Evidence map›Paper›PMID 25443296›Full record

ArticleDevelopmental cell2014

The intraflagellar transport protein IFT27 promotes BBSome exit from cilia through the GTPase ARL6/BBS3.

Gerald M Liew, Fan Ye, Andrew R Nager, J Patrick Murphy, Jaclyn S Lee, Mike Aguiar, David K Breslow, Steven P Gygi, Maxence V Nachury

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed
14.9field-weighted citation impact, top 1% 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

136 citing papers in PubMed, 211 citations in OpenAlex.

  1. Review
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  8. Review
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  12. Article
  13. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  14. Article
  15. Review
  16. Article
  17. Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Gerald M LiewDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
Fan YeDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Andrew R NagerDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
J Patrick MurphyDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Jaclyn S LeeDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Mike AguiarDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
David K BreslowDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Maxence V NachuryDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: nachury@stanford.edu.
Stanford University · USHarvard University · USStanford Medicine · US

Funding

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

Abstract

The sorting of signaling receptors into and out of cilia relies on the BBSome, a complex of Bardet-Biedl syndrome (BBS) proteins, and on the intraflagellar transport (IFT) machinery. GTP loading onto the Arf-like GTPase ARL6/BBS3 drives assembly of a membrane-apposed BBSome coat that promotes cargo entry into cilia, yet how and where ARL6 is activated remains elusive. Here, we show that the Rab-like GTPase IFT27/RABL4, a known component of IFT complex B, promotes the exit of BBSome and associated cargoes from cilia. Unbiased proteomics and biochemical reconstitution assays show that, upon disengagement from the rest of IFT-B, IFT27 directly interacts with the nucleotide-free form of ARL6. Furthermore, IFT27 prevents aggregation of nucleotide-free ARL6 in solution. Thus, we propose that IFT27 separates from IFT-B inside cilia to promote ARL6 activation, BBSome coat assembly, and subsequent ciliary exit, mirroring the process by which BBSome mediates cargo entry into cilia.

Indexed as

ADP-Ribosylation FactorsAnimalsBardet-Biedl SyndromeBiological TransportCells, CulturedCiliaMicerab GTP-Binding ProteinsADP-Ribosylation FactorsArl6 protein, mouseintraflagellar transport 27 protein, mouserab GTP-Binding Proteins

Identifiers

PMID25443296
PMCPMC4255629
OpenAlexW2150269114

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.