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Science 23 April 1993:
Vol. 260. no. 5107, pp. 544 - 546
DOI: 10.1126/science.8475387
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Articles

Science, Vol 260, Issue 5107, 544-546
Copyright © 1993 by American Association for the Advancement of Science

articles

Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45

RR Hovis, JA Donovan, MA Musci, DG Motto, FD Goldman, SE Ross, and GA Koretzky

Department of Internal Medicine, University of Iowa College of Medicine, Iowa City 52242.

Surface expression of the CD45 tyrosine phosphatase is essential for the T cell antigen receptor (TCR) to couple optimally with its second messenger pathways. CD45 may be required to dephosphorylate a TCR-activated protein tyrosine kinase, which then transduces an activation signal from the TCR. A chimeric molecule that contained extracellular and transmembrane sequences from an allele of a major histocompatibility class I molecule and cytoplasmic sequences of CD45 restored TCR signaling in a CD45-deficient mutant T cell line. Thus, expression of the complex extracellular domain of CD45 is not required for the TCR to couple to its signaling machinery.


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Characterization of a CD43/Leukosialin-mediated Pathway for Inducing Apoptosis in Human T-Lymphoblastoid Cells.
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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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