PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced apoptosis

Biochem Biophys Res Commun. 2010 Dec 17;403(3-4):340-4. doi: 10.1016/j.bbrc.2010.11.031. Epub 2010 Nov 13.

Abstract

We have previously reported that the two components of R2TP complex, RNA polymerase II-associated protein 3 (RPAP3), and Reptin, regulate apoptosis. Here we characterize another component of the complex, PIH1 domain containing protein 1 (PIH1D1). PIH1D1 interacts with both RPAP3 and Monad in HEK293 or U2OS cells. PIH1D1 transcripts were abundant in lung, leukocyte, and placenta. The reduction in endogenous PIH1D1 by siRNA enhanced apoptosis and caspase-3 activation induced by doxorubicin in U2OS cells. These results suggest that PIH1D1 may also function as a novel modulator of apoptosis pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Apoptosis Regulatory Proteins / genetics
  • Apoptosis Regulatory Proteins / metabolism*
  • Apoptosis*
  • Carrier Proteins / metabolism*
  • Cell Line
  • Cell Line, Tumor
  • DNA Helicases / metabolism*
  • Doxorubicin / pharmacology
  • Humans
  • Tissue Distribution

Substances

  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • DNAAF10 protein, human
  • PIH1D1 protein, human
  • RPAP3 protein, human
  • Doxorubicin
  • ATPases Associated with Diverse Cellular Activities
  • DNA Helicases
  • RUVBL2 protein, human