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Ca2+-dependent nuclear export mediated by calreticulin.

James M Holaska1, Ben E Black, Fraydoon Rastinejad

  • 1Center for Cell Signaling. Departments of Microbiology. Biochemistry and Molecular Genetics. Pharmacology, University of Virginia, Charlottesville, Virginia 22908, USA.

Molecular and Cellular Biology
|August 9, 2002
PubMed
Summary
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Calcium ions (Ca2+) are crucial for the nuclear export of the glucocorticoid receptor (GR) via calreticulin (CRT). This Ca2+-dependent pathway differs from the Crm1 pathway and may regulate GR function.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The glucocorticoid receptor (GR) regulates gene expression upon binding its ligand.
  • Nuclear export of GR is a key step in regulating its function.
  • Calreticulin (CRT) has been implicated in the nuclear export of GR.

Purpose of the Study:

  • To investigate the role of Ca2+ in CRT-mediated nuclear export of GR.
  • To determine if Ca2+ is required for GR binding to CRT and subsequent nuclear export.
  • To elucidate the distinctness of this pathway from other known nuclear transport mechanisms.

Main Methods:

  • Digitonin-permeabilized mammalian cells were used to study GR export.
  • Intracellular Ca2+ levels were manipulated using chemical treatments.

Related Experiment Videos

  • Binding assays were performed to assess the interaction between CRT and GR's DNA binding domain (DBD).
  • Ran GTPase involvement was examined.

    • Main Results:

    • Ca2+-free CRT failed to bind the GR DNA binding domain (DBD) and inhibit GR nuclear export.
    • Ca2+ addition restored both CRT-DBD binding and GR nuclear export.
    • Depletion of intracellular Ca2+ inhibited GR export in intact cells.
    • Ran GTPase was not required for GR export.
    • The identified pathway is distinct from the Crm1 pathway.

    Conclusions:

    • Ca2+ is essential for calreticulin-dependent nuclear export of the glucocorticoid receptor.
    • This Ca2+-regulated pathway represents a novel mechanism for controlling GR function.
    • Signaling pathways that modulate intracellular Ca2+ may regulate GR activity by controlling its nuclear export.