Undulations Drive Domain Registration from the Two Membrane Leaflets

Galimzyanov, Timur R.; Kuzmin, Peter I.; Pohl, Peter; Akimov, Sergey A.

doi:10.1016/j.bpj.2016.12.023

Cited by 35 publications

(49 citation statements)

References 40 publications

(52 reference statements)

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“…The experimentally determined coupling energy of two L o monolayer domains into the bilayer L o /L o domain 16 effectively arises from the energy penalty of assembly of a "hybrid" L o /L d bilayer. Recently, the origin of the penalty has been attributed to the unfavorable amplitude of thermal undulations of the "hybrid" L o /L d bilayer as compared to two symmetric coexisting L o /L o and L d /L d membrane regions 18,19,21 . This coupling mechanism has entropic nature and cannot be described in terms of our elastic model, as the model does not explicitly consider thermal fluctuations.…”

Section: Statement Of the Problemmentioning

confidence: 99%

Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting

Pinigin

Kondrashov

Jiménez-Munguía

et al. 2020

Sci Rep

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Liquid-ordered lipid domains represent a lateral inhomogeneity in cellular membranes. these domains have elastic and physicochemical properties different from those of the surrounding membrane. in particular, their thickness exceeds that of the disordered membrane. thus, elastic deformations arise at the domain boundary in order to compensate for the thickness mismatch. in equilibrium, the deformations lead to an incomplete register of monolayer ordered domains: the elastic energy is minimal if domains in opposing monolayers lie on the top of each other, and their boundaries are laterally shifted by about 3 nm. This configuration introduces a region, composed of one ordered and one disordered monolayers, with an intermediate bilayer thickness. Besides, a jump in a local monolayer curvature takes place in this intermediate region, concentrating here most of the elastic stress. This region can participate in a lateral sorting of membrane inclusions by offering them an optimal bilayer thickness and local curvature conditions. In the present study, we consider the sorting of deformable lipid inclusions, undeformable peripheral and deeply incorporated peptide inclusions, and undeformable transmembrane inclusions of different molecular geometry. With rare exceptions, all types of inclusions have an affinity to the ordered domain boundary as compared to the bulk phases. the optimal lateral distribution of inclusions allows relaxing the elastic stress at the boundary of domains.Cellular membranes are laterally heterogeneous 1-3 . Many membrane proteins are believed to function properly only inside lipid-protein domains, also referred to as rafts 4-7 . Proteins in these domains are surrounded by a more or less thick lipid shell [8][9][10][11] . In model purely lipidic systems it is demonstrated that lipids can form similar domains, in which they are in a liquid-ordered (L o ) phase state, while the surrounding membrane is liquid-disordered (L d ) [12][13][14][15] . Ordered domains are usually bilayer, i.e. exist in both membrane leaflets at the same lateral position [14][15][16][17] . Such transbilayer coupling could be driven by elastic deformations arising at the domain boundary and by membrane thermal fluctuations 18-21 . The mechanism of this coupling is not specific to the exact lipid composition of the domain: only the higher ordering of lipids with respect to the surrounding membrane is important [22][23][24] . A bilayer structure of rafts is believed to be a key property in providing raft-dependent signal transduction across the plasma membrane 4,5 . There are increasing evidences that a raft interior itself may be laterally inhomogeneous: some molecules may prefer its boundary region rather than its bulk part. In particular, the fusion peptide of the human immunodeficiency virus (HIV) gp41 protein functions with the highest efficiency only in the presence of the L o /L d phase boundary in the target membrane 25,26 . In addition, the HIV receptor CCR5 preferentially localizes at the domain boundary 26 . It means t...

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Section: Statement Of the Problemmentioning

confidence: 99%

Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting

Pinigin

Kondrashov

Jiménez-Munguía

et al. 2020

Sci Rep

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“…In general, due to the difference in RA-PE adduct distribution between the two leaflets, asymmetric changes of spontaneous membrane curvature may arise. In turn, the stability of membrane domains (lipid rafts) may be altered [112].…”

Section: Modification Of Membrane Properties By Pe and Pe Adductsmentioning

confidence: 99%

The Role of Phosphatidylethanolamine Adducts in Modification of the Activity of Membrane Proteins under Oxidative Stress

Pohl

Jovanović

2019

Molecules

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Reactive oxygen species (ROS) and their derivatives, reactive aldehydes (RAs), have been implicated in the pathogenesis of many diseases, including metabolic, cardiovascular, and inflammatory disease. Understanding how RAs can modify the function of membrane proteins is critical for the design of therapeutic approaches in the above-mentioned pathologies. Over the last few decades, direct interactions of RA with proteins have been extensively studied. Yet, few studies have been performed on the modifications of membrane lipids arising from the interaction of RAs with the lipid amino group that leads to the formation of adducts. It is even less well understood how various multiple adducts affect the properties of the lipid membrane and those of embedded membrane proteins. In this short review, we discuss a crucial role of phosphatidylethanolamine (PE) and PE-derived adducts as mediators of RA effects on membrane proteins. We propose potential PE-mediated mechanisms that explain the modulation of membrane properties and the functions of membrane transporters, channels, receptors, and enzymes. We aim to highlight this new area of research and to encourage a more nuanced investigation of the complex nature of the new lipid-mediated mechanism in the modification of membrane protein function under oxidative stress.

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“…In contrast, stiffer ordered domains localise to areas with lower curvature ( R 2 ), which naturally coincide with the opposing monolayers (Galimzyanov et al. 2017) …”

Section: Lipid–lipid Lipid–water and Lipid–water–solute Interactionsmentioning

confidence: 99%

“…The simple reason for this is that stiffer lipid domains localise to areas with lower monolayer curvature (Galimzyanov et al. 2017). These areas naturally coincide with opposing monolayers.…”

Section: Lipid–lipid Lipid–water and Lipid–water–solute Interactionsmentioning

confidence: 99%

Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology

et al. 2018

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Undulations Drive Domain Registration from the Two Membrane Leaflets

Cited by 35 publications

References 40 publications

Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting

Elastic deformations mediate interaction of the raft boundary with membrane inclusions leading to their effective lateral sorting

The Role of Phosphatidylethanolamine Adducts in Modification of the Activity of Membrane Proteins under Oxidative Stress

Understanding Conformational Dynamics of Complex Lipid Mixtures Relevant to Biology

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