Ubiquitin is part of the retrovirus budding machinery

Patnaik, Akash; Chau, Vincent; Wills, John W.

doi:10.1073/pnas.97.24.13069

Cited by 261 publications

(304 citation statements)

References 48 publications

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“…2E; 0 h), indicating MG132 acts quickly on rhTRIM5␣ restriction to restore late RT products. This finding is consistent with MG132 relieving rhTRIM5␣ restriction by rapidly inhibiting proteasome-mediated degradation rather than influencing ubiquitin-mediated protein trafficking, which is disrupted through depleting free ubiquitin pools after hours of proteasome inhibition (32).…”

Section: Mg132 Acts Rapidly To Relieve Exogenous Rhtrim5␣ Restriction Ofsupporting

confidence: 77%

“…An example in which inhibiting proteasome function perturbs protein trafficking is seen during release of retroviral Rous sarcoma virus (RSV) virions, where several hours exposure to proteasome inhibitors blocks virion release (32). However, we find here that the effect of proteasome inhibition to relieve rhTRIM5␣ restriction of HIV-1 late RT products was rapid (Fig.…”

Section: Discussioncontrasting

confidence: 45%

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Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Anderson

Campbell

et al. 2006

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

247

292

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Section: Mg132 Acts Rapidly To Relieve Exogenous Rhtrim5␣ Restriction Ofsupporting

confidence: 77%

Section: Discussioncontrasting

confidence: 45%

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Anderson

Campbell

et al. 2006

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

247

292

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“…E3 ubiquitin ligases of the Nedd4 family were shown to be involved in budding of RSV and MPMV retroviruses (26,48,66). Proteasome inhibitors were found to interfere with the release of HIV-1 (55) and RSV (47), suggesting that depletion of free ubiquitin from the cytoplasm of mammalian cells disrupts retroviral budding and release. The role of ubiquitin in retroviral budding and release remains unclear.…”

mentioning

confidence: 99%

PPPYEPTAP Motif Is the Late Domain of Human T-Cell Leukemia Virus Type 1 Gag and Mediates Its Functional Interaction with Cellular Proteins Nedd4 and Tsg101

Bouamr

Melillo

Wang

et al. 2003

J Virol

122

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The human T-cell leukemia virus type 1 (HTLV-1) Gag polyprotein contains two adjacent proline-rich motifs (sequence PPPYEPTAP) in the C terminus of the matrix domain. Proline-to-alanine mutations were introduced into either or both motifs of HTLV-1 to determine the effect on the release of HTLV-1 virus-like particles from 293T cells. The release of both single mutants was significantly reduced, whereas a double mutation in both motifs abolished the release of the HTLV-1 particles. Two-hybrid and in vitro binding assays showed that the HTLV-1 Gag polyprotein binds both Tsg101 and Nedd4 proteins. The interaction with HTLV-1 Gag required the central WW domain of Nedd4 and the ubiquitin enzyme variant (UEV) domain of Tsg101. We expressed various fragments of Nedd4 and Tsg101 proteins in 293T cells and tested for their ability to interfere with virion release mediated by the HTLV-1 Gag-Pro polyprotein. Fragments consisting of the N-terminal UEV domain of Tsg101 and the central WW and C-terminal Hect domains of Nedd4 protein all caused transdominant inhibition of HTLV-1 particle release. Similarly, inhibition of the proteasome significantly decreased HTLV-1 particle release. Furthermore, the WW domain overexpression caused an early arrest of HTLV-1 particle morphogenesis before the membrane is deformed into the typical half-shell structure. This result suggests that Nedd4 is involved early in budding of HTLV-1.

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“…Many ubiquitin-dependent processes, such as internalization of cell surface proteins (Hicke, 1999), This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04 -05-0425) on January 5, 2005. targeting of membrane proteins to multivesicular bodies (MVBs) (Katzmann et al, 2001;Losko et al, 2001;Reggiori and Pelham, 2001), retrovirus budding (Patnaik et al, 2000;Schubert et al, 2000;Strack et al, 2000), or ER-associated degradation (ERAD) (Hiller et al, 1996;Wiertz et al, 1996) occur at cellular membranes. To identify potential regulators of ubiquitin-dependent processes at membranes, we looked for membrane-associated Dubs among the 16 yeast members of the Ubp family (Kinner and Kö lling, 2003).…”

Section: Introductionmentioning

confidence: 99%

The Deubiquitinating Enzyme Ubp1 Affects Sorting of the ATP-binding Cassette-Transporter Ste6 in the Endocytic Pathway

Schmitz

Kinner

Kölling

2005

MBoC

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Deubiquitinating enzymes (Dubs) are potential regulators of ubiquitination-dependent processes. Here, we focus on a member of the yeast ubiquitin-specific processing protease (Ubp) family, the Ubp1 protein. We could show that Ubp1 exists in two forms: a longer membrane-anchored form (mUbp1) and a shorter soluble form (sUbp1) that seem to be independently expressed from the same gene. The membrane-associated mUbp1 variant could be localized to the endoplasmic reticulum (ER) membrane by sucrose density gradient centrifugation and by immunofluorescence microscopy. Overexpression of the soluble Ubp1 variant stabilizes the ATP-binding cassette-transporter Ste6, which is transported to the lysosome-like vacuole for degradation, and whose transport is regulated by ubiquitination. Ste6 stabilization was not the result of a general increase in deubiquitination activity, because overexpression of Ubp1 had no effect on the degradation of the ER-associated degradation substrate carboxypeptidase Y* and most importantly on Ste6 ubiquitination itself. Also, overexpression of another yeast Dub, Ubp3, had no effect on Ste6 turnover. This suggests that the Ubp1 target is a component of the protein transport machinery. On Ubp1 overexpression, Ste6 accumulates at the cell surface, which is consistent with a role of Ubp1 at the internalization step of endocytosis or with enhanced recycling to the cell surface from an internal compartment. INTRODUCTIONMany cellular proteins are modified by the attachment of the 76-amino acid polypeptide ubiquitin (Hochstrasser, 1996;Hershko and Ciechanover, 1998). The main role of ubiquitination is to target proteins for degradation either directly by acting as a degradation signal that is recognized by the 26S proteasome or indirectly by sorting membrane proteins into the lysosomal/vacuolar degradation pathway (Hicke, 1999). Ubiquitination of substrate proteins, which occurs by a cascade of enzymatic reactions, is reversible. Ubiquitin can again be removed from proteins by deubiquitinating enzymes (Dubs). A large number of Dubs have been identified in various organisms that are either cysteine proteases or metalloproteases (Verma et al., 2002; Yao and Cohen, 2002). The more classical cysteine proteases can again be divided into two groups: the ubiquitin C-terminal hydrolases (Uchs) that preferentially cleave ubiquitin from peptides and small adducts (e.g., Yuh1 in yeast) and the extremely divergent family of ubiquitin-specific processing proteases (Ubps) that cleave ubiquitin from protein substrates (Hochstrasser, 1996). Of the 17 cysteine-protease-type Dubs in yeast 16 belong to the Ubp class.The degree of ubiquitination seems to be mainly regulated at the level of ubiquitin attachment. However, evidence is accumulating that deubiquitination also can be important for the regulation of ubiquitination levels. Evidence has been presented that the deubiquitinating enzyme Fat facets (Faf), which is involved in eye development in Drosophila, acts as a substrate-specific regulator of ubiquitination of the...

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Ubiquitin is part of the retrovirus budding machinery

Cited by 261 publications

References 48 publications

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection

PPPYEPTAP Motif Is the Late Domain of Human T-Cell Leukemia Virus Type 1 Gag and Mediates Its Functional Interaction with Cellular Proteins Nedd4 and Tsg101

The Deubiquitinating Enzyme Ubp1 Affects Sorting of the ATP-binding Cassette-Transporter Ste6 in the Endocytic Pathway

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