Structure and Disassembly of Filaments Formed by the ESCRT-III Subunit Vps24

Ghazi-Tabatabai, Sara; Saksena, Suraj; Short, Judith M.; Pobbati, Ajaybabu V.; Veprintsev, Dmitry B.; Crowther, R. Anthony; Emr, Scott D.; Egelman, Edward H.; Williams, Roger L.

doi:10.1016/j.str.2008.06.010

Cited by 124 publications

(135 citation statements)

References 62 publications

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“…In agreement with these observations, Snf7 (human CHMP4) and Vps24 (human CHMP3) form helical polymers in vitro that can be disassembled by Vps4 in the presence of ATP. A role for Vps4 in the assembly of the ESCRT-III lattice is also suggested by the finding that, in the presence of ADP, Vps4 causes the chimeric filaments to bundle into extensive cables (Ghazi-Tabatabai et al, 2008). Recent work by Scott Emr and colleagues has also provided genetic and biochemical evidence that supports the idea that individual ESCRT-III subunits have specific functions and are recruited in an ordered manner.…”

Section: A Membrane-deformation and -Scission Machinerymentioning

confidence: 94%

No strings attached: the ESCRT machinery in viral budding and cytokinesis

McDonald

Martín-Serrano

2009

Journal of Cell Science

103

104

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Since the initial discovery of the endosomal sorting complex required for transport (ESCRT) pathway, research in this field has exploded. ESCRT proteins are part of the endosomal trafficking system and play a crucial role in the biogenesis of multivesicular bodies by functioning in the formation of vesicles that bud away from the cytoplasm. Subsequently, a surprising role for ESCRT proteins was defined in the budding step of some enveloped retroviruses, including HIV-1. ESCRT proteins are also employed in this outward budding process, which results in the resolution of a membranous tether between the host cell and the budding virus particle. Remarkably, it has recently been described that ESCRT proteins also have a role in the topologically equivalent process of cell division. In the same way that viral particles recruit the ESCRT proteins to the site of viral budding, ESCRT proteins are also recruited to the midbody – the site of release of daughter cell from mother cell during cytokinesis. In this Commentary, we describe recent advances in the understanding of ESCRT proteins and how they act to mediate these diverse processes.

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Section: A Membrane-deformation and -Scission Machinerymentioning

confidence: 94%

No strings attached: the ESCRT machinery in viral budding and cytokinesis

McDonald

Martín-Serrano

2009

Journal of Cell Science

103

104

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“…Vps4p/SKD1 forms an oligomeric complex that disassembles ESCRT-III upon binding. The disassembly of ESCRT-III is essential for the completion of the sorting of cargos to the intraluminal vesicles of MVBs (Babst et al, 1998;Ghazi-Tabatabai et al, 2008;Lata et al, 2008). The regulated assembly and disassembly of ESCRT-III is a prerequisite for proper MVB formation, and in a yeast vps4 mutant, ESCRT-III components aggregate in so-called class E compartments while cargo sorting is blocked (Babst et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

The Arabidopsis Deubiquitinating Enzyme AMSH3 Interacts with ESCRT-III Subunits and Regulates Their Localization

Katsiarimpa¹,

Anzenberger

Schlager

et al. 2011

The Plant Cell

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Ubiquitination and deubiquitination regulate various cellular processes. We have recently shown that the deubiquitinating enzyme Associated Molecule with the SH3 domain of STAM3 (AMSH3) is involved in vacuole biogenesis and intracellular trafficking in Arabidopsis thaliana. However, little is known about the identity of its interaction partners and deubiquitination substrates. Here, we provide evidence that AMSH3 interacts with ESCRT-III subunits VPS2.1 and VPS24.1. The interaction of ESCRT-III subunits with AMSH3 is mediated by the MIM1 domain and depends on the MIT domain of AMSH3. We further show that AMSH3, VPS2.1, and VPS24.1 localize to class E compartments when ESCRT-III disassembly is inhibited by coexpression of inactive Suppressor of K+ transport Defect 1 (SKD1), an AAA-ATPase involved in the disassembly of ESCRT-III. We also provide evidence that AMSH3 and SKD1 compete for binding to VPS2.1. Furthermore, we show that the loss of AMSH3 enzymatic activity leads to the formation of cellular compartments that contain AMSH3, VPS2.1, and VPS24.1. Taken together, our study presents evidence that AMSH3 interacts with classical core ESCRT-III components and thereby provides a molecular framework for the function of AMSH3 in plants.

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“…The propensity to form filaments seems to be a general property of ESCRT-III proteins. So far, homo-or hetero-oligomeric filaments have been described for CHMP1B, CHMP2A, CHMP2B, Vps24 and CHMP3, Snf7 and CHMP4A, CHMP4B, and IST1 (Ghazi-Tabatabai et al 2008;Hanson et al 2008;Lata et al 2008b;Bajorek et al 2009;Bodon et al 2011;Henne et al 2012).…”

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confidence: 99%

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7

et al. 2015

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Endosomal sorting complex required for transport (ESCRT) proteins are involved in a number of cellular processes, such as endosomal protein sorting, HIV budding, cytokinesis, plasma membrane repair, and resealing of the nuclear envelope during mitosis. Here we explored the function of a noncanonical member of the ESCRT-III protein family, the Saccharomyces cerevisiae ortholog of human CHMP7. Very little is known about this protein. In silico analysis predicted that Chm7 (yeast ORF YJL049w) is a fusion of an ESCRT-II and ESCRT-III-like domain, which would suggest a role in endosomal protein sorting. However, our data argue against a role of Chm7 in endosomal protein sorting. The turnover of the endocytic cargo protein Ste6 and the vacuolar protein sorting of carboxypeptidase S (CPS) were not affected by CHM7 deletion, and Chm7 also responded very differently to a loss in Vps4 function compared to a canonical ESCRT-III protein. Our data indicate that the Chm7 function could be connected to the endoplasmic reticulum (ER). In line with a function at the ER, we observed a strong negative genetic interaction between the deletion of a gene function (APQ12) implicated in nuclear pore complex assembly and messenger RNA (mRNA) export and the CHM7 deletion. The patterns of genetic interactions between the APQ12 deletion and deletions of ESCRT-III genes, two-hybrid interactions, and the specific localization of mCherry fusion proteins are consistent with the notion that Chm7 performs a novel function at the ER as part of an alternative ESCRT-III complex.

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Structure and Disassembly of Filaments Formed by the ESCRT-III Subunit Vps24

Cited by 124 publications

References 62 publications

No strings attached: the ESCRT machinery in viral budding and cytokinesis

No strings attached: the ESCRT machinery in viral budding and cytokinesis

The Arabidopsis Deubiquitinating Enzyme AMSH3 Interacts with ESCRT-III Subunits and Regulates Their Localization

Evidence for a Nonendosomal Function of the Saccharomyces cerevisiae ESCRT-III-Like Protein Chm7

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