ESCRT Filaments as Spiral Springs

Carlson, Lars A.; Shen, Qing-Tao; Pavlin, Mark Remec; Hurley, James H.

doi:10.1016/j.devcel.2015.11.007

Cited by 23 publications

(22 citation statements)

References 8 publications

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“…Furthermore, the correct calculations show that the minimal membrane–protein adhesion strength required for membrane scission by dome-shaped assemblies is over two-fold higher than had been previously predicted. For cone-shaped assemblies, we have demonstrated within the theoretical framework of curvature elasticity and membrane-protein adhesion that cone flattening as recently proposed [1, 22] can indeed lead to closure and scission of the membrane neck. In fact, we showed that neck closure and scission are ‘easier’ in the cone model than in the dome model, in the sense that the minimal membrane–protein adhesion strength required for membrane scission is lower in the cone model.…”

Section: Resultsmentioning

confidence: 52%

“…It was first speculated in Ref [22] that flattening of the ESCRT cone could lead to narrowing and eventually scission of the membrane neck, and this hypothesis was described in more detail in Ref [1]. However, no quantitative explanation of why cone flattening should lead to narrowing of the neck has been given so far.…”

Section: Resultsmentioning

confidence: 99%

“…[5, 19–21] Furthermore, in vitro experiments provide evidence that ESCRT-III spirals polymeryze most probably outwards, forming consecutively wider rings. [14] For these and other reasons, a new mechanism has been recently proposed as described by the ‘buckling model’, [1, 22] which proposes that the ESCRT-III complex assembles at the neck and grows away from the bud in the shape of a truncated cone, until further growth or assembly of specific ESCRT components triggers an instability that flattens the cone into a planar spiral, thereby leading to scission of the membrane neck, see Fig 1B. Because the main ingredient of the mechanism is not buckling, but rather the reverse of it, we will refer to it as the flattening cone model in the following.…”

Section: Introductionmentioning

confidence: 99%

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Domes and cones: Adhesion-induced fission of membranes by ESCRT proteins

Agudo-Canalejo

Lipowsky

2018

PLoS Comput Biol

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ESCRT proteins participate in the fission step of exocytic membrane budding, by assisting in the closure and scission of the membrane neck that connects the nascent bud to the plasma membrane. However, the precise mechanism by which the proteins achieve this so-called reverse-topology membrane scission remains to be elucidated. One mechanism is described by the dome model, which postulates that ESCRT-III proteins assemble in the shape of a hemispherical dome at the location of the neck, and guide the closure of this neck via membrane–protein adhesion. A different mechanism is described by the flattening cone model, in which the ESCRT-III complex first assembles at the neck in the shape of a cone, which then flattens leading to neck closure. Here, we use the theoretical framework of curvature elasticity and membrane–protein adhesion to quantitatively describe and compare both mechanisms. This comparison shows that the minimal adhesive strength of the membrane–protein interactions required for scission is much lower for cones than for domes, and that the geometric constraints on the shape of the assembly required to induce scission are more stringent for domes than for cones. Finally, we compute for the first time the adhesion-induced constriction forces exerted by the ESCRT assemblies onto the membrane necks. These forces are higher for cones and of the order of 100 pN.

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Section: Resultsmentioning

confidence: 52%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Domes and cones: Adhesion-induced fission of membranes by ESCRT proteins

Agudo-Canalejo

Lipowsky

2018

PLoS Comput Biol

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“…Buckling can directly give rise to membrane invaginations 57 . It is also possible for buckling to run in reverse and to lead to membrane scission 103 , as shown at the end of Video 3 and in Fig. 7c.…”

Section: Scission Mechanismmentioning

confidence: 95%

Reverse-topology membrane scission by the ESCRT proteins

Schöneberg

Lee

Iwasa

et al. 2016

Nat Rev Mol Cell Biol

380

419

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Preface The narrow membrane necks formed during viral, exosomal, and intra-endosomal budding from membranes, cytokinesis, and related processes have interiors that are contiguous with the cytosol. The severing of these necks involves action from the opposite face of the membrane as compared to the well-characterized coated vesicle pathways, and is referred to as “reverse” or “inverse” topology membrane scission. This process is carried out by the endosomal sorting complexes required for transport (ESCRT) proteins. In particular, the ESCRT-III proteins can form filaments, flat spirals, tubes and conical funnels, which are thought to somehow direct membrane remodeling and scission. Their assembly, and their disassembly by the ATPase VPS4, has been intensively studied, but the mechanism of scission has been elusive. New insights from cryo-electron microscopy and various types of spectroscopy may finally be close to rectifying this situation.

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“…Importantly, the energy required for the subsequent membrane fission reaction could be provided through an ATP-dependent reversal of the transition from tubular back to planar filaments (Carlson et al 2015). In this model, extruded membranes would be drawn together and a cargo-filled vesicle released from the end of the tubule when the ESCRT-III filaments pulled on the tubule base by retracting back out of the tubule to readopt a planar configuration.…”

Section: Membrane Remodeling Constriction and Fissionmentioning

confidence: 99%

Structures, Functions, and Dynamics of ESCRT-III/Vps4 Membrane Remodeling and Fission Complexes

McCullough

Frost

Sundquist

2018

Annu. Rev. Cell Dev. Biol.

231

272

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The endosomal sorting complexes required for transport (ESCRT) pathway mediates cellular membrane remodeling and fission reactions. The pathway comprises five core complexes: ALIX, ESCRT-I, ESCRT-II, ESCRT-III, and Vps4. These soluble complexes are typically recruited to target membranes by site-specific adaptors that bind one or both of the early-acting ESCRT factors: ALIX and ESCRT-I/ESCRT-II. These factors, in turn, nucleate assembly of ESCRT-III subunits into membrane-bound filaments that recruit the AAA ATPase Vps4. Together, ESCRT-III filaments and Vps4 remodel and sever membranes. Here, we review recent advances in our understanding of the structures, activities, and mechanisms of the ESCRT-III and Vps4 machinery, including the first high-resolution structures of ESCRT-III filaments, the assembled Vps4 enzyme in complex with an ESCRT-III substrate, the discovery that ESCRT-III/Vps4 complexes can promote both inside-out and outside-in membrane fission reactions, and emerging mechanistic models for ESCRT-mediated membrane fission.

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ESCRT Filaments as Spiral Springs

Abstract: In a recent issue of Cell, Chiaruttini et al. (2015) reveal the mechanical properties of the mysterious spiral filaments formed by the yeast ESCRT-III protein Snf7. The spirals are shown to be springs whose bending drives membrane deformation and perhaps membrane scission.

Cited by 23 publications

References 8 publications

Domes and cones: Adhesion-induced fission of membranes by ESCRT proteins

Domes and cones: Adhesion-induced fission of membranes by ESCRT proteins

Reverse-topology membrane scission by the ESCRT proteins

Structures, Functions, and Dynamics of ESCRT-III/Vps4 Membrane Remodeling and Fission Complexes

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