Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains

Yuki Itsuki, Makio Saeki, Hirokazu Nakahara, Hiroshi Egusa, Yasuyuki Irie, Yutaka Terao, Shigetada Kawabata, Hirofumi Yatani, Yoshinori Kamisaki

Research output: Contribution to journalArticle

26 Citations (Scopus)

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: MINT-6551090:Monad (uniprotkb:Q96MX6) physically interacts (MI:0218) with RPAP3 (uniprotkb:Q9H6T3) by anti tag coimmunoprecipitation (MI:0007)MINT-6551101, MINT-6551118:Monad (uniprotkb:Q96MX6) physically interacts (MI:0218) with RPAP3 (uniprotkb:Q9H6T3) by pull down (MI:0096)MINT-6551132:RPAP3 (uniprotkb:Q9H6T3) physically interacts (MI:0218) with Monad (uniprotkb:Q96MX6) by anti bait coimmunoprecipitation (MI:0006).

Original languageEnglish
Pages (from-to)2365-2370
Number of pages6
JournalFEBS Letters
Volume582
Issue number16
DOIs
Publication statusPublished - 2008 Jul 9

Keywords

  • Apoptosis
  • Caspase
  • Cell death
  • TNF-α
  • TPR
  • WD repeat

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Itsuki, Y., Saeki, M., Nakahara, H., Egusa, H., Irie, Y., Terao, Y., Kawabata, S., Yatani, H., & Kamisaki, Y. (2008). Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains. FEBS Letters, 582(16), 2365-2370. https://doi.org/10.1016/j.febslet.2008.05.041