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Localizing the EGF receptor

Nature Cell Biology volume 4, page E22 (2002)Cite this article

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The epidermal growth factor receptor (EGFR) is cotranslationally inserted into the endoplasmic reticulum (ER) membrane as a type I transmembrane protein. This is a highly regulated process involving inherent topogenic and anchoring sequences. Furthermore, the lumenal/extracellular part of the receptor is subsequently glycosylated and folded, and the extracellular domain eventually possesses several stabilising disulphide bonds. The transmembrane part of the receptor is very hydrophobic. In mutants of the insulin receptor, where one or more hydrophobic residues of the transmembrane segment were instead polar, the entire protein was transported into the ER lumen and eventually secreted. An event whereby the full-length EGFR after synthesis and membrane insertion could be translocated out of the membrane, into the cytoplasm and subsequently into the nucleus by way of a nuclear localization sequence, as proposed by Lin et al.1, would involve yet unresolved and exciting mechanisms. But no such mechanism is substantiated, nor suggested, in the paper published in the recent issue of Nature Cell Biology1.

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References

  1. Lin, S.-Y., et al. Nature Cell Biol. 3, 802–808 (2001).

    Article  CAS  Google Scholar 

  2. Pelkmans, L., Kartenbeck, J, & Helenius, A. Nature Cell Biol. 3, 473–483 (2001).

    Article  CAS  Google Scholar 

  3. Reilly, J. F. & Maher, P. A. J. Cell Biol. 152, 1307–1312 (2001).

  4. Peng, H. et al. Mol. Biol. Cell 12, 449–462 (2001).

    Article  CAS  Google Scholar 

  5. Bargmann, C. I., Hung, M. C. & Weinberg, R. A. Cell 45, 649–657 (1986).

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Pathology, University of Oslo, Oslo, 0027, Norway

    M. Oksvold, H. Huitfeldt, E. Stang & I. Madshus

Authors
  1. M. Oksvold
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  2. H. Huitfeldt
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  3. E. Stang
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  4. I. Madshus
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Oksvold, M., Huitfeldt, H., Stang, E. et al. Localizing the EGF receptor. Nat Cell Biol 4, E22 (2002). https://doi.org/10.1038/ncb0202-e22a

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