In or out? | Nature Reviews Molecular Cell Biology

Access through your institution Buy or subscribe Membrane proteins are vitally important to the integrity and functions of a cell, and to successfully integrate into the complex environment

of the membrane, a protein must have a similarly complex structure, the nature of which is compatible with the membrane environment. Most membrane proteins have a bundle of tightly packed

α-helices that span the width of the membrane and that are predominantly hydrophobic in character. To fold successfully inside the cell such membrane proteins must insert into, and fold

within, the endoplasmic reticulum (ER) membrane as they are being translated. This insertion is mediated by the Sec61-translocon protein complex that provides a channel through which the

translating protein is conducted. It can translocate polypeptides into the aqueous environment of the ER lumen or can move them laterally into the lipid environment of the ER membrane. But

what factors determine whether the translocon inserts a polypeptide into the membrane or pushes it out into the lumen? This is a preview of subscription content, access via your institution

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about institutional subscriptions * Read our FAQs * Contact customer support REFERENCES ORIGINAL RESEARCH PAPER * Hessa, T. et al. Recognition of transmembrane helices by the endoplasmic

reticulum translocon. _Nature_ 433, 377–381 (2005) Article  CAS  Google Scholar  FURTHER READING * White, S. H. & Wimley, W. C. Membrane protein folding and stability: physical

principles. _Annu. Rev. Biophys. Biomol. Struct._ 28, 319–381 (1999) Article  CAS  Google Scholar  * Hessa, T., White, S. H. & von Heijne, G. Membrane insertion of a potassium-channel

voltage sensor. _Science_ 27 Jan 2005 (10.1126/science.1109176). Download references Authors * Lesley Cunliffe View author publications You can also search for this author inPubMed Google

Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Cunliffe, L. In or out?. _Nat Rev Mol Cell Biol_ 6, 192 (2005). https://doi.org/10.1038/nrm1605

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