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Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada
The receptor-like protein tyrosine phosphatase CD45 is essential
for TCR signal transduction. Substrates of CD45 include the protein
tyrosine kinases p56lck and
p59fyn, both of which have been shown to be
enriched in detergent-insoluble microdomains. Here we find that there
is a cholesterol-dependent association between CD45 and the
raft-associated protein linker for activation of T cells, suggesting
that CD45 and linker for activation of T cells may colocalize in lipid
rafts. Consistent with this observation, we find that 
5% of total
CD45 can be detected in Triton X-100-insoluble buoyant fractions of
sucrose gradients, demonstrating that CD45 is not excluded from lipid
rafts. Upon stimulation of T cells with anti-CD3, there is a
reduction in the amount of CD45 found associating with lipid rafts. Our
data suggest that CD45 is present in lipid rafts in T cells before
activation, perhaps to activate raft-associated
p56lck, allowing membrane-proximal signaling
events to proceed. Furthermore, the reduction in CD45 content of lipid
rafts after CD3 stimulation may serve to limit the amounts of activated
p56lck in rafts and thus possibly the duration
of T cell responses.
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