Conformational Changes in the Endosomal Sorting Complex Required for the Transport III Subunit Ist1 Lead to Distinct Modes of ATPase Vps4 Regulation

Tan, Jason Andrew; Davies, Brian A.; Payne, Johanna A.; Benson, Linda M.; Katzmann, David J.

doi:10.1074/jbc.m115.665604

Cited by 21 publications

(30 citation statements)

References 72 publications

(97 reference statements)

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“…These findings differ dramatically from those of several other groups, which previously failed to identify defects in ESCRT-mediated cargo degradation following Ist1 inhibition 23 , 24 , 26 , 43 , 44 . A major distinction between our respective approaches rests with our unique ability to analyze de novo MVE formation during a native period of high endocytic flux, while others have relied largely upon examination of cargo sorting at steady state.…”

Section: Resultscontrasting

confidence: 99%

Ist1 regulates ESCRT-III assembly and function during multivesicular endosome biogenesis in Caenorhabditis elegans embryos

et al. 2017

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Degradation of most integral membrane proteins is directed by the endosomal sorting complex required for transport (ESCRT) machinery, which selectively targets ubiquitin-modified cargoes into intralumenal vesicles (ILVs) within multivesicular endosomes (MVEs). To better understand the mechanisms underlying ESCRT-mediated formation of ILVs, we exploited the rapid, de novo biogenesis of MVEs during the oocyte-to-embryo transition in C. elegans. In contrast to previous models suggesting that ILVs form individually, we demonstrate that they remain tethered to one another subsequent to internalization, arguing that they bud continuously from stable subdomains. In addition, we show that membrane bending and ILV formation are directed specifically by the ESCRT-III complex in vivo in a manner regulated by Ist1, which promotes ESCRT-III assembly and inhibits the incorporation of upstream ESCRT components into ILVs. Our findings underscore essential actions for ESCRT-III in membrane remodeling, cargo selection, and cargo retention, which act repetitively to maximize the rate of ILV formation.

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Section: Resultscontrasting

confidence: 99%

Ist1 regulates ESCRT-III assembly and function during multivesicular endosome biogenesis in Caenorhabditis elegans embryos

et al. 2017

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“…MBP-His-tag was cleaved off using TEV followed by purification on a Superdex 200 26/60 column (buffer: 20mM HEPES pH 8.0). Did2 and Ist1 (gift from David Katzmann lab, Mayo clinic, USA) were expressed and purified as previously described (Tan et al, 2015). In detail, proteins were expressed at 30 C overnight in Rosetta2 (induction 0.5M IPTG), before lysis by sonication (lysis buffer: 50mM Tris pH8.5, 5mM b-Mercaptoethanol, 1% Triton, cOmplete).…”

Section: Methods Detailsmentioning

confidence: 99%

An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission

Pfitzner

Mercier

Jiang

et al. 2020

Cell

144

213

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“…However, unlike in HIV-1 release or MVB formation, recruitment of VPS4A and VPS4B to the division site depends on IST1 ( K d ≈ 1 μM between IST1 and the Vps4 MIT domain; Agromayor et al, 2009 ; Bajorek et al, 2009a ). Since the yeast homolog of CHMP1 (DId2) is responsible for the recruitment of Ist1 to the ESCRT-III complex at the MVB sites (Dimaano et al, 2008 ; Tan et al, 2015 ), it seems that IST1 is recruited to the ESCRT-III filaments at the abscission site by CHMP1. In addition, CHMP1A can bind VPS4 directly through its MIM1 motif with a K d ≈ 4.5 μM, and recruit it to the ESCRT-III filament (Stuchell-Brereton et al, 2007 ).…”

Section: The Escrt and CDV Machineries In Cytokinesismentioning

confidence: 99%

Dividing the Archaeal Way: The Ancient Cdv Cell-Division Machinery

2018

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Cell division in most prokaryotes is mediated by the well-studied fts genes, with FtsZ as the principal player. In many archaeal species, however, division is orchestrated differently. The Crenarchaeota phylum of archaea features the action of the three proteins, CdvABC. This Cdv system is a unique and less-well-studied division mechanism that merits closer inspection. In vivo, the three Cdv proteins form a composite band that contracts concomitantly with the septum formation. Of the three Cdv proteins, CdvA is the first to be recruited to the division site, while CdvB and CdvC are thought to participate in the active part of the Cdv division machinery. Interestingly, CdvB shares homology with a family of proteins from the eukaryotic ESCRT-III complex, and CdvC is a homolog of the eukaryotic Vps4 complex. These two eukaryotic complexes are key factors in the endosomal sorting complex required for transport (ESCRT) pathway, which is responsible for various budding processes in eukaryotic cells and which participates in the final stages of division in Metazoa. There, ESCRT-III forms a contractile machinery that actively cuts the membrane, whereas Vps4, which is an ATPase, is necessary for the turnover of the ESCRT membrane-abscission polymers. In contrast to CdvB and CdvC, CdvA is unique to the archaeal Crenarchaeota and Thaumarchaeota phyla. The Crenarchaeota division mechanism has often been suggested to represent a simplified version of the ESCRT division machinery thus providing a model system to study the evolution and mechanism of cell division in higher organisms. However, there are still many open questions regarding this parallelism and the division mechanism of Crenarchaeota. Here, we review the existing data on the role of the Cdv proteins in the division process of Crenarchaeota as well as concisely review the ESCRT system in eukaryotes. We survey the similarities and differences between the division and abscission mechanisms in the two cases. We suggest that the Cdv system functions differently in archaea than ESCRT does in eukaryotes, and that, unlike the eukaryotic case, the Cdv system's main function may be related to surplus membrane invagination and cell-wall synthesis.

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Conformational Changes in the Endosomal Sorting Complex Required for the Transport III Subunit Ist1 Lead to Distinct Modes of ATPase Vps4 Regulation

Cited by 21 publications

References 72 publications

Ist1 regulates ESCRT-III assembly and function during multivesicular endosome biogenesis in Caenorhabditis elegans embryos

Ist1 regulates ESCRT-III assembly and function during multivesicular endosome biogenesis in Caenorhabditis elegans embryos

An ESCRT-III Polymerization Sequence Drives Membrane Deformation and Fission

Dividing the Archaeal Way: The Ancient Cdv Cell-Division Machinery

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