Cluster Formation of Anchored Proteins Induced by Membrane-Mediated Interaction

Li, Shuangyang; Zhang, Xuehua; Wang, Wenchuan

doi:10.1016/j.bpj.2010.02.032

Cited by 40 publications

(36 citation statements)

References 55 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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“…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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“…In particular, the role of shape complementarity in the protein-protein interactions is still very poorly understood for the case without the electrostatic-complementarity and hydrophobic mismatch. Computer simulation methods have become increasingly valuable to extract information about structural and dynamical properties at a molecular level, and a lot of simulation studies have been performed to explore the interactions of proteins with the membrane 14 19 20 21 22 23 24 25 . However, to our knowledge, only few studies were focused on the protein shape-complementarity caused by non-specific interactions 26 27 .…”

mentioning

confidence: 99%

The Role of Shape Complementarity in the Protein-Protein Interactions

Zhang

Cao

2013

Sci Rep

Self Cite

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We use a dissipative particle dynamic simulation to investigate the effects of shape complementarity on the protein-protein interactions. By monitoring different kinds of protein shape-complementarity modes, we gave a clear mechanism to reveal the role of the shape complementarity in the protein-protein interactions, i.e., when the two proteins with shape complementarity approach each other, the conformation of lipid chains between two proteins would be restricted significantly. The lipid molecules tend to leave the gap formed by two proteins to maximize the configuration entropy, and therefore yield an effective entropy-induced protein-protein attraction, which enhances the protein aggregation. In short, this work provides an insight into understanding the importance of the shape complementarity in the protein-protein interactions especially for protein aggregation and antibody–antigen complexes. Definitely, the shape complementarity is the third key factor affecting protein aggregation and complex, besides the electrostatic-complementarity and hydrophobic complementarity.

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Cluster Formation of Anchored Proteins Induced by Membrane-Mediated Interaction

Cited by 40 publications

References 55 publications

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

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

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

The Role of Shape Complementarity in the Protein-Protein Interactions

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