Design Principles of the ESCRT-III Vps24-Vps2 Module

Banjade, Sudeep; Shah, Yousuf H; Tang, Shaogeng; Emr, Scott D.

doi:10.1101/2020.12.28.424573

Cited by 3 publications

(2 citation statements)

References 49 publications

(57 reference statements)

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“…CHMP3 is dispensable for HIV-1 budding 21 and S. cerevisiae Vps24 can be substituted by Vps2 overexpression restoring partial endosomal cargo sorting 71 . Both processes depend on CHMP2A and Vps2 interaction with CHMP4 or Snf7 22,21 .…”

Section: Discussionmentioning

confidence: 99%

Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage

Azad

Guilligay

Boscheron

et al. 2023

Nat Struct Mol Biol

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Section: Discussionmentioning

confidence: 99%

Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage

Azad

Guilligay

Boscheron

et al. 2023

Nat Struct Mol Biol

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“…6, A and B). To study whether this valency dependence of ubiquitin-binding sites has any effect in vivo on cargo sorting, we used the model endocytosis cargo Mup1 and its sorting assays previously described (( 23 ). We made combinations of several mutations on Vps27 and Hse1 and studied the effects of these mutations on Mup1 sorting to the vacuole.…”

Section: Resultsmentioning

confidence: 99%

Recruitment and organization of ESCRT-0 and ubiquitinated cargo via condensation

et al. 2022

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The general mechanisms by which ESCRTs (Endosomal Sorting Complexes Required for Transport) are specifically recruited to various membranes, and how ESCRT subunits are spatially organized remain central questions in cell biology. At the endosome and lysosomes, ubiquitination of membrane proteins triggers ESCRT-mediated substrate recognition and degradation. Using the yeast lysosome/vacuole, we define the principles by which substrate engagement by ESCRTs occurs at this organelle. We find that multivalent interactions between ESCRT-0 and polyubiquitin are critical for substrate recognition at yeast vacuoles, with a lower-valency requirement for cargo engagement at endosomes. Direct recruitment of ESCRT-0 induces dynamic foci on the vacuole membrane and forms fluid condensates in vitro with polyubiquitin. We propose that self-assembly of early ESCRTs induces condensation, an initial step in ESCRT assembly/nucleation at membranes. This property can be tuned specifically at various organelles by modulating the number of binding interactions.

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Rules for the self-assembly of ESCRT-III on endosomes

Sprenger

Migliano

Oleschko

et al. 2021

Preprint

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The endosomal sorting complexes required for transport (ESCRT) mediate various membrane remodeling processes in cells by mechanism that are incompletely understood. Here we combined genetic experiments in budding yeast with site-specific cross-linking to identify rules that govern the self-assembly of individual ESCRT-III proteins into functional ESCRT-III complexes on endosomes. Together with current structural models of ESCRT-III, our findings suggest that, once nucleated, the growing Snf7 protofilament seeds the lateral co-assembly of a Vps24 - Vps2 heterofilament. Both Vps24 and Vps2 use positively charged amino acid residues in their helices α1 to interact with negatively charged amino acids in helix α4 of Snf7 subunits of the protofilament. In the Vps24 - Vps2 heterofilament, the two subunits alternate and interact with each other using hydrophobic interactions between helices α2/α3. The co-assembly of the Vps24 - Vps2 heterofilament restricts the lateral expansion of Snf7 protofilaments and leads the immediate recruitment of the AAA-ATPase Vps4. This self-assembly process of three ESCRT-III subunits results in the formation of a Snf7 protofilament and the co-assembly of a Vps24 - Vps2 heterofilament. This sets the stage for Vps4 recruitment and the subsequent ATP-driven dynamic self-organization of ESCRT-III / Vps4 assemblies and the ensuing membrane budding and scission events.

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Design Principles of the ESCRT-III Vps24-Vps2 Module

Cited by 3 publications

References 49 publications

Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage

Structural basis of CHMP2A–CHMP3 ESCRT-III polymer assembly and membrane cleavage

Recruitment and organization of ESCRT-0 and ubiquitinated cargo via condensation

Rules for the self-assembly of ESCRT-III on endosomes

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