The electrical interplay between proteins and lipids in membranes
- PMID: 25817548
- DOI: 10.1016/j.bbamem.2015.03.017
The electrical interplay between proteins and lipids in membranes
Abstract
All molecular interactions that are relevant to cellular and molecular structures are electrical in nature but manifest in a rich variety of forms that each has its own range and influences on the net effect of how molecular species interact. This article outlines how electrical interactions between the protein and lipid membrane components underlie many of the activities of membrane function. Particular emphasis is placed on spatially localised behaviour in membranes involving modulation of protein activity and microdomain structure. The interactions between membrane lipids and membrane proteins together with their role within cell biology represent an enormous body of work. Broad conclusions are not easy given the complexities of the various systems and even consensus with model membrane systems containing two or three lipid types is difficult. By defining two types of broad lipid-protein interaction, respectively Type I as specific and Type II as more non-specific and focussing on the electrical interactions mostly in the extra-membrane regions it is possible to assemble broad rules or a consensus of the dominant features of the interplay between these two fundamentally important classes of membrane component. This article is part of a special issue entitled: Lipid-protein interactions.
Keywords: DLVO theory; Membrane dipole potential; Membrane electrostatic surface potential; Membrane functional imaging; Membrane microdomain; Potential of mean force.
Copyright © 2015 Elsevier B.V. All rights reserved.
Similar articles
-
Model membrane platforms to study protein-membrane interactions.Mol Membr Biol. 2012 Aug;29(5):144-54. doi: 10.3109/09687688.2012.700490. Epub 2012 Jul 26. Mol Membr Biol. 2012. PMID: 22831167 Review.
-
Structural insights into functional lipid-protein interactions in secondary transporters.Biochim Biophys Acta. 2015 Mar;1850(3):476-87. doi: 10.1016/j.bbagen.2014.05.010. Epub 2014 May 20. Biochim Biophys Acta. 2015. PMID: 24859688 Review.
-
Thermosensing via transmembrane protein-lipid interactions.Biochim Biophys Acta. 2015 Sep;1848(9):1757-64. doi: 10.1016/j.bbamem.2015.04.005. Epub 2015 Apr 20. Biochim Biophys Acta. 2015. PMID: 25906947 Review.
-
Domain formation in the plasma membrane: roles of nonequilibrium lipid transport and membrane proteins.Phys Rev Lett. 2008 May 2;100(17):178102. doi: 10.1103/PhysRevLett.100.178102. Epub 2008 Apr 28. Phys Rev Lett. 2008. PMID: 18518341
-
Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization.Biochim Biophys Acta. 2015 Sep;1848(9):1886-96. doi: 10.1016/j.bbamem.2015.03.011. Epub 2015 Mar 16. Biochim Biophys Acta. 2015. PMID: 25791349 Review.
Cited by
-
Differential Membrane Lipid Profiles and Vibrational Spectra of Three Edaphic Algae and One Cyanobacterium.Int J Mol Sci. 2021 Oct 19;22(20):11277. doi: 10.3390/ijms222011277. Int J Mol Sci. 2021. PMID: 34681936 Free PMC article.
-
Cyclodextrins: Only Pharmaceutical Excipients or Full-Fledged Drug Candidates?Pharmaceutics. 2022 Nov 22;14(12):2559. doi: 10.3390/pharmaceutics14122559. Pharmaceutics. 2022. PMID: 36559052 Free PMC article. Review.
-
Effect of the Lipid Landscape on the Efficacy of Cell-Penetrating Peptides.Cells. 2023 Jun 23;12(13):1700. doi: 10.3390/cells12131700. Cells. 2023. PMID: 37443733 Free PMC article. Review.
-
Assessing anesthetic activity through modulation of the membrane dipole potential.J Lipid Res. 2017 Oct;58(10):1962-1976. doi: 10.1194/jlr.M073932. Epub 2017 Aug 17. J Lipid Res. 2017. PMID: 28818873 Free PMC article.
-
Novel insights into the modulation of the voltage-gated potassium channel KV1.3 activation gating by membrane ceramides.J Lipid Res. 2024 Aug;65(8):100596. doi: 10.1016/j.jlr.2024.100596. Epub 2024 Jul 15. J Lipid Res. 2024. PMID: 39019344 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
