References
- Thompson CB, Allison JP. The emerging role of CTLA-4 as an immune attenuator. Immunity 1997; 7: 445–450.
- Tivol EA, Borriello F, Schweitzer AN, Lynch WP, Bluestone JA, Sharpe AH. Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 1995; 3: 541–547.
- Walunas TL, Lenschow DJ, Bakker CY et al. CTLA-4 can function as a negative regulator of T cell activation. Immunity 1994; 1: 405–413.
- Waterhouse P, Penninger JM, Timms E et al. Lymphoproliferativedisorders with early lethality in mice deficient in Ctla-4. Science 1995; 270: 985–988.
- Lee KM, Chuang E, Griffin M et al. Molecular basis of T cellinactivation by CTLA-4. Science 1998; 282: 2263–2266.
- Marengere LE, Waterhouse P, Duncan GS, Mittrucker HW, Feng GS, Mak TW. Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4. Science 1996; 272: 1170–1173.
- Cinek T, Sadra A, Imboden JB. Cutting edge: tyrosine-indepen-dent transmission of inhibitory signals by CTLA-4. J Immunol 2000; 164: 5–8.
- Nakaseko C, Miyatake S, Iida T et al. Cytotoxic T lymphocyte antigen 4 (CTLA-4) engagement delivers an inhibitory signal through the membrane-proximal region in the absence of the tyrosine motif in the cytoplasmic tail. J Exp Med 1999; 190: 765–774.
- Kitayama H, Sugimoto Y, Matsuzaki T, Ikawa Y, Noda M. A ras-related gene with transformation suppressor activity. Cell 1989; 56: 77–84.
- Boussiotis VA, Freeman GJ, Berezovskaya A, Barber DL, Nadler LM. Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rapl. Science 1997; 278: 124–128.
- Franke B, Akkerman JW, Bos JL. Rapid Ca2±-mediated activa-tion of Rapl in human platelets. EMBO J 1997; 16: 252–259.
- Shiratori T, Miyatake S, Ohno H et al. Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2. Immunity 1997; 6: 583–589.
- Carey KD, Dillon Ti, Schmitt JM et al. CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein Rapl. Mol Cell Biol 2000; 20: 8409–8419.
- Kurachi H, Wada Y, Tsukamoto N et al. Human SPA-1 gene product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rapl and Rap2. Segregate expression profiles from a raplGAP gene product. J Biol Chem 1997; 272: 28081–28088.
- Dustin ML, Chan AC. Signaling takes shape in the immune system. Cell 2000; 103: 283–294.
- Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 1998; 395: 82–86.
- Dillon Ti, Carey KD, Wetzel SA, Parker DC, Stork Pi. Regulation of the small GTPase Rapl and extracellular signal-regulated kinases by the costimulatory molecule CTLA-4. Mol Cell Biol 2005; 25: 4117–4128.
- Asha H, de Ruiter ND, Wang MG, Hariharan IK. The Rapl GTPase functions as a regulator of morphogenesis in vivo. EMBO J 1999; 18: 605–615.
- M'Rabet L, Coffer P, Zwartkruis F et al. Activation of the small GTPase rapl in human neutrophils. Blood 1998; 92: 2133–2140.
- Tsukamoto N, Hattori M, Yang H, Bos JL, Minato N. Rapl GTPase-activating protein SPA-1 negatively regulates cell adhe-sion. J Biol Chem 1999; 274: 18463–18469.
- Sakkab D, Lewitzky M, Posern G et al. Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rapl via the large docking protein Gabl and the adapter protein CRKL. J Biol Chem 2000; 275: 10772–10778.
- Dustin ML, Bromley SK, Kan Z, Peterson DA, Unanue ER. Antigen receptor engagement delivers a stop signal to migrating T lymphocytes. Proc Natl Acad Sci USA 1997; 94: 3909–3913.
- Schneider H, Downey J, Smith A et al. Reversal of the TCR stop signal by CTLA-4. Science 2006; 313: 1972–1975.
- Gotoh T, Hattori S, Nakamura S et al. Identification of Rapl as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G. Mol Cell Biol 1995; 15: 6746–6753.
- Kawasaki H, Springett GM, Toki S et al. A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia. Proc Nail Acad Sci USA 1998; 95: 13278–13283.
- Rubinfeld B, Munemitsu S, Clark R et al. Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rapl. Cell 1991; 65: 1033–1042.