164–171 (2002).
H. Schneider, K. V. S. Prasad, S. E. Shoelson and C. E. Rudd, CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells. J. Exp. Med. 181, 351–355 (1995).
H. Schneider et al., Cutting Edge: CTLA-4 (CD152) differentially regulates mitogen-activated protein kinases (extracellular signal-regulated kinase and c-Jun Nterminal kinase) in CD4+ T cells from receptor/ligand-deficient mice. J. Immunol. 169, 3475–3479 (2002).
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Schneider, H., Valk, E., Dias, S.d.R., Wei, B., Rudd, C.E. (2006). CTLA-4 Regulation of T Cell Function via RAP-1-Mediated Adhesion. In: Tsoukas, C. (eds) Lymphocyte Signal Transduction. Advances in Experimental Medicine and Biology, vol 584. Springer, Boston, MA. https://doi.org/10.1007/0-387-34132-3_9
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