Evidence map›Paper›PMID 15014437›Full record

ArticleThe EMBO journal2004

An intramolecular interaction between the FHA domain and a coiled coil negatively regulates the kinesin motor KIF1A.

Jae-Ran Lee, Hyewon Shin, Jeonghoon Choi, Jaewon Ko, Seho Kim, Hyun Woo Lee, Karam Kim, Seong-Hwan Rho, Jun Hyuck Lee, Hye-Eun Song and 2 more

Abstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Kinesins inOpen biology · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. A highly conserved 3Science advances · 2021
    Article
  9. Article
  10. Overexpression ofJournal of cardiovascular development and disease · 2020
    Article
  11. Article
  12. Intracellular cargo transport by single-headed kinesin motors.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Coiled-coil 1-mediated fastening of the neck and motor domains for kinesin-3 autoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. The axonal cytoskeleton: from organization to function.Frontiers in molecular neuroscience · 2015
    Review
  18. Article
  19. Review
  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

12 authors.

Jae-Ran LeeNational Creative Research Initiative Center for Synaptogenesis and Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, Korea.
Hyewon Shin
Jeonghoon Choi
Jaewon Ko
Seho Kim
Hyun Woo Lee
Karam Kim
Seong-Hwan Rho
Jun Hyuck Lee
Hye-Eun Song
Soo Hyun Eom
Eunjoon Kim

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Motor proteins not actively involved in transporting cargoes should remain inactive at sites of cargo loading to save energy and remain available for loading. KIF1A/Unc104 is a monomeric kinesin known to dimerize into a processive motor at high protein concentrations. However, the molecular mechanisms underlying monomer stabilization and monomer-to-dimer transition are not well understood. Here, we report an intramolecular interaction in KIF1A between the forkhead-associated (FHA) domain and a coiled-coil domain (CC2) immediately following the FHA domain. Disrupting this interaction by point mutations in the FHA or CC2 domains leads to a dramatic accumulation of KIF1A in the periphery of living cultured neurons and an enhancement of the microtubule (MT) binding and self-multimerization of KIF1A. In addition, point mutations causing rigidity in the predicted flexible hinge disrupt the intramolecular FHA-CC2 interaction and increase MT binding and peripheral accumulation of KIF1A. These results suggest that the intramolecular FHA-CC2 interaction negatively regulates KIF1A activity by inhibiting MT binding and dimerization of KIF1A, and point to a novel role of the FHA domain in the regulation of kinesin motors.

Indexed as

Protein Structure, SecondaryAnimalsCells, CulturedHumansKinesinsModels, MolecularMolecular Motor ProteinsNerve Tissue ProteinsNeuronsPoint MutationProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsKIF1A protein, humanKinesinsMolecular Motor ProteinsNerve Tissue ProteinsRecombinant Fusion Proteins

Identifiers

PMID15014437
PMCPMC391070

What OpenQuestion holds

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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.