Tubulation by Amphiphysin Requires Concentration-Dependent Switching from Wedging to Scaffolding

Isas, J. Mario; Ambroso, Mark R.; Hegde, Prabhavati B.; Langen, Jennifer; Langen, Ralf

doi:10.1016/j.str.2015.02.014

Cited by 47 publications

(95 citation statements)

References 61 publications

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“…What might be the mechanistic basis for this? N-BAR proteins such as amphiphysin and endophilin contain an N-terminal amphipathic ␣-helix (H0) that inserts into membranes and facilitates the anchoring of BAR domains to membranes (54)(55)(56). Some other BAR domain proteins harbor a lipid-binding domain such as the pleckstrin homology (PH) domain, which is important for membrane binding and the generation of membrane curvature (47,57).…”

Section: Discussionmentioning

confidence: 99%

BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

Chen

Fisher

et al. 2016

Molecular and Cellular Biology

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dChibby1 (Cby1) is a small, conserved coiled-coil protein that localizes to centrioles/basal bodies and plays a crucial role in the formation and function of cilia. During early stages of ciliogenesis, Cby1 is required for the efficient recruitment of small vesicles at the distal end of centrioles to facilitate basal body docking to the plasma membrane. Here, we identified family with sequence similarity 92, member A (FAM92A) and FAM92B, which harbor predicted lipid-binding BAR domains, as novel Cby1-interacting partners using tandem affinity purification and mass spectrometry. We found that in cultured cell lines, FAM92A colocalizes with Cby1 at the centrioles/basal bodies of primary cilia, while FAM92B is undetectable. In airway multiciliated cells, both FAM92A and -92B colocalize with Cby1 at the base of cilia. Notably, the centriolar localization of FAM92A and -92B depends largely on Cby1. Knockdown of FAM92A in RPE1 cells impairs ciliogenesis. Consistent with the membrane-remodeling properties of BAR domains, FAM92A and -92B in cooperation with Cby1 induce deformed membrane-like structures containing the small GTPase Rab8 in cultured cells. Our results therefore suggest that FAM92 proteins interact with Cby1 to promote ciliogenesis via regulation of membrane-remodeling processes.

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Section: Discussionmentioning

confidence: 99%

BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

Chen

Fisher

et al. 2016

Molecular and Cellular Biology

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“…By using electron paramagnetic resonance, it has recently been revealed that N-BAR domains differently bind spherical than cylindrical membranes [56,57]. On a spherical membrane, binding is primarily mediated by the helices while, on a membrane nanotube, the BAR domain more tightly adheres on the surface.…”

Section: Discussionmentioning

confidence: 99%

“…The surface density of proteins and the size of the vesicles are individually measured with total internal reflection microscopy, allowing a measure of the curvature-induced sorting with very good precision [55]. This measure is a priori complementary to the sorting deduced from nanotube experiments, but it is possible that the geometry of the membrane might influence how anisotropic proteins (such as BAR domains) bind to the surface, ultimately affecting their sorting [56,57].…”

Section: (D) Small Liposomesmentioning

confidence: 99%

Physical basis of some membrane shaping mechanisms

Šimunović

Prévost

Callan-Jones

et al. 2016

Phil. Trans. R. Soc. A.

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In vesicular transport pathways, membrane proteins and lipids are internalized, externalized or transported within cells, not by bulk diffusion of single molecules, but embedded in the membrane of small vesicles or thin tubules. The formation of these 'transport carriers' follows sequential events: membrane bending, fission from the donor compartment, transport and eventually fusion with the acceptor membrane. A similar sequence is involved during the internalization of drug or gene carriers inside cells. These membrane-shaping events are generally mediated by proteins binding to membranes. The mechanisms behind these biological processes are actively studied both in the context of cell biology and biophysics. Bin/amphiphysin/Rvs (BAR) domain proteins are ideally suited for illustrating how simple soft matter principles can account for membrane deformation by proteins. We review here some experimental methods and corresponding theoretical models to measure how these proteins affect the mechanics and the shape of membranes. In more detail, we show how an experimental method employing optical tweezers to pull a tube from a giant vesicle may give important quantitative insights into the mechanism by which proteins sense and generate membrane curvature and the mechanism of membrane scission.This article is part of the themed issue 'Soft interfacial materials: from fundamentals to formulation'.

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“…Some of the BAR superfamily proteins, such as N-BAR proteins, also have hydrophobic insertions. Experimentally, the membrane tubulation and curvaturesensing by various types of BAR superfamily proteins have been observed [7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Membrane structure formation induced by two types of banana-shaped proteins

Noguchi

Fournier

2017

Soft Matter

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The assembly of banana-shaped rodlike proteins on membranes, and the associated membrane shape transformations, are investigated by analytical theory and coarse-grained simulations. The membrane-mediated interactions between two banana-shaped inclusions are derived theoretically using a point-like formalism based on fixed anisotropic curvatures, both for zero surface tension and for finite surface tension. On a larger scale, the interactions between assemblies of such rodlike inclusions are determined analytically. Meshless membrane simulations are performed in the presence of a large number of inclusions of two types, corresponding to curved rods of opposite curvatures, both for flat membranes and vesicles. Rods of the same type aggregate into linear assemblies perpendicular to the rod axis, leading to membrane tubulation. However, rods of the other type, those of opposite curvature, are attracted to the lateral sides of these assemblies, and stabilize a straight bump structure that prevents tubulation. When the two types of rods have almost opposite curvatures, the bumps attract one another, forming a stripe structure. Positive surface tension is found to stabilize the stripe formation. The simulation results agree well with the theoretical predictions provided the point-like curvatures of the model are scaled-down to account for the effective flexibility of the simulated rods.

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Tubulation by Amphiphysin Requires Concentration-Dependent Switching from Wedging to Scaffolding

Cited by 47 publications

References 61 publications

BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

BAR Domain-Containing FAM92 Proteins Interact with Chibby1 To Facilitate Ciliogenesis

Physical basis of some membrane shaping mechanisms

Membrane structure formation induced by two types of banana-shaped proteins

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