Evidence map›Paper›PMID 27633000›Full record

ArticleJournal of cell science2016

A ternary complex comprising transportin1, Rab8 and the ciliary targeting signal directs proteins to ciliary membranes.

Viswanadh Madugula, Lei Lu

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.8field-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

36 citing papers in PubMed, 52 citations in OpenAlex.

  1. Tension TRAAKer: a chemigenetic fluorescent membrane tension reporter.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  10. Development of a highly sensitive platform for protein-protein interaction detection and regulation of T cell function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Early Endosomes Act as Local Exocytosis Hubs to Repair Endothelial Membrane Damage.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Comparison of Ciliary Targeting of Two Rhodopsin-Like GPCRs: Role of C-Terminal Localization Sequences in Relation to Cilium Type.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  19. Article
  20. The Transition Zone Protein AHI1 Regulates Neuronal Ciliary Trafficking of MCHR1 and Its Downstream Signaling Pathway.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    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

2 authors at 1 institution in 1 country.

Viswanadh MadugulaSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore.
Lei LuSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore lulei@ntu.edu.sg.ORCID 0000-0002-8192-1471
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sensory functions of cilia are dependent on the enrichment of cilium-resident proteins. Although it is known that ciliary targeting signals (CTSs) specifically target ciliary proteins to cilia, it is still unclear how CTSs facilitate the entry and retention of cilium-resident proteins at the molecular level. We found that non-ciliary membrane reporters can passively diffuse into cilia through the lateral transport pathway, and the translocation of membrane reporters through the ciliary diffusion barrier is facilitated by importin binding motifs and domains. Screening known CTSs of ciliary membrane residents uncovered that fibrocystin, photoreceptor retinol dehydrogenase, rhodopsin and retinitis pigmentosa 2 interact with transportin1 (TNPO1) through previously identified CTSs. We further discovered that a new ternary complex, comprising TNPO1, Rab8 and a CTS, can assemble or disassemble under the guanine nucleotide exchange activity of Rab8. Our study suggests a new mechanism in which the TNPO1-Rab8-CTS complex mediates selective entry into and retention of cargos within cilia.

Indexed as

Signal TransductionAlcohol OxidoreductasesAmino Acid Motifsbeta KaryopherinsCell MembraneCiliaDiffusionGene Knockdown TechniquesGenes, ReporterGuanine NucleotidesHEK293 CellsHeLa CellsHumansIntracellular MembranesMultiprotein ComplexesProtein BindingAlcohol Oxidoreductasesbeta KaryopherinsGuanine NucleotidesMultiprotein ComplexesPKHD1 protein, humanRAB8A protein, humanrab GTP-Binding Proteinsran GTP-Binding ProteinReceptors, Cell SurfaceRhodopsinTNPO1 protein, humanCiliaCiliary targeting signalRab8Transportin1

Identifiers

PMID27633000
PMCPMC5087665
OpenAlexW2530353274

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.