Evidence map›Paper›PMID 21106837›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010

Kinesin I transports tetramerized Kv3 channels through the axon initial segment via direct binding.

Mingxuan Xu, Yuanzheng Gu, Joshua Barry, Chen Gu

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

43 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Proper localization of the SCA13-linked KNeurobiology of disease · 2026
    Article
  3. AProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
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  19. Fibroblast Growth Factor Homologous Factors: New Roles in Neuronal Health and Disease.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2016
    Review
  20. 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

4 authors at 2 institutions in 2 countries.

Mingxuan XuDepartment of Neuroscience and Center for Molecular Neurobiology, The Ohio State University, Columbus, OH 43210, USA.
Yuanzheng Gu
Joshua Barry
Chen Gu
The Ohio State University · USInstitute of Neurobiology and Molecular Medicine · IT

Funding

Mechanism and function of Kv channel targetingR01NS062720 · NINDS · OHIO STATE UNIVERSITY · PI GU, CHEN · 2009 to 2013
$1.4M
NINDS NIH HHS R01 NS062720
6 · The paper itself

Abstract

Precise targeting of various voltage-gated ion channels to proper membrane domains is crucial for their distinct roles in neuronal excitability and synaptic transmission. How each channel protein is transported within the cytoplasm is poorly understood. Here, we report that KIF5/kinesin I transports Kv3.1 voltage-gated K(+) (Kv) channels through the axon initial segment (AIS) via direct binding. First, we have identified a novel interaction between Kv3.1 and KIF5, confirmed by immunoprecipitation from mouse brain lysates and by pull-down assays with exogenously expressed proteins. The interaction is mediated by a direct binding between the Kv3.1 N-terminal T1 domain and a conserved region in KIF5 tail domains, in which proper T1 tetramerization is crucial. Overexpression of this region of KIF5B markedly reduces axonal levels of Kv3.1bHA. In mature hippocampal neurons, endogenous Kv3.1b and KIF5 colocalize. Suppressing the endogenous KIF5B level by RNA interference significantly reduces the Kv3.1b axonal level. Furthermore, mutating the Zn(2+)-binding site within T1 markedly decreases channel axonal targeting and forward trafficking, likely through disrupting T1 tetramerization and hence eliminating the binding to KIF5 tail. The mutation also alters channel activity. Interestingly, coexpression of the YFP (yellow fluorescent protein)-tagged KIF5B assists dendritic Kv3.1a and even mutants with a faulty axonal targeting motif to penetrate the AIS. Finally, fluorescently tagged Kv3.1 channels colocalize and comove with KIF5B along axons revealed by two-color time-lapse imaging. Our findings suggest that the binding to KIF5 ensures properly assembled and functioning Kv3.1 channels to be transported into axons.

Indexed as

AnimalsAnimals, NewbornAxonsCells, CulturedGene Knockdown TechniquesHEK293 CellsHumansKinesinsMiceProtein BindingProtein TransportRatsShaw Potassium ChannelsKCNC1 protein, humanKIF5B protein, humanKinesinsShaw Potassium Channels

Identifiers

PMID21106837
PMCPMC2996050
OpenAlexW1970604829

What OpenQuestion holds

Textmetadata
LicenceTDM
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.