Evidence map›Paper›PMID 14581525›Full record

ArticleJournal of virology2003

PPPYVEPTAP 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 [corrected].

Fadila Bouamr, Jessica A Melillo, Margaret Q Wang, Kunio Nagashima, Martha de Los Santos, Alan Rein, Stephen P Goff

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

78 citing papers in PubMed, 131 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Viruses go modular.The Journal of biological chemistry · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 4 institutions in 1 country.

Fadila BouamrDepartment of Biochemistry and Molecular Biophysics, College of Physicians and Surgeons, Columbia University, New York, New York, USA.
Jessica A Melillo
Margaret Q Wang
Kunio Nagashima
Martha de Los Santos
Alan Rein
Stephen P Goff
Columbia University · USHoward Hughes Medical Institute · USNational Cancer Institute · USScience Applications International Corporation (United States) · US

Funding

Retrovirus Assembly and MaturationZ01BC010511 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI REIN, ALAN · 2003 to 2008
$2.1M
NCI NIH HHS N01 CO012400PHS HHS N01-C0-12400
6 · The paper itself

Abstract

The human T-cell leukemia virus type 1 (HTLV-1) Gag polyprotein contains two adjacent proline-rich motifs (sequence PPPYVEPTAP) in the C terminus of the matrix domain [corrected]. 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.

Indexed as

Amino Acid MotifsAmino Acid SequenceCell LineCysteine EndopeptidasesDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportGene Products, gagHumansHuman T-lymphotropic virus 1Molecular Sequence DataMultienzyme ComplexesNedd4 Ubiquitin Protein LigasesProteasome Endopeptidase ComplexTranscription FactorsTsg101 ProteinUbiquitin-Protein LigasesCysteine EndopeptidasesDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportGene Products, gagMultienzyme ComplexesNedd4 protein, humanNedd4 Ubiquitin Protein LigasesProteasome Endopeptidase ComplexTranscription FactorsTsg101 ProteinUbiquitin-Protein Ligases

Identifiers

PMID14581525
PMCPMC253756
OpenAlexW2130138387

What OpenQuestion holds

Textmetadata
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.