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MBC in Press, published online ahead of print January 10, 2007
Mol. Biol. Cell 10.1091/mbc.E06-09-0802

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

Role of the Sec61 Translocon in EGF Receptor Trafficking to the Nucleus and Gene Expression

Hong-Jun Liao and Graham Carpenter

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{beta}, a component of the Sec61 translocon, and is retrotranslocated from the ER to the cytoplasm. Abrogation of Sec61{beta} 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.


Address correspondence to: Graham Carpenter (graham.carpenter{at}vanderbilt.edu)




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