Protein induced lipid demixing in homogeneous membranes

Stumpf, Bernd Henning; Nowakowski, Piotr; Eggeling, Christian; Maciołek, Anna; Smith, Ana‐Sunčana

doi:10.1103/physrevresearch.3.l042013

Cited by 8 publications

(10 citation statements)

References 47 publications

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“…Multi-component lipid bilayers exhibit local heterogeneity that can get enhanced due to the presence of adsorbed polymers, bound proteins, or other macromolecules. [72][73][74][75] Local lipid demixing can eventually lead to an altered membrane morphology (due to different spontaneous curvatures of lipid components), which has far-reaching consequences in biology.…”

Section: Local Demixing Of Lipidsmentioning

confidence: 99%

Coacervation of poly-electrolytes in the presence of lipid bilayers: mutual alteration of structure and morphology

Mondal

Cui

2022

Chem. Sci.

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Section: Local Demixing Of Lipidsmentioning

confidence: 99%

Coacervation of poly-electrolytes in the presence of lipid bilayers: mutual alteration of structure and morphology

Mondal

Cui

2022

Chem. Sci.

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“…Of course, the further away from the origin we go, the smaller the magnitudes of the order parameters are. We identify the perturbation in the order parameters caused by the presence of the anchor with experimentally observed so-called domains of lipids that form around the pinning points [21,22]. In order to facilitate the comparison between our model and experimental systems, it is necessary to introduce an effective size R of the induced domain.…”

Section: Order Parameter Profiles and Size Of Induced Domainsmentioning

confidence: 99%

“…Depending on the sign of the hydrophobic mismatch, the lipid composition around the protein will preferentially be in one of the two phases (Lo or Ld). In this complementary mechanism, the composition of the membrane is coupled to its thickness [20,21], and not necessarily to the overall spontaneous curvature of the membrane.…”

Section: Introductionmentioning

confidence: 99%

“…Further detailed analysis was both performed analytically and in simulations by several groups [22][23][24][25][26][27][28]. The thickness mechanism was suggested in a numerical study [20], while the analytic approach was then put froward only last year by us [21]. In Ref.…”

Section: Introductionmentioning

confidence: 99%

“…[21], we proposed a model which couples the elasticity theory of lipid bilayer thickness deformations [16,20,29,30] with the Landau-Ginzburg theory of critical demixing transition and with the inclusions. Our model was able to reproduce experimental observations of the formation of lipid domains around lipids linked to a reconstituted actin cortex filament in a model membrane [21,22]. In these experiments the lipid bilayer was supported, which strongly suppresses spontaneous curvature effects.…”

Section: Introductionmentioning

confidence: 99%

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Protein-lipid domains in heterogeneous membranes beyond spontaneous curvature effects

Nowakowski¹,

Stumpf²,

Smith³

et al. 2022

Preprint

Self Cite

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We study a model of a lipid bilayer membrane described by two order parameters: the chemical composition described using the Gaussian model and the spatial configuration described with the elastic deformation model of a membrane with a finite thickness, or equivalently, for an adherent membrane. We assume and explain on physical grounds the linear coupling between the two order parameters. Using the exact solution, we calculate the correlation functions and order parameters profiles. We also study the domains that form around inclusions on the membrane. We propose and compare six distinct ways to quantify the size of such domains. Despite of its simplicity, the model has many interesting features like Fisher-Widom line or two distinct critical regions.

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Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami

Kanwa

Gavrilovic

Brüggenthies

et al. 2023

Adv Materials Inter

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Self‐assembly of biological molecules and structures is a fundamental property of life. Whereas most biological functions are based on self‐assembled proteins and protein complexes, the self‐assembly of lipids is important for the spatial organization of heterogeneous cellular reaction environments and to catalyze cooperative interactions on/with membranes. Lipid domains or “rafts”, which are known to selectively recruit proteins, play an important functional role in sorting and trafficking of membrane components between subcellular organelles. However, how the recruitment and interactions of proteins in turn contributes to the formation and turnover of these structures has not been systematically addressed, due to the large variety in membrane–protein features and their spatiotemporal dynamics. The small size and transient nature of lipid domains adds to the complexity in visualizing them in living cells. Here, DNA origami is presented as a programmable tool to mimic protein clustering and assembly on membranes and illustrate how nanometer sized lipid domains coalesce into visible domains upon origami self‐assembly in defined patterns. Hence, the local membrane composition can be efficiently regulated by the self‐assembly of peripheral membrane binders. This reinforces the hypothesis that lipid rafts in cells occur as a result of membrane–protein interactions and, in particular, protein self‐assembly.

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Protein induced lipid demixing in homogeneous membranes

Cited by 8 publications

References 47 publications

Coacervation of poly-electrolytes in the presence of lipid bilayers: mutual alteration of structure and morphology

Coacervation of poly-electrolytes in the presence of lipid bilayers: mutual alteration of structure and morphology

Protein-lipid domains in heterogeneous membranes beyond spontaneous curvature effects

Inducing Lipid Domains in Membranes by Self‐Assembly of DNA Origami

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