The relationship between membrane curvature generation and clustering of anchored proteins: a computer simulation study

Yue, Tongtao; Li, Shuangyang; Zhang, Xuehua; Wang, Wenchuan

doi:10.1039/c0sm00418a

Cited by 67 publications

(85 citation statements)

References 49 publications

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“…6B). Recent computational studies hypothesized that deep membrane insertion of a hydrophobic moiety increases the stability and rate of protein self-assembly (34,35,52), whereas shallow insertion effectively produces or stabilizes highly curved membranes (33,44). We postulate that deep membrane insertion may promote direct SpoVM-SpoVM intermolecular interactions to form higherorder structures, or promote clustering of SpoVM molecules within the lipid bilayer indirectly through membrane-protein interactions, to produce the observed modest binding cooperativity.…”

Section: Discussionmentioning

confidence: 83%

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Structural basis for the geometry-driven localization of a small protein

Gill

Castaing

Hsin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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In bacteria, certain shape-sensing proteins localize to differently curved membranes. During sporulation in Bacillus subtilis, the only convex (positively curved) surface in the cell is the forespore, an approximately spherical internal organelle. Previously, we demonstrated that SpoVM localizes to the forespore by preferentially adsorbing onto slightly convex membranes. Here, we used NMR and molecular dynamics simulations of SpoVM and a localization mutant (SpoVM P9A ) to reveal that SpoVM's atypical amphipathic α-helix inserts deeply into the membrane and interacts extensively with acyl chains to sense packing differences in differently curved membranes. Based on binding to spherical supported lipid bilayers and Monte Carlo simulations, we hypothesize that SpoVM's membrane insertion, along with potential cooperative interactions with other SpoVM molecules in the lipid bilayer, drives its preferential localization onto slightly convex membranes. Such a mechanism, which is distinct from that used by high curvature-sensing proteins, may be widely conserved for the localization of proteins onto the surface of cellular organelles.ArfGAP1 | SpoIVA | DivIVA | curvature sensing | lipid packing

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Section: Discussionmentioning

confidence: 83%

“…Previous computational studies proposed a link between the topology of a peripheral membrane protein and its ability to detect highly curved membranes (33)(34)(35).…”

Section: Curvature-dependent Adsorption Through Slight Increases In Bmentioning

confidence: 99%

Structural basis for the geometry-driven localization of a small protein

Gill

Castaing

Hsin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…A variety of experimental and simulation studies have investigated other factors which can affect protein aggregation in biological and model membranes in general, such as the degree of hydrophobic mismatch between protein and lipid [36], [52], [54]–[58] (which can also affect local stretching or compression of the surrounding membrane [59], [60]), membrane curvature [52], [61], [62], and the effect of cholesterol on adaptations to the protein-lipid interface [57]. It is also feasible that the degree of hydration at the membrane-water-protein interface (a function of the TM region structure, as well as the membrane environment [63]) may affect protein aggregation.…”

Section: Discussionmentioning

confidence: 99%

Formation of Raft-Like Assemblies within Clusters of Influenza Hemagglutinin Observed by MD Simulations

et al. 2013

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The association of hemagglutinin (HA) with lipid rafts in the plasma membrane is an important feature of the assembly process of influenza virus A. Lipid rafts are thought to be small, fluctuating patches of membrane enriched in saturated phospholipids, sphingolipids, cholesterol and certain types of protein. However, raft-associating transmembrane (TM) proteins generally partition into Ld domains in model membranes, which are enriched in unsaturated lipids and depleted in saturated lipids and cholesterol. The reason for this apparent disparity in behavior is unclear, but model membranes differ from the plasma membrane in a number of ways. In particular, the higher protein concentration in the plasma membrane may influence the partitioning of membrane proteins for rafts. To investigate the effect of high local protein concentration, we have conducted coarse-grained molecular dynamics (CG MD) simulations of HA clusters in domain-forming bilayers. During the simulations, we observed a continuous increase in the proportion of raft-type lipids (saturated phospholipids and cholesterol) within the area of membrane spanned by the protein cluster. Lateral diffusion of unsaturated lipids was significantly attenuated within the cluster, while saturated lipids were relatively unaffected. On this basis, we suggest a possible explanation for the change in lipid distribution, namely that steric crowding by the slow-diffusing proteins increases the chemical potential for unsaturated lipids within the cluster region. We therefore suggest that a local aggregation of HA can be sufficient to drive association of the protein with raft-type lipids. This may also represent a general mechanism for the targeting of TM proteins to rafts in the plasma membrane, which is of functional importance in a wide range of cellular processes.

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“…In addition, there have been a number of computational investigations on the interactions of cylindrical inclusions and preassembled lipid membranes [32][33][34][35][36][37][38][39][40][41][42][43][44][45][46][47][48]. Our earlier investigations on the self-assembly of lipids and nanotubes with hairs at both ends demonstrated their selforganization into a hybrid vesicle or a bicelle, depending upon the relative fraction of NTs to lipids in the solution [49].…”

Section: Introductionmentioning

confidence: 99%

Interactions of End-functionalized Nanotubes with Lipid Vesicles: Spontaneous Insertion and Nanotube Self-Organization

Dutt¹,

Nayhouse²,

Kuksenok³

et al. 2011

CNANO

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Via Dissipative Particle Dynamics (DPD) approach, we study the spontaneous insertion of amphiphilic nanotubes into a lipid vesicle, which is immersed in a hydrophilic solvent. Individual lipids are composed of a hydrophilic head group and two hydrophobic tails. Each nanotube encompasses an ABA architecture, with a hydrophobic shaft (B) and two hydrophilic ends (A). To facilitate the selective transport of species through the nanotubes, we introduce hydrophilic tethers at one end of the tube. We show that nanotubes initially located in the host solvent spontaneously penetrate the vesicle's membrane and assume a transmembrane position, with the hydrophilic tethers extending from the surface of the vesicle. Adding nanotubes one at a time after the previous nanotube has been inserted, we characterize the interactions among the nanotubes that have self-assembled into the vesicle's membrane and focus on their clustering within the membrane. We also show that the nanotube insertion and clustering within the vesicle strongly affects the vesicle shape in cases of a sufficiently large number of tubes. Ultimately, these nanotube-lipid systems can be used for creating hybrid controlled release vesicles.

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The relationship between membrane curvature generation and clustering of anchored proteins: a computer simulation study

Cited by 67 publications

References 49 publications

Structural basis for the geometry-driven localization of a small protein

Structural basis for the geometry-driven localization of a small protein

Formation of Raft-Like Assemblies within Clusters of Influenza Hemagglutinin Observed by MD Simulations

Interactions of End-functionalized Nanotubes with Lipid Vesicles: Spontaneous Insertion and Nanotube Self-Organization

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