Evidence map›Paper›PMID 32084403›Full record

ArticleCurrent biology : CB2020

Microtubule Minus-End Binding Protein CAMSAP2 and Kinesin-14 Motor KIFC3 Control Dendritic Microtubule Organization.

Yujie Cao, Joanna Lipka, Riccardo Stucchi, Mithila Burute, Xingxiu Pan, Sybren Portegies, Roderick Tas, Jelmer Willems, Lena Will, Harold MacGillavry and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Current biology : CB, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  7. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
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  19. KIFC1 Regulates the Trajectory of Neuronal Migration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  20. Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

14 authors at 1 institution in 1 country.

Yujie CaoCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Joanna LipkaCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Riccardo StucchiCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands; Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 Utrecht, the Netherlands.
Mithila BuruteCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Xingxiu PanCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Sybren PortegiesCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Roderick TasCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Jelmer WillemsCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Lena WillCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Harold MacGillavryCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Maarten AltelaarBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, 3584 Utrecht, the Netherlands.
Lukas C KapiteinCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Martin HarterinkCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands.
Casper C HoogenraadCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, 3584 Utrecht, the Netherlands; Department of Neuroscience, Genentech, Inc., South San Francisco, CA 94080, USA. Electronic address: c.hoogenraad@uu.nl.
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuronal dendrites are characterized by an anti-parallel microtubule organization. The mixed oriented microtubules promote dendrite development and facilitate polarized cargo trafficking; however, the mechanism that regulates dendritic microtubule organization is still unclear. Here, we found that the kinesin-14 motor KIFC3 is important for organizing dendritic microtubules and to control dendrite development. The kinesin-14 motor proteins (Drosophila melanogaster Ncd, Saccharomyces cerevisiae Kar3, Saccharomyces pombe Pkl1, and Xenopus laevis XCTK2) are characterized by a C-terminal motor domain and are well described to organize the spindle microtubule during mitosis using an additional microtubule binding site in the N terminus [1-4]. In mammals, there are three kinesin-14 members, KIFC1, KIFC2, and KIFC3. It was recently shown that KIFC1 is important for organizing axonal microtubules in neurons, a process that depends on the two microtubule-interacting domains [5]. Unlike KIFC1, KIFC2 and KIFC3 lack the N-terminal microtubule binding domain and only have one microtubule-interacting domain, the motor domain [6, 7]. Thus, in order to regulate microtubule-microtubule crosslinking or sliding, KIFC2 and KIFC3 need to interact with additional microtubule binding proteins to connect two microtubules. We found that KIFC3 has a dendrite-specific distribution and interacts with microtubule minus-end binding protein CAMSAP2. Depletion of KIFC3 or CAMSAP2 results in increased microtubule dynamics during dendritic development. We propose a model in which CAMSAP2 anchors KIFC3 at microtubule minus ends and immobilizes microtubule arrays in dendrites.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsHEK293 CellsHumansKinesinsMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein TransportCAMSAP2 protein, humanKifc3 protein, humanKinesinsMicrotubule-Associated ProteinsCAMSAP2dendriteKIFC3kinesinMAPmicrotubule minus-endmicrotubule organizationmotor proteinneuron

Identifiers

PMID32084403
PMCPMC7063570
OpenAlexW3008666202

What OpenQuestion holds

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LicenceCC BY
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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.