Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A

Scott, Anna I.; Gaspar, Jason; Stuchell‐Brereton, Melissa D.; Alam, Steven L.; Skalicky, Jack J.; Sundquist, Wesley I.

doi:10.1073/pnas.0502165102

Cited by 161 publications

(185 citation statements)

References 43 publications

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“…Similarly, the ⌬RS but not the ⌬S truncation largely eliminated the interaction of GST-CHMP3 151-end with Vps4A (Fig. 5B), shown previously to bind to the C-terminal domains of CHMP proteins (41). In contrast, neither mutation affected binding to the N-terminal CHMP3 1-150 FLAG fragment (Fig.…”

Section: Accessibility Of the Binding Site For The Acidic Domain Corrmentioning

confidence: 83%

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

Zamborlini

Usami²,

Radoshitzky³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

164

214

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The endosomal sorting complex ESCRT-III, which is formed by the structurally related CHMP proteins, is engaged by HIV-1 to promote viral budding. Here we show that progressive truncations into the C-terminal acidic domains of CHMP proteins trigger an increasingly robust anti-HIV budding activity. Together with biochemical evidence for specific intramolecular interactions between the basic and acidic halves of CHMP3 and CHMP4B, these results suggest that the acidic domains are autoinhibitory. The acidic half of CHMP3 also interacts with the endosome-associated ubiquitin isopeptidase AMSH, and the coexpression of AMSH or its CHMP3-binding domain converts wild-type CHMP3 into a potent inhibitor of HIV-1 release. Point mutations in CHMP3 that prevent binding to AMSH abrogate this effect, suggesting that binding to AMSH relieves the autoinhibition of CHMP3. Collectively, our results indicate that CHMP proteins are regulated through an autoinhibitory switch mechanism that allows tight control of ESCRT-III assembly.AMSH ͉ endosomal sorting machinery ͉ viral budding

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Section: Accessibility Of the Binding Site For The Acidic Domain Corrmentioning

confidence: 83%

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding

Zamborlini

Usami²,

Radoshitzky³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

164

214

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“…Five Ala and/or Gly residues (9,16,28,35) are highly conserved and are involved in the formation of an 'Alanine zipper' between the first two helixes (see Supplementary material Figure S4) [64]. The 'Alanine zipper' also participates in the coiled coil formation as a result of its interaction with aromatic and/or large hydrophobic side-chain residues as Leu, Tyr and Ile.…”

Section: Vps4mentioning

confidence: 99%

“…VPS4 proteins act by binding, catalyzing and energizing the dissociation of the ESCRT-III complex and the release of the membrane-associated SNF7 domain proteins into the cytoplasm for further rounds of sorting [57,63]. In diverse protein-protein interaction studies, it has been shown that VPS4 and its two mammalian homologs VPS4B or SKD1 and VPS4A or SKD2 interact with 'classical' ESCRT-III complex components (SNF7 or CHMP4, VPS2 or CHMP2, VPS20 or CHMP6) and the associated proteins VPS46 or CHMP1, and VTA1 or SBP1 [20][21][22]24,25,[63][64][65][66].The two highly related human VPS4 proteins are 80% identical and share approximately 60% amino acid identity with the yeast VPS4 protein (see Supplementary material Table S5 and Figure S4). Apart from the catalytic AAA-ATPase domain of VPS4 proteins, their substrate specificity is defined by a 70-amino acid N-terminal MIT domain (see Figure S4).…”

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confidence: 99%

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Exploring the ESCRTing machinery in eukaryotes

Winter

Hauser

2006

Trends in Plant Science

170

200

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The profile of protein sorting into multivesicular bodies (MVBs) has risen recently with the identification of three heteromeric complexes known as ESCRT-I,-II,-III (Endosomal Sorting Complex Required for Transport). Genetic analyses in yeast have identified up to 15 soluble class E VPS (vacuolar protein sorting) proteins that have been assigned to the ESCRT machinery and function in cargo recognition and sorting, complex assembly, vesicle formation and dissociation. Despite their functional importance in yeast and mammalian cells, little is known about their presence and function in other organisms including plants. We have made use of the fully sequenced genomes of Arabidopsis thaliana and Oryza sativa, Drosophila melanogaster and Caenorhabditis elegans to explore the identity, structural characteristics and phylogenetic relationships of proteins assigned to the ESCRT machinery.Multivesicular bodies (MVBs) are late endosomal organelles with up to several hundred interluminal vesicles that originate by invagination and budding of the limiting endosomal membrane (Figure 1) [1,2]. MVBs are also prevacuolar compartments involved in the retrograde endocytotic pathway where, upon fusion to vacuoles or lysosomes, the interluminal vesicles are released [3][4][5][6]. In yeast and mammals, MVBs are involved in sorting and degradation of transmembrane surface proteins as transporters (e.g. GAP1, STE6 and PDR5), receptors (e.g. EGFR, GHR, STE3 and STE2), in budding of viruses (e.g. HIV, MuLV and RSV) and in lipid partitioning [7,8]. However, MVBs are also central for sorting vacuolar proteins directly from the late Golgi to the anterograde and biosynthetic pathway ( Figure 1) [9]. Furthermore, MVBs operate in the exocytotic pathway and the secreted interluminal vesicles are known as exosomes (Figure 1) [10][11][12]. Thus, MVBs act as an intermediate station for cargo on the way to degradation, intracellular recycling and secretion ( Figure 1). Although MVBs have been described in plants, little is known about their biogenesis, cargos and function [2,4,[13][14][15][16]. These studies show that plant MVBs are prevacuolar compartments and are labeled by vacuolar sorting receptor (VSR) antibodies such as BP80 [5,17]. Plant MVBs are not only involved in the transport of proteins to lytic but also to protein-storage vacuoles. As plasmalemmasomes in tobacco, MVBs have been implicated in the internalization of arabinogalactanrich plasma membrane proteins that are sequestered within the vacuole [18] Upstream cargo recognition and sorting system of the ESCRT machineryThe entry of membrane proteins into the MVB pathway starts with the binding of monoubiquitinated cargos to the outer endosomal membrane and the recruitment of the ESCRT-I complex. This membrane association is mediated by ubiquitin-binding proteins that contain one or two UIMs or a GAT domain in combination with protein domains that had been implicated in binding to membranes such as the phosphatidylinositol-3 phosphate (PI3P) binding FYVE finger domain (Figure...

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“…A mammalian orthologue of Vps46p, CHMP1B, interacts by yeast two-hybrid analysis with spastin, another mammalian AAA-type ATPase that when mutated is the most common cause of hereditary spastic paraplegia (26). Recently, the microtubule interacting and transport (MIT) domain of VPS4A, the other mammalian Vps4p orthologue, was solved and found to bind CHMP1B in vitro (27).…”

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confidence: 99%