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Science 23 April 1993:
Vol. 260. no. 5107, pp. 541 - 544
DOI: 10.1126/science.8475386

Articles

Science, Vol 260, Issue 5107, 541-544
Copyright © 1993 by American Association for the Advancement of Science


articles

Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains

S Volarevic, BB Niklinska, CM Burns, CH June, AM Weissman, and JD Ashwell

Laboratory of Immune Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

The CD45 protein is a transmembrane tyrosine phosphatase that is required for normal T cell receptor (TCR)-mediated signaling. A chimeric complementary DNA encoding the intracellular enzymatically active portion of murine CD45 preceded by a short amino-terminal sequence from p60c-src was transfected into CD45- T cells. Expression of this chimeric protein corrected most of the TCR signaling abnormalities observed in the absence of CD45, including TCR-mediated enhancement of tyrosine kinase activity and Ca2+ flux. Thus, the enzymatically active intracellular portion of CD45 is sufficient to allow TCR transmembrane signaling.


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Differential Regulation of Activation-induced Tyrosine Phosphorylation and Recruitment of SLP-76 to Vav by Distinct Isoforms of the CD45 Protein-tyrosine Phosphatase.
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An Activated Epidermal Growth Factor Receptor/Lck Chimera Restores Early T Cell Receptor-mediated Calcium Response in a CD45-deficient T Cell Line.
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CD45 Protein-tyrosine Phosphatase Associates with the WW Domain-containing Protein, CD45AP, through the Transmembrane Region.
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Distinct Isoforms of the CD45 Protein-tyrosine Phosphatase Differentially Regulate Interleukin 2 Secretion and Activation Signal Pathways Involving Vav in T Cells.
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