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A more recent version of this article appeared on March 1, 2007
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Submitted on September 8, 2006
Revised on December 15, 2006
Accepted on January 2, 2007
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146
Monitoring Editor: Sandra Schmid
The EGF-dependent trafficking of the intact EGF receptor to the nucleus and its requirement for growth factor induction of cyclin D and other genes has been reported. Unresolved is the mechanism by which this or other transmembrane proteins are excised from a lipid bilayer before nuclear translocalization. We report that, following the addition of EGF, the cell surface EGF receptor is trafficked to the ER where it associates with Sec61
, a component of the Sec61 translocon, and is retrotranslocated from the ER to the cytoplasm. Abrogation of Sec61 expression prevents EGF-dependent localization of EGF receptors to the nucleus and expression of cyclin D. This indicates that EGF receptors are trafficked from the ER to the nucleus by a novel pathway that involves the Sec61 translocon.
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