First Author | Rodrigues-Lima F | Year | 2001 |
Journal | Biochem Biophys Res Commun | Volume | 285 |
Issue | 5 | Pages | 1274-9 |
PubMed ID | 11478795 | Mgi Jnum | J:72154 |
Mgi Id | MGI:2151894 | Doi | 10.1006/bbrc.2001.5328 |
Citation | Rodrigues-Lima F, et al. (2001) Sequence analysis identifies TTRAP, a protein that associates with CD40 and TNF receptor-associated factors, as a member of a superfamily of divalent cation-dependent phosphodiesterases. Biochem Biophys Res Commun 285(5):1274-9 |
abstractText | CD40 is a member of the tumor necrosis factor (TNF) receptor family. CD40-mediated signal transduction involves the recruitment of several cytoplasmic proteins and induces expression of a large number of genes. TTRAP, a novel protein that interacts with the cytoplasmic domain of CD40 and with TNF-receptor associated factors (TRAFs), has been cloned and shown to inhibit nuclear factor-kappaB activation (NF-kappaB). By using various bioinformatics-based sequence and structure analyses of proteins involved in signaling by the TNF receptor family, we found that TTRAP is a member of a superfamily of Mg(2+)/Mn(2+)-dependent phosphodiesterases. More precisely, our results suggest that TTRAP is related to the human APE1, a Mg(2+)-dependent endonuclease. This potential novel function of TTRAP raises the intriguing possibility for a role of APE1-like DNA-repair endonucleases in TNF receptor family-mediated signaling and functions. Copyright 2001 Academic Press. |