Evidence map›Paper›PMID 25402481›Full record

ArticleNature structural & molecular biology2014

Structural basis for membrane targeting of the BBSome by ARL6.

André Mourão, Andrew R Nager, Maxence V Nachury, Esben Lorentzen

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.7field-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

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. A molten globule ensemble primes Arf1-GDP for the nucleotide switch.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Unraveling the intricate cargo-BBSome coupling mechanism at the ciliary tip.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Appearing and disappearing acts of cilia.Journal of biosciences · 2023
    Review
  11. Bardet-Biedl Syndrome: Current Perspectives and Clinical Outlook.Therapeutics and clinical risk management · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Journal of medical genetics · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 2 countries.

André MourãoDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried, Germany.
Andrew R NagerDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California, USA.
Maxence V NachuryDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California, USA.ORCID 0000000349181562
Esben LorentzenDepartment of Structural Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried, Germany.
Max Planck Society · DEStanford University · US

Funding

Quality control of the primary cilium proteomeR01GM089933 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Maxence V Nachury · 2010 to 2026
$5.8M
European Research Council 310343NIGMS NIH HHS R01 GM089933NIGMS NIH HHS R01GM089933
6 · The paper itself

Abstract

The BBSome is a coat-like ciliary trafficking complex composed of proteins mutated in Bardet-Biedl syndrome (BBS). A critical step in BBSome-mediated sorting is recruitment of the BBSome to membranes by the GTP-bound Arf-like GTPase ARL6. We have determined crystal structures of Chlamydomonas reinhardtii ARL6-GDP, ARL6-GTP and the ARL6-GTP-BBS1 complex. The structures demonstrate how ARL6-GTP binds the BBS1 β-propeller at blades 1 and 7 and explain why GTP- but not GDP-bound ARL6 can recruit the BBSome to membranes. Single point mutations in the ARL6-GTP-BBS1 interface abolish the interaction of ARL6 with the BBSome and prevent the import of BBSomes into cilia. Furthermore, we show that BBS1 with the M390R mutation, responsible for 30% of all reported BBS disease cases, fails to interact with ARL6-GTP, thus providing a molecular rationale for patient pathologies.

Indexed as

ADP-Ribosylation FactorsBardet-Biedl SyndromeChlamydomonas reinhardtiiCiliaCrystallography, X-RayGuanosine TriphosphateHumansMicrotubule-Associated ProteinsModels, MolecularPlant ProteinsPoint MutationProtein ConformationProtein TransportRecombinant ProteinsADP-Ribosylation FactorsARL6 protein, humanBbs1 protein, humanGuanosine TriphosphateMicrotubule-Associated ProteinsPlant ProteinsRecombinant Proteins

Identifiers

PMID25402481
PMCPMC4255524
OpenAlexW2047722888

What OpenQuestion holds

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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.