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Related Experiment Videos

A nuclear export signal and phosphorylation regulate Dok1 subcellular localization and functions.

Yamei Niu1, François Roy, Frédéric Saltel

  • 1Infections and Cancer Biology Group, International Agency for Research on Cancer, 150 cours Albert-Thomas, 69008 Lyon, France.

Molecular and Cellular Biology
|May 18, 2006
PubMed
Summary

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Dok1 protein shuttles between the nucleus and cytoplasm, regulated by CRM1-dependent nuclear export. External stimuli and phosphorylation control Dok1 localization, impacting its cell signaling functions.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Dok1 is primarily known as a cytoplasmic adaptor protein.
  • Dok1 regulates mitogen-activated protein kinase (MAPK) activation, cell proliferation, transformation, spreading, and migration.

Purpose of the Study:

  • To investigate the subcellular localization of Dok1.
  • To identify mechanisms regulating Dok1 localization.
  • To determine the functional significance of Dok1 nuclear-cytoplasmic shuttling.

Main Methods:

  • Leptomycin B (LMB) treatment to inhibit CRM1-mediated nuclear export.
  • Identification of a functional nuclear export signal (NES) in Dok1.
  • Analysis of Dok1 localization under various cellular conditions (serum starvation/stimulation, cell adhesion, growth factor exposure).

Related Experiment Videos

  • Assessment of Dok1 function in NES-mutant cells.

    • Main Results:

    • Dok1 shuttles between the nucleus and cytoplasm.
    • Leptomycin B treatment causes Dok1 nuclear accumulation, indicating CRM1-dependent nuclear export.
    • A functional NES (348LLKAKLTDPKED359) is identified, crucial for cytoplasmic localization.
    • Src-induced tyrosine phosphorylation and IKKbeta influence Dok1 localization.
    • Cellular conditions like serum starvation/stimulation and adhesion modulate Dok1 localization.
    • Nuclear localization of NES-mutant Dok1 impairs its ability to inhibit proliferation and promote cell spreading/motility.

    Conclusions:

    • Dok1 actively transits through the nucleus and is exported to the cytoplasm via the CRM1 system.
    • External stimuli and phosphorylation-dependent regulation of nuclear export maintain Dok1 in the cytoplasm for signaling.
    • This dynamic localization is critical for Dok1's regulatory functions in cell signaling.