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Originally published as MBC in Press, 10.1091/mbc.E06-09-0802 on January 10, 2007

Vol. 18, Issue 3, 1064-1072, March 2007

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

Hong-Jun Liao, and Graham Carpenter

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146

Submitted September 8, 2006; Revised December 15, 2006; Accepted January 2, 2007
Monitoring Editor: Sandra Schmid

The epidermal growth factor (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, after the addition of EGF, the cell surface EGF receptor is trafficked to the endoplasmic reticulum (ER) where it associates with Sec61beta, a component of the Sec61 translocon, and is retrotranslocated from the ER to the cytoplasm. Abrogation of Sec61beta 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.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-09-0802) on January 10, 2007.

Formula The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org)

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




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