2004
DOI: 10.1128/jvi.78.24.13943-13953.2004
|View full text |Cite
|
Sign up to set email alerts
|

Role of Nedd4 and Ubiquitination of Rous Sarcoma Virus Gag in Budding of Virus-Like Particles from Cells

Abstract: When the Nedd4-binding site (L domain) was deleted, ubiquitinated Gag was not detected. Interestingly, the release of Gag with ubiquitin covalently linked to the C terminus (Gag-Ub) was still blocked by LDI-1 WW. To understand the mechanism of this inhibition, we examined cells expressing Gag and LDI-1 WW by electron microscopy. In the presence of LDI-1 WW, VLPs were found in electron-dense inclusion bodies in the cytoplasm of transfected cells. In contrast, when cells that coexpressed Gag-Ub and LDI-1 WW were… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

2
76
0

Year Published

2006
2006
2024
2024

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 60 publications
(78 citation statements)
references
References 26 publications
2
76
0
Order By: Relevance
“…PPxY or PxY motifs are common binding sites for WW domains in Rsp5 (Chang et al, 2000) and in the Nedd4 family of HECT domain E3 Ub ligases in mammalian cells, which are homologues of Rsp5 (Ingham et al, 2004). Notably, several types of enveloped viruses encode structural proteins containing PPxY motifs that bind Nedd4 and bud from infected cells by a process that is both topologically equivalent to MVB vesicle budding and is dependent on the functions of class E Vps proteins (Harty et al, 2000;Bouamr et al, 2003;Gottwein et al, 2003;Martin-Serrano et al, 2004;Vana et al, 2004;SeguraMorales et al, 2005; reviewed in Morita and Sundquist, 2004). Like Rsp5, Nedd4 proteins function in ubiquitination of cargoes sorted into the MVB pathway (Staub et al, 1997;Marchese et al, 2003), but whether ubiquitination of viral proteins by Nedd4 is directly required for packaging of viral particles is unclear (Morita and Sundquist, 2004).…”
Section: Discussionmentioning
confidence: 99%
“…PPxY or PxY motifs are common binding sites for WW domains in Rsp5 (Chang et al, 2000) and in the Nedd4 family of HECT domain E3 Ub ligases in mammalian cells, which are homologues of Rsp5 (Ingham et al, 2004). Notably, several types of enveloped viruses encode structural proteins containing PPxY motifs that bind Nedd4 and bud from infected cells by a process that is both topologically equivalent to MVB vesicle budding and is dependent on the functions of class E Vps proteins (Harty et al, 2000;Bouamr et al, 2003;Gottwein et al, 2003;Martin-Serrano et al, 2004;Vana et al, 2004;SeguraMorales et al, 2005; reviewed in Morita and Sundquist, 2004). Like Rsp5, Nedd4 proteins function in ubiquitination of cargoes sorted into the MVB pathway (Staub et al, 1997;Marchese et al, 2003), but whether ubiquitination of viral proteins by Nedd4 is directly required for packaging of viral particles is unclear (Morita and Sundquist, 2004).…”
Section: Discussionmentioning
confidence: 99%
“…We chose to further examine Nedd4, because it is the prototypical member of the Nedd4 family of ubiquitin ligases and has been shown to be a cofactor for PPXY motif (PY motif)-dependent viral budding (6,23,36,60,71,80). Unfortunately, other candidate Nedd4 family proteins could not be tested, either because antibodies were not available or because they were not detected in Vero cell lysates with commercially available antibodies.…”
Section: Several Nedd4 Family Ubiquitin Ligases Interact With Ul56mentioning
confidence: 99%
“…Nedd4 regulates viral budding of Ebola virus (23,80), human T-cell leukemia virus type 1 (6,60), and Rous sarcoma virus (36,71). In addition to these viruses, many enveloped RNA and DNA viruses exploit the multivesicular body (MVB) machinery for budding, such as retroviruses (21,56,74,79,81), rhabdoviruses (12), other filoviruses (38), arenaviruses (54,64), paramyxoviruses (59,62), hepatitis B virus (44,76), HSV (8,13), and probably orthomyxoviruses and human herpes virus type 6 (47).…”
mentioning
confidence: 99%
See 1 more Smart Citation
“…The YPXL and LXXLF motifs bind to AIP-1/Alix, which acts downstream of Tsg101 and appears to bridge ESCRT-I and ESCRT-III complexes (42,66,73). The third motif, PPXY, plays a role in recruiting host ubiquitin ligases (7,8,17,34,38,40,54,70,73,79,80). Although it is clear that the cellular ubiquitination machinery is important for the budding of many animal viruses, current knowledge about the exact targets of the ubiquitin ligases and their interactions with other components of the budding machinery is still very limited (7,41,47,49,53).…”
mentioning
confidence: 99%