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- W2783272316 abstract "3501 Accumulating evidence indicates that endocytosis plays an essential role in the nuclear translocation of the cell surface EGF receptor (EGFR). However, the central issue of the nuclear translocation of cell surface membrane receptors is how the receptors embedded in the endosome membrane pass through the nuclear pore complex. In this report, we propose a novel mechanism by which the membrane bound form of EGFR translocates into the nucleus. Digitonin permeabilization, which selectively release out soluble nuclear transporters in the cytoplasm, has no effects on EGFR nuclear transport, suggesting that the cytoplasmic-nuclear trafficking of EGFR depends on a membrane-bound environment. Confocal microscopy revealed that in response to EGF, a portion of EGFR redistributes to the endoplasmic reticulum (ER), where its NH 2 -terminus resides within the lumen. Furthermore, EGFR forms complex with Sec61-β, which is the component of ER translocon. Knockdown of Sec61-β prevents the EGF-dependent translocation of EGFR from the nuclear envelope to the nucleus. Together, these results suggest that upon EGF treatment, the membrane-bound EGFR translocates to the ER, then move into the nucleus through the interaction with the Sec61 translocon." @default.
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- W2783272316 date "2008-05-01" @default.
- W2783272316 modified "2023-10-14" @default.
- W2783272316 title "Nuclear transport of EGFR is through the integral trafficking from the endoplasmic reticulum to the nuclear envelope" @default.
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