Vps60 initiates alternative ESCRT-III filaments

Pfitzner, Anna-Katharina; Zivkovic, Henry; Bernat-Silvestre, César; West, Matt; Peltier, Tanner; Humbert, Frédéric; Odorizzi, Greg; Roux, Aurélien

doi:10.1083/jcb.202206028

Cited by 10 publications

(6 citation statements)

References 79 publications

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“…We have suggested before that ESCRT-III complexes undergo remodeling during the process of ILV formation (ALSLEBEN AND KÖLLING 2022). Especially the relationship between the Snf7 complex and the Mos10 complex is unclear at present (ALSLEBEN AND KÖLLING 2022;PFITZNER et al 2023). It is possible that the complex precipitated by Tms1 represents a late stage in the ESCRT-III cycle.…”

Section: Vps55 and Tms1 Interact With Escrt-iiimentioning

confidence: 99%

“…We have been especially interested in the ESCRT-III associated protein Mos10 (also known as Vps60) (KRANZ et al 2001). Recent evidence suggests that Mos10 forms an alternative ESCRT-III complex independent of the canonical Snf7 containing complex (ALSLEBEN AND KÖLLING 2022;PFITZNER et al 2023). Both complexes appear to be involved in the formation of intraluminal vesicles (ILVs) during multivesicular body (MVB) formation in the endocytic pathway (PFITZNER et al 2023).…”

Section: Introductionmentioning

confidence: 99%

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Link between lipid remodeling and ESCRT-III function in multivesicular body formation

Kölling

2023

Preprint

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Despite a tremendous amount of work, it is still unclear how the endosomal sorting complex required for transport (ESCRT)-III complex acts in membrane remodeling and abscission. Here we present evidence that a change in membrane composition is connected to ESCRT-III function during multivesicular body (MVB) formation. The central observation was a strong synergistic effect of two mutations on the turnover of an endocytic cargo protein. One mutation deletes Tms1, a yeast SERINC homologue. Human SERINC3 and SERINC5 are HIV-1 restriction factors and have been shown to act as scramblases, flipping phospholipids between membrane leaflets. The other mutation deletes the Vps68 subunit of the Vps55/Vps68 complex, which loosely resembles Tms1 in its overall structure. The strong synergistic effect suggests that Tms1 and Vps55/Vps68 perform a similar function. Since we could also show that Vps55 physically interacts with ESCRT-III, we propose that a scramblase is recruited to ESCRT-III and prepares the membrane for intraluminal vesicles formation at MVBs.SummaryIt is still unclear how ESCRT-III acts on membranes. Here evidence is presented that ESCRT-III recruits a scramblase to the site of intraluminal vesicle formation at late endosomes indicating that a change in membrane composition is crucial for MVB formation.

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Section: Vps55 and Tms1 Interact With Escrt-iiimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Link between lipid remodeling and ESCRT-III function in multivesicular body formation

Kölling

2023

Preprint

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“…The remodeling of late endosomes into MVBs occurs after the invagination of their membrane. This results in the formation of a multitude of small vesicles called intraluminal vesicles (ILVs) [ 31 , 32 ]. In the course of this remodeling process, ILVs can be loaded with exceptionally diverse molecules ranging from cytosolic proteins to metabolites, lipids, and even nucleic acids.…”

Section: Exosomes Are Small Specialized Extracellular Vesicles (Evs)mentioning

confidence: 99%

Exosome-Mediated Antigen Delivery: Unveiling Novel Strategies in Viral Infection Control and Vaccine Design

El Safadi,

Mokhtari,

Krejbich

et al. 2024

Vaccines

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Exosomes are small subtypes of extracellular vesicles (EVs) naturally released by different types of cells into their environment. Their physiological roles appear to be multiple, yet many aspects of their biological activities remain to be understood. These vesicles can transport and deliver a variety of cargoes and may serve as unconventional secretory vesicles. Thus, they play a crucial role as important vectors for intercellular communication and the maintenance of homeostasis. Exosome production and content can vary under several stresses or modifications in the cell microenvironment, influencing cellular responses and stimulating immunity. During infectious processes, exosomes are described as double-edged swords, displaying both beneficial and detrimental effects. Owing to their tractability, the analysis of EVs from multiple biofluids has become a booming tool for monitoring various pathologies, from infectious to cancerous origins. In this review, we present an overview of exosome features and discuss their particular and ambiguous functions in infectious contexts. We then focus on their properties as diagnostic or therapeutic tools. In this regard, we explore the capacity of exosomes to vectorize immunogenic viral antigens and their function in mounting adaptive immune responses. As exosomes provide interesting platforms for antigen presentation, we further review the available data on exosome engineering, which enables peptides of interest to be exposed at their surface. In the light of all these data, exosomes are emerging as promising avenues for vaccine strategies.

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“…However, this distinction does not appear to be justified, since all ESCRT-III proteins can team up in various combinations during different cellular processes. For instance, evidence has been presented in yeast for the existence of at least two alternative ESCRT-III complexes, which are based on Chm7 or Mos10, respectively (Bauer, Brune et al 2015; Webster, Thaller et al 2016; Gu, LaJoie et al 2017; Alsleben and Kölling 2022; Pfitzner, Zivkovic et al 2023).…”

Section: Introductionmentioning

confidence: 99%

Identification of ESCRT-III like protein sequences in yeast

Brune,

Kölling

2024

Preprint

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Endosomal sorting complex required for transport (ESCRT-III) is a membrane remodeling complex involved in a large number of cellular processes. It appears to perform an essential function in eukaryotes, since to date no eukaryotic organism completely devoid of ESCRT-III has been found. Yet, yeast cells with a deletion of all eight known ESCRT-III genes are viable. We therefore searched for new, previously undiscovered ESCRT-III like proteins in yeast. HHPred uncovered several proteins with similarity to Snf7. The similarity was mostly restricted to the α1-α2 hairpin region of Snf7. A conserved pattern of amino acids was detected in this region. The protein encoded by ORF YPL199c strikingly resembled Snf7 in its secondary structure. Since this protein could be the ninth member of the ESCRT-III family in yeast, we called it Nbr9 ("number nine"). Nbr9 is palmitoylated and localizes to the plasma membrane. In contrast to other palmitoylated proteins, it is not associated with lipid rafts. When NBR9 was deleted in the octuple ESCRT-III deletion background, the yeast cells were still viable. However, despite a number of experiments, we do not have evidence at present that Nbr9 is part of an alternative ESCRT-III complex.

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Vps60 initiates alternative ESCRT-III filaments

Cited by 10 publications

References 79 publications

Link between lipid remodeling and ESCRT-III function in multivesicular body formation

Link between lipid remodeling and ESCRT-III function in multivesicular body formation

Exosome-Mediated Antigen Delivery: Unveiling Novel Strategies in Viral Infection Control and Vaccine Design

Identification of ESCRT-III like protein sequences in yeast

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