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Science 7 August 1992:
Vol. 257. no. 5071, pp. 795 - 797
DOI: 10.1126/science.1323144

Articles

Science, Vol 257, Issue 5071, 795-797
Copyright © 1992 by American Association for the Advancement of Science


articles

Activation-induced ubiquitination of the T cell antigen receptor

C Cenciarelli, D Hou, KC Hsu, BL Rellahan, DL Wiest, HT Smith, VA Fried, and AM Weissman

Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

The zeta subunit of the T cell antigen receptor (TCR) exists primarily as a disulfide-linked homodimer. This receptor subunit is important in TCR-mediated signal transduction and is a substrate for a TCR-activated protein tyrosine kinase. The zeta chain was found to undergo ubiquitination in response to receptor engagement. This posttranslational modification occurred in normal T cells and tumor lines. Both nonphosphorylated and phosphorylated zeta molecules were modified, and at least one other TCR subunit, CD3 delta, was also ubiquitinated after activation of the receptor. These findings suggest an expanded role for ubiquitination in transmembrane receptor function.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)