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Related Experiment Videos

Interaction between Mnk2 and CBC(VHL) ubiquitin ligase E3 complex.

Pingzhang Wang1, Xin Wang, Feng Wang

  • 1Chinese National Human Genome Center, Beijing 100176, China. sicau2000@yahoo.com.cn

Science in China. Series C, Life Sciences
|July 22, 2006
PubMed
Summary

MAP kinase-interacting kinase-2 (Mnk2) interacts with the VHL complex, suggesting it may be a substrate. This interaction also implicates Mnk2 in cell shape modulation via VHL-binding protein 1.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • MAP kinase-interacting kinase-2 (Mnk2) is activated by MAP kinases and phosphorylates eukaryotic initiation factor 4E (eIF4E).
  • The precise roles of eIF4E phosphorylation and Mnk2 in protein translation remain unclear.
  • Physiological substrates of Mnk2 beyond eIF4E are largely unidentified.

Purpose of the Study:

  • To identify novel physiological substrates of Mnk2.
  • To elucidate the broader physiological functions of Mnk2.

Main Methods:

  • Yeast two-hybrid screening using Mnk2 as bait.
  • Co-immunoprecipitation analysis in mammalian cells to validate protein interactions.

Main Results:

Related Experiment Videos

  • Mnk2 was found to interact with von Hippel-Lindau tumor suppressor (VHL), ring-box 1 (Rbx1), and Cullin2 (Cul2) proteins in yeast.
  • The interaction between Mnk2 and VHL was confirmed in mammalian cells.
  • Mnk2 interacts with the VHL-E3 ubiquitin ligase complex (CBC(VHL)) and may be a substrate.
  • Mnk2 interacts with VHL-binding protein 1 (VBP1), suggesting a role in cytoskeleton maturation and morphogenesis.

    • Conclusions:

    • Mnk2 interacts with components of the CBC(VHL) ubiquitin ligase complex.
    • Mnk2 is a potential new substrate of the CBC(VHL) complex.
    • Mnk2's interaction with VBP1 suggests a role in cell shape modulation and morphogenesis.