HIPK2 associates with RanBPM

Biochem Biophys Res Commun. 2002 Sep 13;297(1):148-53. doi: 10.1016/s0006-291x(02)02020-x.

Abstract

Using the yeast two-hybrid system, we have identified the Ran-binding protein (RanBPM) as an interaction partner of homeodomain-interacting protein kinase 2 (HIPK2). RanBPM has been described as a centrosomal protein through which Ran regulates the centrosomal function. HIPK2 is mainly a nuclear protein, which among other functions represses transcription mediated by homeodomain containing transcription factors. Here, we show that overexpressed wildtype HIPK2 and a kinase defective mutant of HIPK2 directly interact with RanBPM in the nucleus of mammalian cells. Overexpressed wildtype RanBPM and a kinase defective mutant of HIPK2 co-localise with HIPK2 in defined nuclear structures. A carboxy- and an amino-terminal deletion of HIPK2 do not seem to be able to bind to RanBPM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Cytoskeletal Proteins
  • HeLa Cells
  • Humans
  • Mutation
  • Nuclear Proteins / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Two-Hybrid System Techniques
  • ran GTP-Binding Protein / metabolism*

Substances

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Cytoskeletal Proteins
  • Nuclear Proteins
  • Ran binding protein 9
  • Recombinant Proteins
  • HIPK2 protein, human
  • Protein Serine-Threonine Kinases
  • ran GTP-Binding Protein