Evidence map›Paper›PMID 17146056›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding.

Alessia Zamborlini, Yoshiko Usami, Sheli R Radoshitzky, Elena Popova, Giorgio Palu, Heinrich Göttlinger

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

112 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. Article
  3. Three-dimensional architecture of ESCRT-III flat spirals on the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. The endolysosomal pathway and ALS/FTD.Trends in neurosciences · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. The ESCRTs - converging on mechanism.Journal of cell science · 2020
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. ESCRT-dependent cargo sorting at multivesicular endosomes.Seminars in cell & developmental biology · 2018
    Review
  19. The Conserved ESCRT-III Machinery Participates in the Phagocytosis ofFrontiers in cellular and infection microbiology · 2018
    Article
  20. Article

52 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

6 authors at 3 institutions in 2 countries.

Alessia ZamborliniProgram in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Yoshiko Usami
Sheli R Radoshitzky
Elena Popova
Giorgio Palu
Heinrich Göttlinger
University of Massachusetts Chan Medical School · USDana-Farber Cancer Institute · USUniversity of Padua · IT

Funding

Molecular Biology of HIV-Gag ProteinsR37AI029873 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GOTTLINGER, HEINRICH · 2004 to 2013
$5.1M
MOLECULAR BIOLOGY OF HIV GAG PROTEINSR01AI029873 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GOTTLINGER, HEINRICH · 1990 to 2018
$3.7M
Role of HIV-1 p6gag and Ubiquitin in Virus ReleaseR01AI050466 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GOTTLINGER, HEINRICH · 2001 to 2004
$1.2M
NIAID NIH HHS AI 29873NIAID NIH HHS AI 50466NIAID NIH HHS R01 AI029873NIAID NIH HHS R01 AI050466NIAID NIH HHS R37 AI029873
6 · The paper itself

Abstract

The endosomal sorting complex ESCRT-III, which is formed by the structurally related CHMP proteins, is engaged by HIV-1 to promote viral budding. Here we show that progressive truncations into the C-terminal acidic domains of CHMP proteins trigger an increasingly robust anti-HIV budding activity. Together with biochemical evidence for specific intramolecular interactions between the basic and acidic halves of CHMP3 and CHMP4B, these results suggest that the acidic domains are autoinhibitory. The acidic half of CHMP3 also interacts with the endosome-associated ubiquitin isopeptidase AMSH, and the coexpression of AMSH or its CHMP3-binding domain converts wild-type CHMP3 into a potent inhibitor of HIV-1 release. Point mutations in CHMP3 that prevent binding to AMSH abrogate this effect, suggesting that binding to AMSH relieves the autoinhibition of CHMP3. Collectively, our results indicate that CHMP proteins are regulated through an autoinhibitory switch mechanism that allows tight control of ESCRT-III assembly.

Indexed as

AcidsAntiviral AgentsBinding SitesCell LineEndosomal Sorting Complexes Required for TransportHIV-1HumansMutationNerve Tissue ProteinsProtein BindingAcidsAntiviral AgentsCHMP3 protein, humanEndosomal Sorting Complexes Required for TransportNerve Tissue Proteins

Identifiers

PMID17146056
PMCPMC1748189
OpenAlexW2106199678

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.