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J Biol Chem, Vol. 273, Issue 34, 21893-21900, August 21, 1998
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From the Departments of Ezrin is a cytoplasmic linker molecule
between plasma membrane components and the actin-containing
cytoskeleton. We studied whether ezrin is associated with intercellular
adhesion molecule (ICAM)-1, -2, and -3. In transfected cells, ICAM-1
and ICAM-2 colocalized with ezrin in microvillar projections, whereas
an ICAM-1 construct attached to cell membrane via a
glycophosphatidylinositol anchor was uniformly distributed on the
cell surface. An interaction of ICAM-2 and ezrin was seen by affinity
precipitation, microtiter binding assay, coimmunoprecipitation, and
surface plasmon resonance methods. The calculated
KD value was 3.3 × 10 Pathology and
Virology,
7
M. Phosphatidylinositol 4,5-bisphosphate
(PtdIns(4,5)P2) induced an interaction of ezrin and ICAM-1
and enhanced the interaction of ezrin and ICAM-2, but ICAM-3 did not
bind ezrin even in the presence of PtdIns(4,5)P2.
PtdIns(4,5)P2 was shown to bind to cytoplasmic tails of
ICAM-1 and ICAM-2, which are the first adhesion proteins demonstrated
to interact with PtdIns(4,5)P2. The results indicate an
interaction of ezrin with ICAM-1 and ICAM-2 and suggest a regulatory
role of phosphoinositide signaling pathways in regulation of ICAM-ezrin
interaction.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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