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Science 29 March 1991:
Vol. 251. no. 5001, pp. 1611 - 1613
DOI: 10.1126/science.1672776
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Articles

Science, Vol 251, Issue 5001, 1611-1613
Copyright © 1991 by American Association for the Advancement of Science

articles

Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit

ML Hibbs, H Xu, SA Stacker, and TA Springer

Center for Blood Research, Harvard Medical School, Boston, MA 02115.

Interactions between cytotoxic lymphocytes and their targets require the T cell antigen receptor (TCR) and the integrin lymphocyte function-associated molecule-1 (LFA-1, CD11a/CD18). LFA-1 is not constitutively avid for its counter-receptors, intercellular adhesion molecules (ICAMs)-1 and -2. Cross-linking of the TCR transiently converts LFA-1 to a high avidity state and thus provides a mechanism for regulating cellular adhesion and de-adhesion in an antigen-specific manner. Truncation of the cytoplasmic domain of the beta, but not the alpha, subunit of LFA-1 eliminated binding to ICAM-1 and sensitivity to phorbol esters. Thus, LFA-1 binding to ICAM-1 was found to be regulated by the cytoplasmic domain of the beta subunit of LFA-1.


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