Evidence map›Paper›PMID 23027949›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

In vitro reconstitution of the ordered assembly of the endosomal sorting complex required for transport at membrane-bound HIV-1 Gag clusters.

Lars-Anders Carlson, James H Hurley

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

69 citing papers in PubMed, 92 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  6. Review
  7. The "basics" of HIV-1 assembly.PLoS pathogens · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. In vitro reconstitution of calcium-dependent recruitment of the human ESCRT machinery in lysosomal membrane repair.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Review
  15. Nuclear Egress.Current issues in molecular biology · 2021
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

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

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

2 authors at 1 institution in 1 country.

Lars-Anders CarlsonLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
James H Hurley
National Institutes of Health · US

Funding

Structural Studies of Alix and ESCRT Complexes in HIV-1 BuddingZIADK036125 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HURLEY, JAMES · 2009 to 2013
$2.6M
Intramural NIH HHS
6 · The paper itself

Abstract

Most membrane-enveloped viruses depend on host proteins of the endosomal sorting complex required for transport (ESCRT) machinery for their release. HIV-1 is the prototypic ESCRT-dependent virus. The direct interactions between HIV-1 and the early ESCRT factors TSG101 and ALIX have been mapped in detail. However, the full pathway of ESCRT recruitment to HIV-1 budding sites, which culminates with the assembly of the late-acting CHMP4, CHMP3, CHMP2, and CHMP1 subunits, is less completely understood. Here, we report the biochemical reconstitution of ESCRT recruitment to viral assembly sites, using purified proteins and giant unilamellar vesicles. The myristylated full-length Gag protein of HIV-1 was purified to monodispersity. Myr-Gag forms clusters on giant unilamellar vesicle membranes containing the plasma membrane lipid PI(4,5)P(2). These Gag clusters package a fluorescent oligonucleotide, and recruit early ESCRT complexes ESCRT-I or ALIX with the appropriate dependence on the Gag PTAP and LYP(X)(n)L motifs. ALIX directly recruits the key ESCRT-III subunit CHMP4. ESCRT-I can only recruit CHMP4 when ESCRT-II and CHMP6 are present as intermediary factors. Downstream of CHMP4, CHMP3 and CHMP2 assemble synergistically, with the presence of both subunits required for efficient recruitment. The very late-acting factor CHMP1 is not recruited unless the pathway is completed through CHMP3 and CHMP2. These findings define the minimal sets of components needed to complete ESCRT assembly at HIV-1 budding sites, and provide a starting point for in vitro structural and biophysical dissection of the system.

Indexed as

Endosomal Sorting Complexes Required for Transportgag Gene Products, Human Immunodeficiency VirusHIV-1Image Processing, Computer-AssistedMicroscopy, ConfocalOligonucleotidesProtein SubunitsVirus AssemblyEndosomal Sorting Complexes Required for Transportgag Gene Products, Human Immunodeficiency VirusOligonucleotidesp18 gag protein, Human immunodeficiency virus 1Protein Subunits

Identifiers

PMID23027949
PMCPMC3479502
OpenAlexW2007311551

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.