Evidence map›Paper›PMID 16339079›Full record

ArticleMolecular biology of the cell2006

Conventional kinesin mediates microtubule-microtubule interactions in vivo.

Anne Straube, Gerd Hause, Gero Fink, Gero Steinberg

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

44 citing papers in PubMed, 82 citations in OpenAlex.

  1. Kinesin-Induced Buckling Reveals the Limits of Microtubule Self-Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Review
  4. Dynein-Powered Cell Locomotion Guides Metastasis of Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  5. Article
  6. Article
  7. Microtubules in Pancreatic β Cells: Convoluted Roadways Toward Precision.Frontiers in cell and developmental biology · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. A small-molecule activator of kinesin-1 drives remodeling of the microtubule network.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  16. Review
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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 3 institutions in 2 countries.

Anne StraubeMax-Planck-Institut für terrestrische Mikrobiologie, D-35043 Marburg, Germany.
Gerd Hause
Gero Fink
Gero Steinberg
Max Planck Society · DEMartin Luther University Halle-Wittenberg · DEWellcome Centre for Cell Biology · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conventional kinesin is a ubiquitous organelle transporter that moves cargo toward the plus-ends of microtubules. In addition, several in vitro studies indicated a role of conventional kinesin in cross-bridging and sliding microtubules, but in vivo evidence for such a role is missing. In this study, we show that conventional kinesin mediates microtubule-microtubule interactions in the model fungus Ustilago maydis. Live cell imaging and ultrastructural analysis of various mutants in Kin1 revealed that this kinesin-1 motor is required for efficient microtubule bundling and participates in microtubule bending in vivo. High levels of Kin1 led to increased microtubule bending, whereas a rigor-mutation in the motor head suppressed all microtubule motility and promoted strong microtubule bundling, indicating that kinesin can form cross-bridges between microtubules in living cells. This effect required a conserved region in the C terminus of Kin1, which was shown to bind microtubules in vitro. In addition, a fusion protein of yellow fluorescent protein and the Kin1tail localized to microtubule bundles, further supporting the idea that a conserved microtubule binding activity in the tail of conventional kinesins mediates microtubule-microtubule interactions in vivo.

Indexed as

Amino Acid SequenceBinding SitesBiological TransportConserved SequenceFungal ProteinsKinesinsMicrotubulesMolecular Sequence DataMutationProtein BindingRecombinant Fusion ProteinsSequence AlignmentSequence DeletionUstilagoFungal ProteinsKIN1 protein, Ustilago maydisKinesinsRecombinant Fusion Proteins

Identifiers

PMID16339079
PMCPMC1356599
OpenAlexW2073377028

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.