Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit.
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.
Hibbs
M L
ML
Center for Blood Research, Harvard Medical School, Boston, MA 02115.
Xu
H
H
Stacker
S A
SA
Springer
T A
TA
D000595:Amino Acid Sequence; D000818:Animals; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000502:physiology*; D002460:Cell Line; D005434:Flow Cytometry; D018799:Intercellular Adhesion Molecule-1; D016169:Lymphocyte Function-Associated Antigen-1 / Q000235:genetics / Q000502:physiology*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011948:Receptors, Antigen, T-Cell / Q000502:physiology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014162:Transfection
D015815:Cell Adhesion Molecules; D016169:Lymphocyte Function-Associated Antigen-1; D046911:Macromolecular Substances; D011948:Receptors, Antigen, T-Cell; D018799:Intercellular Adhesion Molecule-1; D013755:Tetradecanoylphorbol Acetate