Evidence map›Paper›PMID 18555885›Full record

ArticleVirology2008

Tsg101 can replace Nedd4 function in ASV Gag release but not membrane targeting.

Gisselle Medina, Andrew Pincetic, Lorna S Ehrlich, Yongjun Zhang, Yi Tang, Jonathan Leis, Carol A Carter

Open access · greenAbstract read
In one paragraph

Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 35 citations in OpenAlex.

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  15. How ubiquitin functions with ESCRTs.Traffic (Copenhagen, Denmark) · 2011
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Gisselle MedinaDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794-5222, USA.
Andrew Pincetic
Lorna S Ehrlich
Yongjun Zhang
Yi Tang
Jonathan Leis
Carol A Carter
Northwestern University · USStony Brook University · USLurie Children's Hospital · US

Funding

VIRAL ONCOLOGYT32CA009176 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 1985 to 2012
$5.2M
Training Program in Viral ReplicationT32AI060523 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LAIMINS, LAIMONIS A. · 2004 to 2013
$1.4M
Cellular Proteins Involved in Trafficking of HIV-1R01AI068463 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI CARTER, CAROL A · 2007 to 2010
$1.4M
Cellular Proteins Involved in Trafficking of HIV-1R56AI068463 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI CARTER, CAROL A · 2006 to 2012
$774k
Mechanism of HIV-1 Concerted DNA IntegrationR56AI054143 · NIAID · NORTHWESTERN UNIVERSITY · PI LEIS, JONATHAN P · 2005 to 2005
$260k
NCI NIH HHS 5T32 CA-09176NCI NIH HHS T32 CA009176NIAID NIH HHS AI054143NIAID NIH HHS AI068463NIAID NIH HHS R01 AI068463NIAID NIH HHS R56 AI054143NIAID NIH HHS R56 AI068463NIAID NIH HHS T32 AI060523
6 · The paper itself

Abstract

The Late (L) domain of the avian sarcoma virus (ASV) Gag protein binds Nedd4 ubiquitin ligase E3 family members and is the determinant of efficient virus release in avian and mammalian cells. We previously demonstrated that Nedd4 and Tsg101 constitutively interact raising the possibility that Nedd4 links ASV Gag to the ESCRT machinery. We now demonstrate that covalently linking Tsg101 to ASV Gag lacking the Nedd4 binding site (Deltap2b-Tsg101) ablates the requirement for Nedd4, but the rescue of budding occurs by use of a different budding mechanism than that used by wild type ASV Gag. The evidence that Tsg101 and Nedd4 direct release by different pathways is: (i) Release of the virus-like particles (VLPs) assembled from Gag in DF-1, an avian cell line, was resistant to dominant-negative interference by a Tsg101 mutant previously shown to inhibit release of both HIV and Mo-MLV. (ii) Release of VLPs from DF-1 cells was resistant to siRNA-mediated depletion of the endogenous pool of Tsg101 in these cells. (iii) VLPs assembled from wild-type ASV Gag exhibited highly efficient release from endosome-like membrane domains enriched in the tetraspanin protein CD63 or a fluorescent analogue of the phospholipid phosphatidylethanolamine. However, the VLPs assembled from the L domain mutant Deltap2b or a chimeric Deltap2b-Tsg101 Gag lacked these domain markers even though the chimeric Gag was released efficiently compared to the Deltap2b mutant. These results suggest that Tsg101 and Nedd4 facilitate Gag release through functionally exchangeable but independent routes and that Tsg101 can replace Nedd4 function in facilitating budding but not directing through the same membranes.

Indexed as

AnimalsAvian Sarcoma VirusesBirdsCell LineCell MembraneChlorocebus aethiopsCOS CellsDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportGene Products, gagGenes, gagMicroscopy, Electron, TransmissionNedd4 Ubiquitin Protein LigasesTranscription FactorsTransfectionTsg101 ProteinDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportGene Products, gagNedd4 Ubiquitin Protein LigasesTranscription FactorsTsg101 ProteinUbiquitin-Protein Ligases

Identifiers

PMID18555885
PMCPMC2528022
OpenAlexW2066604682

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.