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Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes

Nature volume 450, pages 663–669 (2007)Cite this article

Abstract

A decisive step in the biosynthesis of many proteins is their partial or complete translocation across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. Most of these proteins are translocated through a protein-conducting channel that is formed by a conserved, heterotrimeric membrane-protein complex, the Sec61 or SecY complex. Depending on channel binding partners, polypeptides are moved by different mechanisms: the polypeptide chain is transferred directly into the channel by the translating ribosome, a ratcheting mechanism is used by the endoplasmic reticulum chaperone BiP, and a pushing mechanism is used by the bacterial ATPase SecA. Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules.

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Figure 1: The translocation channel.
Figure 2: Model of co-translational translocation.
Figure 3: Model of post-translational translocation in eukaryotes.
Figure 4
Figure 5: Different stages of translocation.

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Acknowledgements

I thank A. Osborne, Y. Shibata, B. van den Berg and K. Matlack for critical reading of the manuscript, and W. Li and V. Goder for help with the figures.

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  1. Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA, Massachusetts

    Tom A. Rapoport

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Rapoport, T. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450, 663–669 (2007). https://doi.org/10.1038/nature06384

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