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Related Experiment Videos

Specific interaction between 14-3-3 isoforms and the human CDC25B phosphatase.

V Mils1, V Baldin, F Goubin

  • 1LBCMCP - CNRS, Université Paul Sabatier, 118 Route de Narbonne, 31062 Toulouse cedex, France.

Oncogene
|March 14, 2000
PubMed
Summary

CDC25B phosphatases interact with 14-3-3 proteins through a novel mechanism distinct from CDC25C. Post-translational modifications in vivo expose a high-affinity binding site for specific 14-3-3 isoforms, regulating cell cycle progression.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • CDC25 dual-specificity phosphatases (e.g., CDC25A, B, C) are crucial regulators of cyclin-dependent kinases (CDKs) controlling cell cycle progression.
  • CDC25B is implicated in both S phase and G2/M transitions.
  • Interactions between CDC25 phosphatases and 14-3-3 proteins have been observed, with phosphorylation proposed as a key mediator for CDC25C.

Purpose of the Study:

  • To investigate the molecular basis of the interaction between CDC25B phosphatases and 14-3-3 proteins.
  • To determine if phosphorylation regulates CDC25B binding to 14-3-3 proteins.
  • To compare the interaction mechanisms of CDC25B and CDC25C with 14-3-3 proteins.

Main Methods:

  • Yeast two-hybrid assays to assess interactions between CDC25B splice variants and various 14-3-3 isoforms.

Related Experiment Videos

  • In vitro binding assays with phosphorylated and dephosphorylated CDC25B.
  • Analysis of CDC25B mutants, including a deletion in the amino-terminal region, to identify interaction domains and requirements.

    • Main Results:

    • All CDC25B splice variants showed strong interaction with 14-3-3 eta, beta, and zeta in two-hybrid assays, but weak interaction with epsilon and Theta.
    • In vitro, CDC25B exhibited low-level interaction with multiple 14-3-3 isoforms, unaffected by phosphorylation or dephosphorylation.
    • A specific, strong interaction between CDC25B and 14-3-3 zeta and eta was observed upon deletion of 288 N-terminal residues, requiring Ser 323 integrity but independent of phosphorylation.

    Conclusions:

    • CDC25B interaction with 14-3-3 proteins is regulated differently compared to CDC25C.
    • CDC25B possesses a low-affinity binding site for all 14-3-3 isoforms.
    • In vivo post-translational modification of CDC25B likely exposes a high-affinity, specific binding site for 14-3-3 zeta and eta isoforms, impacting cell cycle control.