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The transmembrane phosphatase CD45 regulates both Lck activity and T cell receptor (TCR) signaling. Here we have tested whether the large ectodomain of CD45 has a role in this regulation. A CD45 chimera containing the large ectodomain of CD43 efficiently rescues TCR signaling in CD45-null T cells, whereas CD45 chimeras containing small ectodomains from other phosphatases do not. Both basal Lck activity in unstimulated cells and the TCR-induced increase in tyrosine phosphorylation of the TCR zeta-chain and in Lck activity depend on the expression of CD45 with a large ectodomain. Unlike CD45 chimeras containing small ectodomains, both the CD45 chimera with a large ectodomain and wild-type CD45 itself are partially localized to glycosphingolipid-enriched membranes (GEMs). Taken together, these data show that the large CD45 ectodomain is required for optimal TCR signaling.

Original publication

DOI

10.1038/ni877

Type

Journal article

Journal

Nat Immunol

Publication Date

02/2003

Volume

4

Pages

189 - 197

Keywords

Animals, Antigens, CD, Antigens, CD2, Antigens, CD43, Antigens, CD45, Antigens, Thy-1, Cell Line, Dimerization, Glycosphingolipids, Humans, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Membrane Lipids, Mice, Protein Structure, Tertiary, Rats, Receptors, Antigen, T-Cell, Recombinant Fusion Proteins, Sialoglycoproteins, Signal Transduction, T-Lymphocytes, Transfection