Evidence map›Paper›PMID 25501369›Full record

ArticleMolecular biology of the cell2015

Kinesin-13 regulates the quantity and quality of tubulin inside cilia.

Krishna Kumar Vasudevan, Yu-Yang Jiang, Karl F Lechtreck, Yasuharu Kushida, Lea M Alford, Winfield S Sale, Todd Hennessey, Jacek Gaertig

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Anterior-posterior pattern formation in ciliates.The Journal of eukaryotic microbiology · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Mechanism of ciliary disassembly.Cellular and molecular life sciences : CMLS · 2016
    Review
  17. Article
  18. Article
  19. Review
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

8 authors.

Krishna Kumar VasudevanDepartment of Cellular Biology, University of Georgia, Athens, GA 30602;
Yu-Yang JiangDepartment of Cellular Biology, University of Georgia, Athens, GA 30602;
Karl F LechtreckDepartment of Cellular Biology, University of Georgia, Athens, GA 30602;
Yasuharu KushidaDepartment of Structural Biosciences, University of Tsukuba, Tsukuba, Ibaraki 305-8577, Japan;
Lea M AlfordDepartment of Cell Biology, Emory University, Atlanta, GA 30303;
Winfield S SaleDepartment of Cell Biology, Emory University, Atlanta, GA 30303;
Todd HennesseyDepartment of Biological Sciences, State University of New York at Buffalo, Buffalo, NY 14260.
Jacek GaertigDepartment of Cellular Biology, University of Georgia, Athens, GA 30602; jgaertig@uga.edu.

Funding

FUNCTIONAL SUBSTRUCTURE OF FLAGELLAR DYNEINR01GM051173 · NIGMS · EMORY UNIVERSITY · PI SALE, WINFIELD S · 1994 to 2020
$3.6M
Regulation of protein transport in ciliaR01GM110413 · NIGMS · UNIVERSITY OF GEORGIA · PI LECHTRECK, KARL · 2014 to 2022
$2.7M
Functional Adaptation of Microtubules by AcetylationR01GM089912 · NIGMS · UNIVERSITY OF GEORGIA · PI GAERTIG, JACEK · 2010 to 2013
$1.1M
NIGMS NIH HHS R01 GM051173NIGMS NIH HHS R01GM0571173NIGMS NIH HHS R01 GM089912NIGMS NIH HHS R01GM089912NIGMS NIH HHS R01 GM110413NIGMS NIH HHS R01GM110413
6 · The paper itself

Abstract

Kinesin-13, an end depolymerizer of cytoplasmic and spindle microtubules, also affects the length of cilia. However, in different models, depletion of kinesin-13 either lengthens or shortens cilia, and therefore the exact function of kinesin-13 in cilia remains unclear. We generated null mutations of all kinesin-13 paralogues in the ciliate Tetrahymena. One of the paralogues, Kin13Ap, localizes to the nuclei and is essential for nuclear divisions. The remaining two paralogues, Kin13Bp and Kin13Cp, localize to the cell body and inside assembling cilia. Loss of both Kin13Bp and Kin13Cp resulted in slow cell multiplication and motility, overgrowth of cell body microtubules, shortening of cilia, and synthetic lethality with either paclitaxel or a deletion of MEC-17/ATAT1, the α-tubulin acetyltransferase. The mutant cilia assembled slowly and contained abnormal tubulin, characterized by altered posttranslational modifications and hypersensitivity to paclitaxel. The mutant cilia beat slowly and axonemes showed reduced velocity of microtubule sliding. Thus kinesin-13 positively regulates the axoneme length, influences the properties of ciliary tubulin, and likely indirectly, through its effects on the axonemal microtubules, affects the ciliary dynein-dependent motility.

Indexed as

AcetyltransferasesAxonemeCiliaGene Knockout TechniquesKinesinsMorphogenesisMutationPaclitaxelProtein Processing, Post-TranslationalTetrahymena thermophilaTubulinAcetyltransferasesalpha-tubulin acetylaseKinesinsPaclitaxelTubulin

Identifiers

PMID25501369
PMCPMC4310739

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Registered trials

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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.