FEBS Letters
Volume 582, Issue 16 , Pages 2365-2370, 9 July 2008

Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains

Edited by Barry Halliwell

  • Yuki Itsuki

      Affiliations

    • Department of Pharmacology, Graduate School of Dentistry, Osaka University, 1-8 Yamadaoka, Suita, Osaka 565-0871, Japan
    • Department of Fixed Prosthodontics, Graduate school of Dentistry, Osaka University, Japan
  • ,
  • Makio Saeki

      Affiliations

    • Department of Pharmacology, Graduate School of Dentistry, Osaka University, 1-8 Yamadaoka, Suita, Osaka 565-0871, Japan
    • Corresponding Author InformationCorresponding author. Fax: +81 6 6879 2914.
  • ,
  • Hirokazu Nakahara

      Affiliations

    • The First Department of Oral and Maxillofacial Surgery, Osaka University, Japan
  • ,
  • Hiroshi Egusa

      Affiliations

    • Department of Fixed Prosthodontics, Graduate school of Dentistry, Osaka University, Japan
  • ,
  • Yasuyuki Irie

      Affiliations

    • Department of Pharmacology, Iwate Medical University, Morioka, Iwate, Japan
  • ,
  • Yutaka Terao

      Affiliations

    • Department of Oral and Molecular Microbiology, Graduate School of Dentistry, Osaka University, Japan
  • ,
  • Shigetada Kawabata

      Affiliations

    • Department of Oral and Molecular Microbiology, Graduate School of Dentistry, Osaka University, Japan
  • ,
  • Hirofumi Yatani

      Affiliations

    • Department of Fixed Prosthodontics, Graduate school of Dentistry, Osaka University, Japan
  • ,
  • Yoshinori Kamisaki

      Affiliations

    • Department of Pharmacology, Graduate School of Dentistry, Osaka University, 1-8 Yamadaoka, Suita, Osaka 565-0871, Japan
    • E-Institute of Shanghai Universities, Division of Nitric Oxide and Inflammatory Medicine, Shanghai, China

Received 2 May 2008; received in revised form 28 May 2008; accepted 28 May 2008. published online 05 June 2008.

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)

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

FEBS Letters
Volume 582, Issue 16 , Pages 2365-2370, 9 July 2008