Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization

Biochimica Et Biophysica Acta
Michael Stangl, Dirk Schneider

Abstract

Binding of specific lipids to large, polytopic membrane proteins is well described, and it is clear that such lipids are crucial for protein stability and activity. In contrast, binding of defined lipid species to individual transmembrane helices and regulation of transmembrane helix monomer-oligomer equilibria by binding of distinct lipids is a concept, which has emerged only lately. Lipids bind to single-span membrane proteins, both in the juxta-membrane region as well as in the hydrophobic membrane core. While some interactions counteract transmembrane helix oligomerization, in other cases lipid binding appears to enhance oligomerization. As reversible oligomerization is involved in activation of many membrane proteins, binding of defined lipids to single-span transmembrane proteins might be a mechanism to regulate and/or fine-tune the protein activity. But how could lipid binding trigger the activity of a protein? How can binding of a single lipid molecule to a transmembrane helix affect the structure of a transmembrane helix oligomer, and consequently its signaling state? These questions are discussed in the present article based on recent results obtained with simple, single-span transmembrane proteins. This article is pa...Continue Reading

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Citations

Oct 31, 2015·Journal of the American Chemical Society·Heidi Koldsø, Mark S P Sansom
Aug 6, 2015·Biochemistry·Mark G Teese, Dieter Langosch
Feb 13, 2016·Annual Review of Biomedical Engineering·Hang Yin, Aaron D Flynn
Jun 13, 2019·The Journal of Membrane Biology·Christopher AisenbreyBurkhard Bechinger
Sep 12, 2020·Scientific Reports·Avtar SinghWarren R Zipfel
Aug 23, 2019·Biochimica Et Biophysica Acta. Proteins and Proteomics·Hongxu YangShun Hirota
Oct 20, 2019·Biophysical Journal·Stefanie PannwittDirk Schneider
Jul 17, 2021·Biochimica Et Biophysica Acta. Biomembranes·Jennifer UrbachRuchika Anand

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