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Sci. STKE, 16 April 2002
Vol. 2002, Issue 128, p. pe18
[DOI: 10.1126/stke.2002.128.pe18]

PERSPECTIVES

CTLA-4 Negative Signaling via Lipid Rafts: A New Perspective

Christopher E. Rudd1,2*, Margarita Martín4, and Helga Schneider1,3

1Department of Haematology, Faculty of Medicine, Imperial College School of Science, Technology and Medicine, Hammersmith Hospital, Du Cane Road, London W12 ONN, UK.
2Department of Pathology, Faculty of Medicine, Imperial College School of Science, Technology and Medicine, Hammersmith Hospital, Du Cane Road, London W12 ONN, UK.
3Department of Medicine, Harvard Medical School, Boston, MA 02115 USA.
4Unitat d'Immunologia, Department Biologia Cellular i Anatomia Patològica, Facultat de Medicina, Universitat de Barcelona, Barcelona 08036, Spain.

Summary: Proper function of the immune system requires that activation of T cells is precisely regulated. Responses to the T cell receptor are modulated by signals from other receptors. CTLA-4 (cytotoxic T lymphocyte antigen-4, also called CD152), for example, inhibits cytokine production and proliferation of T cells. Activation of T cells is associated with the accumulation of signaling proteins in lipd rafts--microdomains of the plasma membrane enriched in cholesterol and glycosphingolipds. Rudd et al. discuss evidence that CTLA-4 might inhibit cytokine production and T cell proliferation by limiting the assembly of lipid rafts, which are critical to the formation of a functional immunological synapse between antigen-presenting cells and T cells.

*Corresponding author. Department of Haematology, Faculty of Medicine, Imperial College School of Science, Technology and Medicine, Hammersmith Hospital, Du Cane Road, London W12 ONN, UK. Telephone, 020-8383-8421; fax, 020-8383-8434; e-mail: c.rudd{at}ic.ac.uk

Citation: C. E. Rudd, M. Martín, H. Schneider, CTLA-4 Negative Signaling via Lipid Rafts: A New Perspective. Sci. STKE 2002, pe18 (2002).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
CTLA-4 up-regulation of lymphocyte function-associated antigen 1 adhesion and clustering as an alternate basis for coreceptor function.
H. Schneider, E. Valk, S. da Rocha Dias, B. Wei, and C. E. Rudd (2005)
PNAS 102, 12861-12866
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