Interaction between protein phosphatase 2A and members of the importin β superfamily

Eric J. Lubert, Kevin D. Sarge

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


While performing a yeast two-hybrid library screen to uncover novel PP2A-interacting proteins, we discovered a specific interaction between a member of the importin β/karyopherin β superfamily, importin 9, and the A subunit of PP2A (PR65). This interaction between importin 9 and the A subunit was confirmed by in vitro pulldown, immunoprecipitation, and microcystin-Sepharose chromatography. We also found that another family member, importin β, interacted specifically with the A subunit of PP2A. Finally, we showed that treatment of cells with a concentration of okadaic acid known to inhibit PP2A impeded the nuclear localization of an NLS-containing protein. These results provide evidence that these importins can exist in a native complex with endogenous PP2A and that this serine/threonine phosphatase plays a role in regulating the nuclear import of NLS-containing proteins in vivo.

Original languageEnglish
Pages (from-to)908-913
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Apr 11 2003


  • Heat shock protein 1
  • Importin
  • Nuclear import
  • Nuclear localization signal
  • Phosphatase inhibitor
  • Protein phosphatase 2A
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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