ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis

Tang, Shaogeng; Buchkovich, Nicholas J.; Henne, W. Mike; Banjade, Sudeep; Kim, Yun Jung; Emr, Scott D.

doi:10.7554/elife.15507

Cited by 71 publications

(91 citation statements)

References 23 publications

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“…In the ALIX case, the N-terminal BRO domain binds directly to a C-terminal CHMP4 helix located immediately downstream of the ordered ESCRT-III core domain (Figure 2). ALIX (Bro1) binding may thereby weaken autoinhibitory interactions, consistent with the observation that CHMP4 autoinhibition can be relieved by removing the terminal helix (Lata et al 2008b, 2009; Tang et al 2015, 2016). ALIX can dimerize (Pires et al 2009), and both ESCRT-II and ALIX may, therefore, help activate ESCRT-III subunits to form two filaments or even double-stranded filaments (Henne et al 2012, McCullough et al 2015, Mierzwa et al 2017, Teis et al 2010).…”

Section: Escrt-iiisupporting

confidence: 82%

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

McCullough

Frost

Sundquist

2018

Annu. Rev. Cell Dev. Biol.

215

268

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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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Section: Escrt-iiisupporting

confidence: 82%

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

McCullough

Frost

Sundquist

2018

Annu. Rev. Cell Dev. Biol.

215

268

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“…These data show that in mammalian cells ESCRT-I -II and ALIX comprise two partially redundant entry points to ESCRT-mediated membrane scission in MVB biogenesis, HIV-1 release, and cytokinesis. Moreover, this also appears to be true in yeast MVB biogenesis 23 .…”

Section: The Escrt Machinerymentioning

confidence: 72%

Reverse-topology membrane scission by the ESCRT proteins

Schöneberg

Lee

Iwasa

et al. 2016

Nat Rev Mol Cell Biol

355

411

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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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“…Strict control of this process is required, and many cellular components have been shown to direct Shrub to the membrane, and subsequently trigger assembly of the polymer (McCullough et al, 2013; Tang et al, 2016a). In the absence of this activation trigger, Shrub is maintained in a monomeric state within the cytosol.…”

Section: Discussionmentioning

confidence: 99%

Structural Basis for Regulation of ESCRT-III Complexes by Lgd

McMillan¹,

Tibbe²,

Drabek³

et al. 2017

Cell Reports

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SUMMARY The ESCRT-III complex induces outward membrane budding and fission through homotypic polymerization of its core component Shrub/CHMP4B. Shrub activity is regulated by its direct interaction with a protein called Lgd in flies, or CC2D1A or B in humans. Here, we report the structural basis for this interaction, and propose a mechanism for regulation of polymer assembly. The isolated third DM14 repeat of Lgd binds Shrub, and an Lgd fragment containing only this DM14 repeat and its C-terminal C2 domain is sufficient for in vivo function. The DM14 domain forms a helical hairpin with a conserved, positively charged tip, that, in the structure of a DM14 domain-Shrub complex, occupies a negatively charged surface of Shrub that is otherwise used for homopolymerization. Lgd mutations at this interface disrupt its function in flies, confirming functional importance. Together, these data argue that Lgd regulates ESCRT activity by controlling access to the Shrub self-assembly surface.

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ESCRT-III activation by parallel action of ESCRT-I/II and ESCRT-0/Bro1 during MVB biogenesis

Cited by 71 publications

References 23 publications

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

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

Reverse-topology membrane scission by the ESCRT proteins

Structural Basis for Regulation of ESCRT-III Complexes by Lgd

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