Evidence map›Paper›PMID 25175706›Full record

ArticleDevelopmental cell2014

FLA8/KIF3B phosphorylation regulates kinesin-II interaction with IFT-B to control IFT entry and turnaround.

Yinwen Liang, Yunong Pang, Qiong Wu, Zhangfeng Hu, Xue Han, Yisheng Xu, Haiteng Deng, Junmin Pan

Open access · bronzeAbstract read
PubMed Publisher
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 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Appearing and disappearing acts of cilia.Journal of biosciences · 2023
    Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Yinwen LiangMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yunong PangSchool of Life Sciences, Tsinghua University, Beijing 100084, China.
Qiong WuMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Sciences, Tsinghua University, Beijing 100084, China.
Zhangfeng HuMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Sciences, Tsinghua University, Beijing 100084, China.
Xue HanMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Sciences, Tsinghua University, Beijing 100084, China.
Yisheng XuSchool of Life Sciences, Tsinghua University, Beijing 100084, China.
Haiteng DengSchool of Life Sciences, Tsinghua University, Beijing 100084, China.
Junmin PanMOE Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, China; School of Life Sciences, Tsinghua University, Beijing 100084, China. Electronic address: panjunmin@tsinghua.edu.cn.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The assembly and maintenance of cilia depends on intraflagellar transport (IFT). Activated IFT motor kinesin-II enters the cilium with loaded IFT particles comprising IFT-A and IFT-B complexes. At the ciliary tip, kinesin-II becomes inactivated, and IFT particles are released. Moreover, the rate of IFT entry is dynamically regulated during cilium assembly. However, the regulatory mechanism of IFT entry and loading/unloading of IFT particles remains elusive. We show that the kinesin-II motor subunit FLA8, a homolog of KIF3B, is phosphorylated on the conserved S663 by a calcium-dependent kinase in Chlamydomonas. This phosphorylation disrupts the interaction between kinesin-II and IFT-B, inactivates kinesin-II and inhibits IFT entry, and is also required for IFT-B unloading at the ciliary tip. Furthermore, our data suggest that the IFT entry rate is controlled by regulation of the cellular level of phosphorylated FLA8. Therefore, FLA8 phosphorylation acts as a molecular switch to control IFT entry and turnaround.

Indexed as

Gene Expression Regulation, PlantAmino Acid SequenceAnimalsBiological TransportCalcium-Binding ProteinsChlamydomonas reinhardtiiCiliaFlagellaKinesinsMolecular Sequence DataPhosphorylationPlant ProteinsSequence Homology, Amino AcidCalcium-Binding Proteinskinesin-IIKinesinsPlant Proteins

Identifiers

PMID25175706
OpenAlexW1996256749

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.