Evidence map›Paper›PMID 28077622›Full record

ArticleMolecular biology of the cell2017

Ciliary entry of KIF17 is dependent on its binding to the IFT-B complex via IFT46-IFT56 as well as on its nuclear localization signal.

Teruki Funabashi, Yohei Katoh, Saki Michisaka, Masaya Terada, Maho Sugawa, Kazuhisa Nakayama

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
8.6field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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  5. Article
  6. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  7. Article
  8. Review
  9. Review
  10. Appearing and disappearing acts of cilia.Journal of biosciences · 2023
    Review
  11. Review
  12. The physiological cargo adaptor of kinesin-2 functions as an evolutionary conserved lockpick.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Intraflagellar Transport Proteins as Regulators of Primary Cilia Length.Frontiers in cell and developmental biology · 2021
    Review
  17. Article
  18. Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020
    Review
  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

6 authors at 1 institution in 2 countries.

Teruki FunabashiGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
Yohei KatohGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
Saki MichisakaGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
Masaya TeradaGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
Maho SugawaGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.
Kazuhisa NakayamaGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan kazunaka@pharm.kyoto-u.ac.jp.
Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cilia function as cellular antennae to sense and transduce extracellular signals. A number of proteins are specifically localized in cilia. Anterograde and retrograde ciliary protein trafficking are mediated by the IFT-B and IFT-A complexes in concert with kinesin-2 and dynein-2 motors, respectively. However, the role of KIF17, a homodimeric kinesin-2 protein, in protein trafficking has not been fully understood in vertebrate cilia. In this study, we demonstrated, by using the visible immunoprecipitation assay, that KIF17 interacts with the IFT46-IFT56 dimer in the IFT-B complex through its C-terminal sequence located immediately upstream of the nuclear localization signal (NLS). We then showed that KIF17 reaches the ciliary tip independently of its motor domain and requires IFT-B binding for its entry into cilia rather than for its intraciliary trafficking. We further showed that KIF17 ciliary entry depends not only on its binding to IFT-B but also on its NLS, to which importin α proteins bind. Taking the results together, we conclude that in mammalian cells, KIF17 is dispensable for ciliogenesis and IFT-B trafficking but requires IFT-B, as well as its NLS, for its ciliary entry across the permeability barrier located at the ciliary base.

Indexed as

AxonemeCarrier ProteinsCell LineCiliaDyneinsFlagellaGene Knockout TechniquesHumansKinesinsMolecular Motor ProteinsNuclear Localization SignalsProtein TransportRetinal Pigment EpitheliumCarrier ProteinsDyneinsKIF17 protein, humanKIF2A protein, humanKinesinsMolecular Motor ProteinsNuclear Localization Signals

Identifiers

PMID28077622
PMCPMC5328621
OpenAlexW2579282727

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.