Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains
Abstract
We have previously reported that Monad, a novel WD40 repeat protein, potentiates apoptosis induced by tumor necrosis factor-α(TNF-α) and cycloheximide (CHX). By affinity purification and mass spectrometry, we identified RNA polymerase II-associated protein 3 (RPAP3) as a binding protein of Monad. Overexpression of RPAP3 in HEK 293 potentiated caspase-3 activation and apoptosis induced by TNF-α and CHX. In addition, knockdown of RPAP3 by RNA interference resulted in a significant reduction of apoptosis induced by TNF-α and CHX in HEK293 and HeLa cells. These results raise the possibility that RPAP3, together with Monad, may function as a novel modulator of apoptosis pathway.
Structured summary
Keywords: Apoptosis, Cell death, Caspase, WD repeat, TPR, TNF-α
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PII: S0014-5793(08)00471-7
doi:10.1016/j.febslet.2008.05.041
© 2008 Federation of European Biochemical Societies
