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    Biochem Biophys Res Commun. 2003 Apr 11;303(3):908-13.

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

    Lubert EJ, Sarge KD.

    Department of Molecular and Cellular Biochemistry, University of Kentucky, Chandler Medical Center, 800 Rose Street, Lexington, KY 40536-0298, USA.

    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 beta/karyopherin beta 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 beta, 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.

    PMID: 12670497 [PubMed - indexed for MEDLINE]

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