The Human Endosomal Sorting Complex Required for Transport (ESCRT-I) and Its Role in HIV-1 Budding

Stuchell, Melissa; Garrus, Jennifer; Müller, Bárbara; Stray, Kirsten M.; Ghaffarian, Sanaz; McKinnon, Rena; Kräusslich, Hans Georg; Morham, Scott G.; Sundquist, Wesley I.

doi:10.1074/jbc.m405226200

Cited by 149 publications

(168 citation statements)

References 73 publications

(78 reference statements)

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“…9,32) Interaction of HD-PTP and UBAP1 might allow the association of HD-PTP with TSG101 and VPS37A in the ESCRT-I complex. Since both TSG101 and VPS37A contain UEV domains, 7) we speculate that they have the potential to bind PT/SAP motifs (720-PTAP and 861-PSAP) in HD-PTP and to stabilize a binary complex of HD-PTP and ESCRT-I. Indeed, we have found that HD-PTP associates with TSG101 in a Ca 2þ -independent manner, suggesting that ALG-2 is dispensable as an adaptor.…”

Section: Ei(c) Ei(d) Ei(a) Ei(b) Ei(c) Ei(d) Ei(a) Ei(b)mentioning

confidence: 80%

“…Therefore, similarly to the interaction between ALIX and ALG-2, VPS37C might interact with ALG-2 via VPS37C PPYP motifs. VPS37B has a PTAP motif (a potential binding site to the TSG101 UEV domain), 7,9,27) which overlaps with an alternative ALG-2-binding motif (185-PTAPLPYP, potential ALG-2-binding site underlined). It would be interesting to determine whether ALG-2 influences the assembly of ESCRT-I isocomplex B.…”

Section: A Model Of Escrt-i/alix/alg-2 Ternary Complex Formationmentioning

confidence: 99%

“…The four VPS37 isoforms have a common mod(r) domain, important for interaction with TSG101. 7,8) While VPS37A has an N-terminal UEV domain, VPS37B, VPS37C, and VPS37D have C-terminal extensions rich in prolines. These extensions are called Pro-rich regions (PRRs), and they vary in length (69-193 amino acids).…”

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confidence: 99%

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VPS37 Isoforms Differentially Modulate the Ternary Complex Formation of ALIX, ALG-2, and ESCRT-I

Okumura

Katsuyama

Shibata

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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Section: Ei(c) Ei(d) Ei(a) Ei(b) Ei(c) Ei(d) Ei(a) Ei(b)mentioning

confidence: 80%

Section: A Model Of Escrt-i/alix/alg-2 Ternary Complex Formationmentioning

confidence: 99%

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VPS37 Isoforms Differentially Modulate the Ternary Complex Formation of ALIX, ALG-2, and ESCRT-I

Okumura

Katsuyama

Shibata

et al. 2013

Bioscience, Biotechnology, and Biochemistry

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“…Therefore, VPS23 does not function as an ubiquitin conjugating enzyme and yet it is still able to bind ubiquitinated proteins. Via its C-terminal coiled coil structure, the human VPS23 homolog TSG101 interacts with VPS27, VPS28 [40] and VPS37 [41]. In rice and Arabidopsis, one and two putative VPS23 homologs are present, respectively (see Supplementary material Table S2 and Figure S2A).…”

Section: Escrt-imentioning

confidence: 99%

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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“…This membrane fission event is facilitated by virus-encoded late assembly (L) domains, which in HIV-1 are found in the Cterminal p6 domain of Gag, the viral protein that drives particle assembly (1). The primary L domain of HIV-1 maps to a highly conserved PTAP motif (2,3), which binds to Tsg101, a component of the endosomal sorting complex required for transport-I (ESCRT-I) (4)(5)(6)(7)(8)(9). Additionally, the HIV-1 p6 domain contains a second L domain that binds AIP1/ALIX, which in turn interacts with both ESCRT-I and the later-acting ESCRT-III sorting complex (10)(11)(12)(13).…”

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confidence: 99%

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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The Human Endosomal Sorting Complex Required for Transport (ESCRT-I) and Its Role in HIV-1 Budding

Cited by 149 publications

References 73 publications

VPS37 Isoforms Differentially Modulate the Ternary Complex Formation of ALIX, ALG-2, and ESCRT-I

VPS37 Isoforms Differentially Modulate the Ternary Complex Formation of ALIX, ALG-2, and ESCRT-I

Exploring the ESCRTing machinery in eukaryotes

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

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