DOI: 10.1146/annurev.biophys.37.032807.125904. How Translocons Select Transmembrane Helices

How Translocons Select Transmembrane Helices

10.1146/annurev.biophys.37.032807.125904

Crossref journal-article

Annual Reviews

Annual Review of Biophysics (22)

Abstract

Like all cellular proteins, membrane proteins are synthesized by ribosomes. But unlike their soluble counterparts, highly hydrophobic membrane proteins require auxiliary machineries to prevent aggregation in aqueous cellular compartments. The principal machine is the translocon, which works in concert with ribosomes to manage the orderly insertion of α-helical membrane proteins directly into the endoplasmic reticulum membrane of eukaryotes or into the plasma membrane of bacteria. In the course of insertion, membrane proteins come into thermodynamic equilibrium with the lipid membrane, where physicochemical interactions determine the final three-dimensional structure. Much progress has been made during the past several years toward understanding the physical chemistry of membrane protein stability, the structure of the translocon machine, and the mechanisms by which the translocon selects and inserts transmembrane helices. We review this progress and consider the connection between the physical principles of membrane protein stability and translocon selection of transmembrane helices.

Bibliography

White, S. H., & von Heijne, G. (2008). How Translocons Select Transmembrane Helices. Annual Review of Biophysics, 37(1), 23â42.

Authors 2

Stephen H. White (first)
Gunnar von Heijne (additional)

References 90 Referenced 175

Dates

Type	When
Created	17 years, 6 months ago (Feb. 7, 2008, 1:12 p.m.)
Deposited	3 years, 10 months ago (Oct. 6, 2021, 3:48 p.m.)
Indexed	1 month, 1 week ago (July 26, 2025, 5:23 a.m.)
Issued	17 years, 3 months ago (June 1, 2008)
Published	17 years, 3 months ago (June 1, 2008)
Published Print	17 years, 3 months ago (June 1, 2008)

Funders 0

None

BibTeX

@article{White_2008, title={How Translocons Select Transmembrane Helices}, volume={37}, ISSN={1936-1238}, url={http://dx.doi.org/10.1146/annurev.biophys.37.032807.125904}, DOI={10.1146/annurev.biophys.37.032807.125904}, number={1}, journal={Annual Review of Biophysics}, publisher={Annual Reviews}, author={White, Stephen H. and von Heijne, Gunnar}, year={2008}, month=jun, pages={23–42} }

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  "abstract": "<jats:p> Like all cellular proteins, membrane proteins are synthesized by ribosomes. But unlike their soluble counterparts, highly hydrophobic membrane proteins require auxiliary machineries to prevent aggregation in aqueous cellular compartments. The principal machine is the translocon, which works in concert with ribosomes to manage the orderly insertion of \u03b1-helical membrane proteins directly into the endoplasmic reticulum membrane of eukaryotes or into the plasma membrane of bacteria. In the course of insertion, membrane proteins come into thermodynamic equilibrium with the lipid membrane, where physicochemical interactions determine the final three-dimensional structure. Much progress has been made during the past several years toward understanding the physical chemistry of membrane protein stability, the structure of the translocon machine, and the mechanisms by which the translocon selects and inserts transmembrane helices. We review this progress and consider the connection between the physical principles of membrane protein stability and translocon selection of transmembrane helices. </jats:p>",
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