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Calreticulin Is a receptor for nuclear export.

J M Holaska¹, B E Black, D C Love

¹Center for Cell Signaling, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908, USA.

The Journal of Cell Biology

|January 10, 2001

Summary

Calreticulin (CRT) mediates nuclear export distinct from Crm1, regulating glucocorticoid receptor (GR) activity. This discovery reveals a new nuclear export pathway for steroid hormone receptors.

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Area of Science:

Cell Biology
Molecular Biology
Protein Export

Background:

Cytosol contains nuclear export activity distinct from Crm1.
Calreticulin (CRT) was previously localized to the ER lumen.
CRT is implicated in steroid hormone receptor function.

Purpose of the Study:

Purify and characterize the novel nuclear export activity.
Investigate CRT's role in nuclear export of the glucocorticoid receptor (GR).
Define a new nuclear export pathway.

Main Methods:

Permeabilized cell assays
Protein purification and characterization
Microinjection and transfection assays
RanGTP binding assays

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Main Results:

Calreticulin (CRT) purified as the novel export activity.
Cells possess both ER and cytosolic CRT pools.
CRT mediates PKI and GR nuclear export via a RanGTP-dependent complex.
GR export utilizes its DNA-binding domain as an NES, independent of leptomycin B.

Conclusions:

Calreticulin (CRT) mediates a novel nuclear export pathway.
This pathway regulates glucocorticoid receptor (GR) nuclear export.
CRT's function extends beyond the ER, impacting transcriptional regulation.