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

Margaret L. Hibbs, Hong Xu, Steven A. Stacker, Timothy A. Springer

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38 Citations (Scopus)


Interactions between cytotoxic lymphocytes and their targets require the T cell antigen receptor (TCR) and the integrin lymphocyte function-associated molecule-1 (LFA-1, CDL1a/CD18). LFA-1 is not constitutively avid for its counterreceptors, 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 β, but not the α, 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 13 subunit of LFA-1.

Original languageEnglish
Pages (from-to)1611-1613
Number of pages3
Issue number5001
Publication statusPublished - 1 Jan 1991

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