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Updated: Jul 14, 2026

In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
Published on: July 23, 2010
Papillomavirus binding factor (PBF)-mediated inhibition of cell growth is regulated by 14-3-3beta
Nadine Sichtig1, Steffi Silling, Gertrud Steger
1Institute of Virology, University of Cologne, Fürst-Pückler-Strasse 56, 50935 Cologne, Germany.
Abstract:
The cellular factor, papillomavirus (PV)-binding factor (PBF)/Huntington's disease binding protein 2 (HDBP2), was identified by its ability to bind regulatory sequences of certain papillomavirus types as well as the Huntington's disease gene. PBF is thought to be a novel nuclear-shuttling transcription factor with unknown function. To further characterize PBF, we identified 14-3-3beta as an interaction partner. We demonstrated that PBF binds to 14-3-3beta using two motifs. Akt-kinase and an unidentified kinase that are activated by the PI3K-signaling pathway were able to phosphorylate these motifs, allowing PBF to associate with 14-3-3beta. This interaction may contribute to the control of the subcellular localization of PBF, which migrated into the nucleus in the absence of growth factors. Over-expression of PBF resulted in the inhibition of cell growth, which was enhanced using a 14-3-3 binding-deficient PBF mutant. Thus, our experiments characterized PBF as a new cellular factor mediating the effects of PI3K/Akt signaling and 14-3-3 on cell growth.
Insights
Papillomavirus (PV)-binding factor (PBF) interacts with 14-3-3beta, influencing cell growth. This interaction is regulated by PI3K/Akt signaling, revealing PBF
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Papillomavirus (PV)-binding factor (PBF), also known as Huntington's disease binding protein 2 (HDBP2), is a novel nuclear-shuttling transcription factor.
- Its precise function and regulatory mechanisms remain largely uncharacterized.
Purpose of the Study:
- To elucidate the function and regulation of PBF.
- To identify PBF interaction partners and understand their role in cellular processes.
Main Methods:
- Yeast two-hybrid screening to identify PBF interacting proteins.
- Co-immunoprecipitation assays to confirm PBF-14-3-3beta interaction.
- Kinase assays to investigate phosphorylation of PBF motifs.
- Cellular localization studies and cell growth assays.
Main Results:
- Identified 14-3-3beta as a PBF interaction partner, binding through specific motifs.
- Demonstrated that PI3K/Akt signaling pathway kinases phosphorylate these motifs, facilitating PBF-14-3-3beta association.
- Observed that PBF regulates cell growth, with overexpression inhibiting growth, an effect enhanced by a 14-3-3 binding-deficient mutant.
Conclusions:
- Characterized PBF as a novel cellular factor involved in mediating the effects of PI3K/Akt signaling and 14-3-3 proteins on cell growth.
- The PBF-14-3-3beta interaction plays a role in regulating PBF's subcellular localization and cellular function.
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