The Translocon Sec61β Localized in the Inner Nuclear Membrane Transports Membrane-embedded EGF Receptor to the Nucleus

Nucleoplasm Importin Nuclear pore Sec61 Nuclear membrane
DOI: 10.1074/jbc.m110.158659 Publication Date: 2010-10-12T05:25:21Z
ABSTRACT
Accumulating evidence indicates that endocytosis plays an essential role in the nuclear transport of ErbB family members, such as epidermal growth factor receptor (EGFR) and ErbB-2. Nevertheless, how full-length receptors embedded endosomal membrane pass through pore complexes function non-membrane-bound nucleus remains unclear. Here we show upon EGF treatment, biotinylated cell surface EGFR is trafficked to inner (INM) complexes, remaining a membrane-bound environment. We further find importin β regulates INM addition nucleus/nucleoplasm. Unexpectedly, well known endoplasmic reticulum associated translocon Sec61β found reside associate with EGFR. Knocking down expression reduces level nucleoplasm portion accumulates it portion. Thus, unrecognized release membrane-anchored from lipid bilayer nucleus. The newly identified provides alternative pathway for can be utilized by membrane-embedded proteins
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