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J Biol Chem, Vol. 274, Issue 3, 1753-1758, January 15, 1999
RI with
Detergent-resistant Membranes
From the Department of Chemistry and Chemical Biology, Cornell
University, Ithaca, New York 14853
We recently showed that aggregation of the
high affinity IgE receptor on mast cells, Fc
RI, causes this
immunoreceptor to associate rapidly with specialized regions of the
plasma membrane, where it is phosphorylated by the tyrosine kinase Lyn.
In this study, we further characterize the detergent sensitivity of
this association on rat basophilic leukemia-2H3 mast cells, and we compare the capacity of structural variants of FcRI and other receptors to undergo this association. We show that this interaction is
not mediated by the 
subunit of the receptor or the cytoplasmic tail
of the 
subunit, both of which are involved in signaling. Using
chimeric receptor constructs, we found that the extracellular segment
of the FcRI 
subunit was not sufficient to mediate this association, implicating FcRI and/or transmembrane segments. To determine the specificity of this interaction, we compared the
association of several other receptors. Interleukin-1 type I receptors
on Chinese hamster ovary cells and 4 integrins on rat basophilic leukemia cells showed little or no association with
isolated membrane domains, both before and after aggregation on the
cells. In contrast, interleukin-2 receptor (Tac) on Chinese hamster
ovary cells exhibited aggregation-dependent membrane
domain association similar to FcRI. These results provide insights
into the structural basis and selectivity of lipid-mediated
interactions between certain transmembrane receptors and
detergent-resistant membranes.
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