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Department of Cell Biology and Neuroscience, Rutgers, State University of New Jersey, Piscataway, NJ 08854
CD40 ligand (CD154) expression has been shown to be regulated, in
part, at the posttranscriptional level by a pathway of "regulated
instability" of mRNA decay throughout a time course of T cell
activation. This pathway is modulated at late times of
activation by the binding of a stability complex (termed complex I)
to a CU-rich region in the 3' untranslated region of the CD154
message. We have undertaken experiments to extend these findings and to
analyze the cis-acting elements and
trans-acting factors involved in this regulation. We
have previously shown that the minimal binding sequence for complex I
is a 63 nt CU-rich motif. However, our current study shows that when
this site was deleted additional complex binding was observed upstream
and downstream of the minimal binding region. Only after deletion of an
extended region (termed 
1515) was complex binding completely
abolished. Analysis of complex binding using competition experiments
revealed that the three adjacent regions bound related but not
identical complexes. However, all three sites appeared to have a 55-kDa
protein as the RNA-binding protein. Deletion of the 1515 region
resulted in reduced transcript stability as measured by both in vitro
and in vivo decay assays. Finally, using Abs against known RNA-binding
proteins, we identified the polypyrimidine tract-binding protein (or
heterogeneous nuclear ribonucleoprotein I) as a candidate
RNA-binding component of complex I.
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