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Science 13 July 1990:
Vol. 249. no. 4965, pp. 174 - 177
DOI: 10.1126/science.2371564
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Articles

Science, Vol 249, Issue 4965, 174-177
Copyright © 1990 by American Association for the Advancement of Science

articles

Structural mutations of the T cell receptor zeta chain and its role in T cell activation

SJ Frank, BB Niklinska, DG Orloff, M Mercep, JD Ashwell, and RD Klausner

Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.

T cell hybridomas that express zeta zeta, but not zeta eta, dimers in their T cell receptors (TCRs) produce interleukin-2 (IL-2) and undergo an inhibition of spontaneous growth when activated by antigen, antibodies to the receptor, or antibodies to Thy-1. Hybridomas without zeta and eta were reconstituted with mutated zeta chains. Cytoplasmic truncations of up to 40% of the zeta molecule reconstituted normal surface assembly of TCRs, but antigen-induced IL-2 secretion and growth inhibition were lost. In contrast, cross-linking antibodies to the TCR activated these cells. A point mutation conferred the same signaling phenotype as did the truncations and caused defective antigen-induced tyrosine kinase activation. Thus zeta allows the binding of antigen/major histocompatibility complex (MHC) to alpha beta to effect TCR signaling.


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