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Biochem Soc Trans. 2018 Oct 19;46(5):1355-1366. doi: 10.1042/BST20170424. Epub 2018 Sep 6.

Lipids modulate the insertion and folding of the nascent chains of alpha helical membrane proteins.

Author information

1
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
2
Department of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K. paula.booth@kcl.ac.uk.

Abstract

Membrane proteins must be inserted into a membrane and folded into their correct structure to function correctly. This insertion occurs during translation and synthesis by the ribosome for most α-helical membrane proteins. Precisely how this co-translational insertion and folding occurs, and the role played by the surrounding lipids, is still not understood. Most of the work on the influence of the lipid environment on folding and insertion has focussed on denatured, fully translated proteins, and thus does not replicate folding during unidirectional elongation of nascent chains that occurs in the cell. This review aims to highlight recent advances in elucidating lipid composition and bilayer properties optimal for insertion and folding of nascent chains in the membrane and in the assembly of oligomeric proteins.

KEYWORDS:

lipid bilayer; lipid composition; protein folding; transmembrane proteins

PMID:
30190329
DOI:
10.1042/BST20170424
[Indexed for MEDLINE]

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