Caspase-3-mediated cleavage of PICOT in apoptosis

Nuri Yun, Chiho Kim, Hyeseon Cha, Woo Jin Park, Hirohiko Shibayama, Il Seon Park, Young J. Oh

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Mammalian protein kinase C-interacting cousin of thioredoxin (PICOT) is a multi-domain mono-thiol glutaredoxin that is involved in several signal transduction pathways and is necessary for cell growth and metastasis. Here, we demonstrate that PICOT is a cleavage substrate of the apoptosis-related protein caspase-3. In vitro cleavage assays indicated that PICOT was specifically cleaved by caspase-3. Similarly, endogenous PICOT was cleaved in cell death responses induced by staurosporine and etoposide. These phenomena were blocked in the presence of a pan-caspase inhibitor. Using site-directed mutagenesis, we identified two putative caspase-3 cleavage sequences in PICOT, DRLD(101)/G and EELD(226)/T. Interestingly, overexpression of either PICOT wild type or the D101A/D226A double point mutant accelerated etoposide-induced activation of caspase-3 whereas siRNA-mediated knockdown of PICOT blocked this phenomenon. Our data raise the possibility that the pro-apoptotic role of PICOT is actively regulated via caspase-3-mediated cleavage.

Original languageEnglish (US)
Pages (from-to)533-538
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Mar 15 2013
Externally publishedYes


  • Apoptosis
  • Caspase-3

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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