The cyclin-dependent kinase 11p46 isoform interacts with RanBPM

Monika Mikolajczyk, Jiaqi Shi, Richard R. Vaillancourt, Nancy A. Sachs, Mark Nelson

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


We identified Ran-binding protein (RanBPM) as an interacting partner of the caspase-processed C-terminal domain of cyclin-dependent kinase 11 (CDK11p46) by using the yeast two-hybrid system. CDK11 p110 protein kinases are members of the cyclin-dependent kinase superfamily. During staurosporine-, Fas-, and tumor necrosis factor α-induced apoptosis caspase-processed activated CDK11p46 is generated from larger CDK11p110 isoforms. CDK11p46 promotes apoptosis when it is ectopically expressed in human cells. However, the mechanism of signal transduction through CDK11p46 is still unclear. In this study, we demonstrate that CDK11p46 directly interacts with RanBPM in vitro and in human cells. RanBPM contains a conserved SPRY (repeats in splA and Ryr) domain and is localized both in the nucleus and cytoplasm. The SPRY domain of RanBPM is responsible for the association between CDK11p46 and RanBPM. Furthermore, we show that CDK1146 phosphorylates RanBPM.

Original languageEnglish (US)
Pages (from-to)14-18
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Oct 10 2003


  • Apoptosis
  • CDK11
  • Cyclin-dependent kinase 11
  • Phosphorylation
  • RanBPM

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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