Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression.

Liao HJ, Carpenter G
Mol Biol Cell. 2007 18 (3): 1064-72

PMID: 17215517 · PMCID: PMC1805100 · DOI:10.1091/mbc.e06-09-0802

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.

MeSH Terms (18)

Animals Cell Nucleus Cyclin D Cyclins Endoplasmic Reticulum Epidermal Growth Factor ErbB Receptors Gene Expression Gene Expression Regulation HeLa Cells Humans Membrane Proteins Mice Models, Biological Protein Binding Protein Transport RNA, Messenger SEC Translocation Channels

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