An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission

Pfitzner, Anna-Katharina; Mercier, Vincent; Jiang, Xiuyun; Filseck, Joachim Moser von; Baum, Buzz; Šarić, Anđela; Roux, Aurélien

doi:10.1016/j.cell.2020.07.021

Cited by 143 publications

(241 citation statements)

References 70 publications

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“…In vitro reconstitutions suggest that Snf7, Vps24, and Vps2 are essential for membrane budding, and Vps4 for vesicle scission (11,17). Vps4-mediated turnover of a laterally-associating and helix-inducing polymer of Vps24-Vps2 would constrict the Snf7 scaffold to a fission-competent structure, as predicted by simulations (38) and as recently proposed to occur in archaeal cell division (39).…”

mentioning

confidence: 53%

“…Vps4-mediated turnover of a laterally-associating and helix-inducing polymer of Vps24-Vps2 would constrict the Snf7 scaffold to a fission-competent structure, as predicted by simulations (38) and as recently proposed to occur in archaeal cell division (39). While Did2 and Ist1 are not essential for intraluminal vesicle formation in vitro and in vivo, they have regulatory roles that are controlled by sequential polymerization dynamics through Vps4 (17). So far Vps60 has not been included in in-vitro analyses and there have been fewer in-vivo analyses on this protein.…”

mentioning

confidence: 66%

“…To quantitatively assess the relative contributions among the ESCRT proteins, we assayed for (18), and from in-vitro assays (11,17), which suggest that Snf7, Vps20, Vps24 and Vps2 are the minimal contributors in MVB formation.…”

Section: "Accessory" Escrt-iii Genes Promote Intralumenal Vesicle Formentioning

confidence: 99%

“…7B). In addition, Vps24/Vps2 induce lateral association and bundling (10,17,23), along with helicity of the spirals, which could be an important parameter for ESCRT-III function for MVB biogenesis.…”

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confidence: 99%

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Design Principles of the ESCRT-III Vps24-Vps2 Module

Banjade

Shah

Tang³

et al. 2020

Preprint

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ESCRT-III polymerization is required for all ESCRT-dependent events in the cell. However, the relative contributions of the eight ESCRT-III subunits differ between each process. The minimal features of ESCRT-III proteins necessary for function, and the role for the multiple ESCRT-III subunits remain unclear. To identify essential features of ESCRT-III subunits, we previously studied the polymerization mechanisms of two ESCRT-III subunits Snf7 and Vps24, identifying the association of the helix-4 region of Snf7 with the helix-1 region of Vps24 (Banjade et al., 2019). Here, we find that mutations in the helix-1 region of another ESCRT-III subunit Vps2 can functionally replace Vps24 in S. cerevisiae. Engineering and genetic selections revealed the required features of both subunits. Our data allow us to propose three minimal features required for ESCRT-III function – spiral formation, lateral association of the spirals through heteropolymerization, and binding to the AAA+ ATPase Vps4 for dynamic remodeling.

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confidence: 53%

mentioning

confidence: 66%

Section: "Accessory" Escrt-iii Genes Promote Intralumenal Vesicle Formentioning

confidence: 99%

mentioning

confidence: 99%

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Design Principles of the ESCRT-III Vps24-Vps2 Module

Banjade

Shah

Tang³

et al. 2020

Preprint

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“…A number of in vitro ultrastructural studies of ESCRT-III components are based on single-particle analyses by cryo-EM (Su et al, 2017;Maity et al, 2019;Bertin et al, 2020;Huber et al, 2020;Moser von Filseck et al, 2020;Nguyen et al, 2020;Pfitzner et al, 2020). While in vitro experiments provide useful structural information about the building blocks of the abscission machinery under artificial conditions, it is difficult to correlate this information with the dynamic attributes of the cytokinetic apparatus under physiological conditions.…”

Section: Discussionmentioning

confidence: 99%

A Structural View on ESCRT-Mediated Abscission

Horváth

Müller‐Reichert

2020

Front. Cell Dev. Biol.

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Plant endosomes as protein sorting hubs

2022

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Endocytosis, secretion, and endosomal trafficking are key cellular processes that control the composition of the plasma membrane. Through the coordination of these trafficking pathways, cells can adjust the composition, localization, and turnover of proteins and lipids in response to developmental or environmental cues. Upon being incorporated into vesicles and internalized through endocytosis, plant plasma membrane proteins are delivered to the trans-Golgi network (TGN). At the TGN, plasma membrane proteins are recycled back to the plasma membrane or transferred to multivesicular endosomes (MVEs), where they are further sorted into intralumenal vesicles for degradation in the vacuole. Both types of plant endosomes, TGN and MVEs, act as sorting organelles for multiple endocytic, recycling, and secretory pathways. Molecular assemblies such as retromer, ESCRT (endosomal sorting complex required for transport) machinery, small GTPases, adaptor proteins, and SNAREs associate with specific domains of endosomal membranes to mediate different sorting and membrane-budding events. In this review, we discuss the mechanisms underlying the recognition and sorting of proteins at endosomes, membrane remodeling and budding, and their implications for cellular trafficking and physiological responses in plants.

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An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission

Cited by 143 publications

References 70 publications

Design Principles of the ESCRT-III Vps24-Vps2 Module

Design Principles of the ESCRT-III Vps24-Vps2 Module

A Structural View on ESCRT-Mediated Abscission

Plant endosomes as protein sorting hubs

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