Galimzyanov<i>et al.</i>Reply:

Galimzyanov, Timur R.; Molotkovsky, R. J.; Cohen, Fredric S.; Pohl, Peter; Akimov, Sergey A.

doi:10.1103/physrevlett.116.079802

Cited by 28 publications

(50 citation statements)

References 10 publications

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“…It is only clear that it requires neither cholesterol nor any other specific lipid or proteinaceous component (7,(9)(10)(11)(12). Most prevalent is the idea that the two leaflets interact at the membrane midplane via overhang.…”

Section: Introductionmentioning

confidence: 99%

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Undulations Drive Domain Registration from the Two Membrane Leaflets

Galimzyanov

Kuzmin

Pohl

et al. 2017

Biophysical Journal

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Phase separation in biological membranes plays an important role in protein targeting and transmembrane signaling. Its occurrence in both membrane leaflets commonly gives rise to matching liquid or liquid-ordered domains in the opposing monolayers. The underlying mechanism of such co-localization is not fully understood. The decrease of the line tension around the thicker ordered domain constitutes an important driving force. Yet, robust domain coupling requires an additional energy source, which we have now identified as thermal undulations. Our theoretical analysis of elastic deformations in a lipid bilayer shows that stiffer lipid domains tend to distribute into areas with lower fluctuations of monolayer curvature. These areas naturally align in the opposing monolayers. Thus, coupling requires both membrane leafs to display a heterogeneity in splay rigidities. The heterogeneity may either originate from intrinsic lipid properties or be acquired by adsorption of peripheral molecules. Undulations and line tension act synergistically: the gain in energy due a minimized line tension is proportional to domain radius and thus primarily fuels the registration of smaller domains; whereas the energetic contribution of undulations increases with membrane area and thus primarily acts to coalesce larger domains.

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Section: Introductionmentioning

confidence: 99%

“…Furthermore, it has been questioned if line tension alone may drive registration (19). That is, special conditions have been identified (the area S R of all L o domains per monolayer covers between 47% and 53% of the total membrane area S 0 ) in which minimization of the line tension fails to ensure domain registration (12).…”

Section: Introductionmentioning

confidence: 99%

Undulations Drive Domain Registration from the Two Membrane Leaflets

Galimzyanov

Kuzmin

Pohl

et al. 2017

Biophysical Journal

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“…Raft is thicker than the membrane around it [ 2 ]; deformations of the lipid matrix tend to compensate the hydrophobic mismatch and minimize the area of contact of raft lipid hydrocarbon chains with water occurring near its boundary [ 8 ]. Earlier, it was shown in a series of theoretical papers [ 9 , 10 , 11 , 12 ] that the minimum of the elastic energy of membranes corresponds to a nonzero shift of domain boundaries in opposing monolayers of the membrane. The calculated equilibrium magnitude of the shift is too small (~2–3 nm) to be optically detected.…”

Section: Introductionmentioning

confidence: 99%

Lateral Membrane Heterogeneity Regulates Viral-Induced Membrane Fusion during HIV Entry

Molotkovsky

Alexandrova

Galimzyanov

et al. 2018

IJMS

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Sphingomyelin- and cholesterol- enriched membrane domains, commonly referred to as “rafts” play a crucial role in a large number of intra- and intercellular processes. Recent experiments suggest that not only the volumetric inhomogeneity of lipid distribution in rafts, but also the arrangement of the 1D boundary between the raft and the surrounding membrane is important for the membrane-associated processes. The reason is that the boundary preferentially recruits different peptides, such as HIV (human immunodeficiency virus) fusion peptide. In the present work, we report a theoretical investigation of mechanisms of influence of the raft boundary arrangement upon virus-induced membrane fusion. We theoretically predict that the raft boundary can act as an attractor for viral fusion peptides, which preferentially distribute into the vicinity of the boundary, playing the role of ‘line active components’ of the membrane (‘linactants’). We have calculated the height of the fusion energy barrier and demonstrated that, in the case of fusion between HIV membrane and the target cell, presence of the raft boundary in the vicinity of the fusion site facilitates fusion. The results we obtained can be further generalized to be applicable to other enveloped viruses.

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“…They (i) triggered both domain dissolution and domain induction, and (ii) altered γ at the domain border in a way that stabilized domain size over an extended observation period. This is important because γ acts as the major driving force for registration of nanometer sized domains [ 21 , 43 ]. The registration of LODs (LDDs) from the two leaflets minimizes the energy w stored in the rim of every LOD (LDD) [ 21 , 43 ].…”

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confidence: 99%

“…This is important because γ acts as the major driving force for registration of nanometer sized domains [ 21 , 43 ]. The registration of LODs (LDDs) from the two leaflets minimizes the energy w stored in the rim of every LOD (LDD) [ 21 , 43 ]. We used the following parameters to calculate w : LOD’s hydrophobic thickness per monolayer h R = 1.8 nm, LDD’s hydrophobic thickness per monolayer h s = 1.3 nm, splay modulus of the LOD monolayer B R = 20 k B T , splay modulus of LDD monolayer B S = 10 k B T , and lateral compression-stretching modulus K A = 120 mN/m (per monolayer).…”

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confidence: 99%

Ordered Lipid Domains Assemble via Concerted Recruitment of Constituents from Both Membrane Leaflets

et al. 2020

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Lipid rafts serve as anchoring platforms for membrane proteins. Thus far they escaped direct observation by light microscopy due to their small size. Here we used differently colored dyes as reporters for the registration of both ordered and disordered lipids from the two leaves of a freestanding bilayer. Photoswitchable lipids dissolved or reformed the domains. Measurements of domain mobility indicated the presence of 120 nm wide ordered and 40 nm wide disordered domains. These sizes are in line with the predicted roles of line tension and membrane undulation as driving forces for alignment.

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Galimzyanovet al.Reply:

Cited by 28 publications

References 10 publications

Undulations Drive Domain Registration from the Two Membrane Leaflets

Undulations Drive Domain Registration from the Two Membrane Leaflets

Lateral Membrane Heterogeneity Regulates Viral-Induced Membrane Fusion during HIV Entry

Ordered Lipid Domains Assemble via Concerted Recruitment of Constituents from Both Membrane Leaflets

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