Evidence map›Paper›PMID 23361315›Full record

ArticleThe EMBO journal2013

Structure-based in silico identification of ubiquitin-binding domains provides insights into the ALIX-V:ubiquitin complex and retrovirus budding.

Tal Keren-Kaplan, Ilan Attali, Michael Estrin, Lillian S Kuo, Efrat Farkash, Moran Jerabek-Willemsen, Noa Blutraich, Shay Artzi, Aviyah Peri, Eric O Freed and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Exosomes: Methods for Isolation and Characterization in Biological Samples.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
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  9. Bro1 family proteins harmonize cargo sorting with vesicle formation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. ALIX increases protein content and protective function of iPSC-derived exosomes.Journal of molecular medicine (Berlin, Germany) · 2019
    Article
  18. Article
  19. Review
  20. HIV-1 gag recruits PACSIN2 to promote virus spreading.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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

12 authors at 4 institutions in 3 countries.

Tal Keren-KaplanDepartment of Biochemistry and Molecular Biology and Rich Institute for Structural Biology, George S. Wise Faculty of Life Sciences Tel Aviv University, Tel Aviv, Israel.
Ilan Attali
Michael Estrin
Lillian S Kuo
Efrat Farkash
Moran Jerabek-Willemsen
Noa Blutraich
Shay Artzi
Aviyah Peri
Eric O Freed
Haim J Wolfson
Gali Prag
Tel Aviv University · ILFrederick National Laboratory for Cancer Research · USNanoTemper Technologies (Germany) · DENational Cancer Institute · US

Funding

Retrovirus Budding and Endosomal SortingZIABC010776 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FREED, ERIC · 2009 to 2015
$3.5M
Intramural NIH HHS
6 · The paper itself

Abstract

The ubiquitylation signal promotes trafficking of endogenous and retroviral transmembrane proteins. The signal is decoded by a large set of ubiquitin (Ub) receptors that tether Ub-binding domains (UBDs) to the trafficking machinery. We developed a structure-based procedure to scan the protein data bank for hidden UBDs. The screen retrieved many of the known UBDs. Intriguingly, new potential UBDs were identified, including the ALIX-V domain. Pull-down, cross-linking and E3-independent ubiquitylation assays biochemically corroborated the in silico findings. Guided by the output model, we designed mutations at the postulated ALIX-V:Ub interface. Biophysical affinity measurements using microscale-thermophoresis of wild-type and mutant proteins revealed some of the interacting residues of the complex. ALIX-V binds mono-Ub with a K(d) of 119 μM. We show that ALIX-V oligomerizes with a Hill coefficient of 5.4 and IC(50) of 27.6 μM and that mono-Ub induces ALIX-V oligomerization. Moreover, we show that ALIX-V preferentially binds K63 di-Ub compared with mono-Ub and K48 di-Ub. Finally, an in vivo functionality assay demonstrates the significance of ALIX-V:Ub interaction in equine infectious anaemia virus budding. These results not only validate the new procedure, but also demonstrate that ALIX-V directly interacts with Ub in vivo and that this interaction can influence retroviral budding.

Indexed as

Multienzyme ComplexesMutationUbiquitin-Protein LigasesAnimalsHumansInfectious Anemia Virus, EquineMiceModels, BiologicalProtein Structure, TertiaryVirus ReleaseMultienzyme ComplexesUbiquitin-Protein Ligases

Identifiers

PMID23361315
PMCPMC3579145
OpenAlexW2095898148

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.