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Department of Cell Biology and Neuroscience, Rutgers, The State University of New Jersey, Piscataway, NJ 08854
CD154 expression is regulated throughout a time course of
CD3-dependent T cell activation by differential mRNA decay. To
understand the molecular basis of the "stability" phase of this
pathway, experiments were conducted to identify sequences and specific
complexes important in this regulation. Gel retardation assays using
extracts from both Jurkat T cells and CD3-activated CD4+ T
cells revealed a major complex (complex I) that bound a 65-bp highly
CU-rich region of the CD154 3' untranslated region. The specificity of
the CU-rich element for complex-I formation was confirmed by disruption
of this complex by oligo(dCT) competition. Formation of complex I
strongly correlated with CD154 mRNA stability across a time course of T
cell activation. UV cross-linking identified a major
oligo(dCT)-sensitive species at 
90 kDa that showed induced and
increased expression in extracts from 24- and 48-hr
anti-CD3-activated T cells, respectively. This protein was absent
in equivalent extracts from resting or 2-h-activated T cells. Using an
in vitro decay assay, we found that a CD154-specific transcript was
more rapidly degraded in 2-h-activated extract and stabilized in the
24- and 48-h extracts compared to extracts from resting T cells.
Disruption of complex I resulted in the rapid decay of a CD154-specific
transcript demonstrating a functional role for complex I in mRNA
stabilization in vitro. These studies support a model of
posttranscriptional regulation of CD154 expression being controlled in
part by the interaction of a poly(CU)-binding complex with a specific
sequence in the 3' untranslated region.
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