Evidence map›Paper›PMID 23201121›Full record

ArticleDevelopmental cell2012

ALIX is a Lys63-specific polyubiquitin binding protein that functions in retrovirus budding.

Dara P Dowlatshahi, Virginie Sandrin, Sandro Vivona, Thomas A Shaler, Stephen E Kaiser, Francesco Melandri, Wesley I Sundquist, Ron R Kopito

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

50 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. 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
  3. Research progress on the mechanism of exosome-mediated virus infection.Frontiers in cellular and infection microbiology · 2024
    Review
  4. Exosomes: Methods for Isolation and Characterization in Biological Samples.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  5. Review
  6. Article
  7. Bro1 family proteins harmonize cargo sorting with vesicle formation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Emerging Mechanisms of Endocytosis inLife (Basel, Switzerland) · 2021
    Review
  14. Occludin, caveolin-1, and Alix form a multi-protein complex and regulate HIV-1 infection of brain pericytes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. ALIX increases protein content and protective function of iPSC-derived exosomes.Journal of molecular medicine (Berlin, Germany) · 2019
    Article
  20. Review
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

8 authors at 4 institutions in 1 country.

Dara P DowlatshahiDepartment of Biology, Stanford University, Stanford, CA 94305, USA.
Virginie Sandrin
Sandro Vivona
Thomas A Shaler
Stephen E Kaiser
Francesco Melandri
Wesley I Sundquist
Ron R Kopito
Stanford University · USUniversity of Utah · USBioChem Technology (United States) · USSRI International · US

Funding

The Ubiquitin Proteasome System in Quality ControlR01GM074874 · NIGMS · STANFORD UNIVERSITY · PI KOPITO, RON R · 2006 to 2022
$8.0M
Biochemistry of HIV-1 Membrane Recognition and BuddingR01AI051174 · NIAID · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2002 to 2016
$7.2M
NIAID NIH HHS R01 AI051174NIGMS NIH HHS R01 GM074874
6 · The paper itself

Abstract

The diversity of ubiquitin (Ub)-dependent signaling is attributed to the ability of this small protein to form different types of covalently linked polyUb chains and to the existence of Ub binding proteins that interpret this molecular syntax. We used affinity capture/mass spectrometry to identify ALIX, a component of the ESCRT pathway, as a Ub binding protein. We report that the V domain of ALIX binds directly and selectively to K63-linked polyUb chains, exhibiting a strong preference for chains composed of more than three Ub. Sequence analysis identified two potential Ub binding sites on a single α-helical surface within the coiled-coil region of the V domain. Mutation of these putative Ub binding sites inhibited polyUb binding to the isolated V domain in vitro and impaired budding of lentiviruses. These data reveal an important role for K63 polyUb binding by ALIX in retroviral release.

Indexed as

Virus ReleaseBinding SitesCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsCell LineEndosomal Sorting Complexes Required for TransportHEK293 CellsHIV-1HumansInfectious Anemia Virus, EquineProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryRetroviridaeSignal TransductionCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsEndosomal Sorting Complexes Required for TransportPDCD6IP protein, humanUbiquitin

Identifiers

PMID23201121
PMCPMC3522770
OpenAlexW2037692580

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.