Evidence map›Paper›PMID 20071331›Full record

ArticleThe Journal of biological chemistry2010

Microtubule-associated protein-like binding of the kinesin-1 tail to microtubules.

Mark A Seeger, Sarah E Rice

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

58 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Roles of molecular motors in insulin-secreting beta cells.Current opinion in cell biology · 2025
    Review
  5. Article
  6. Imaging microtubule dynamics: A new frontier in biomarker development for neurodegenerative diseases.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Review
  7. Article
  8. Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025
    Review
  9. Article
  10. Review
  11. Dynein-Powered Cell Locomotion Guides Metastasis of Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Acentrosomal spindle assembly and maintenance inMolecular biology of the cell · 2022
    Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Mark A SeegerDepartment of Cell and Molecular Biology, Northwestern University, Chicago, Illinois 60611, USA.
Sarah E Rice
Northwestern University · US

Funding

Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
The Mechanism of Kinesin Self-RegulationR01GM072656 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI RICE, SARAH E. · 2005 to 2014
$2.5M
NIGMS NIH HHS 5T32 GM008382NIGMS NIH HHS GM072656NIGMS NIH HHS R01 GM072656NIGMS NIH HHS T32 GM008382
6 · The paper itself

Abstract

The kinesin-1 molecular motor contains an ATP-dependent microtubule-binding site in its N-terminal head domain and an ATP-independent microtubule-binding site in its C-terminal tail domain. Here we demonstrate that a kinesin-1 tail fragment associates with microtubules with submicromolar affinity. Binding is largely electrostatic in nature, and is facilitated by a region of basic amino acids in the tail and the acidic E-hook at the C terminus of tubulin. The tail binds to a site on tubulin that is independent of the head domain-binding site but overlaps with the binding site of the microtubule-associated protein Tau. Surprisingly, the kinesin tail domain stimulates microtubule assembly and stability in a manner similar to Tau. The biological function of this strong kinesin tail-microtubule interaction remains to be seen, but it is likely to play an important role in kinesin regulation due to the close proximity of the microtubule-binding region to the conserved regulatory and cargo-binding domains of the tail.

Indexed as

Allosteric RegulationCircular DichroismElectrochemistryFluorescence PolarizationHumansKinesinsMicroscopy, ElectronMicrotubule-Associated ProteinsMicrotubulesMutagenesisProtein BindingProtein Structure, Tertiarytau ProteinsKIF5B protein, humanKinesinsMAPT protein, humanMicrotubule-Associated Proteinstau Proteins

Identifiers

PMID20071331
PMCPMC2832967
OpenAlexW2081739769

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.