Evidence map›Paper›PMID 26884162›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

The light chains of kinesin-1 are autoinhibited.

Yan Y Yip, Stefano Pernigo, Anneri Sanger, Mengjia Xu, Maddy Parsons, Roberto A Steiner, Mark P Dodding

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Involvement of kinesins in skeletal dysplasia: a review.American journal of physiology. Cell physiology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Selective motor activation in organelle transport along axons.Nature reviews. Molecular cell biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  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

7 authors.

Yan Y YipRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom.
Stefano PernigoRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom.
Anneri SangerRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom.
Mengjia XuRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom.
Maddy ParsonsRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom.
Roberto A SteinerRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom mark.dodding@kcl.ac.uk roberto.steiner@kcl.ac.uk.
Mark P DoddingRandall Division of Cell and Molecular Biophysics, King's College London, London SE1 1UL, United Kingdom mark.dodding@kcl.ac.uk roberto.steiner@kcl.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/L006774/1Wellcome Trust
6 · The paper itself

Abstract

The light chains (KLCs) of the microtubule motor kinesin-1 bind cargoes and regulate its activity. Through their tetratricopeptide repeat domain (KLC(TPR)), they can recognize short linear peptide motifs found in many cargo proteins characterized by a central tryptophan flanked by aspartic/glutamic acid residues (W-acidic). Using a fluorescence resonance energy transfer biosensor in combination with X-ray crystallographic, biochemical, and biophysical approaches, we describe how an intramolecular interaction between the KLC2(TPR) domain and a conserved peptide motif within an unstructured region of the molecule, partly occludes the W-acidic binding site on the TPR domain. Cargo binding displaces this interaction, effecting a global conformational change in KLCs resulting in a more extended conformation. Thus, like the motor-bearing kinesin heavy chains, KLCs exist in a dynamic conformational state that is regulated by self-interaction and cargo binding. We propose a model by which, via this molecular switch, W-acidic cargo binding regulates the activity of the holoenzyme.

Indexed as

Amino Acid SequenceHumansKinesinsMolecular Sequence DataSequence Homology, Amino AcidKIF5B protein, humanKinesinscytoskeletonkinesinKLCmicrotubule motorTPR domain

Identifiers

PMID26884162
PMCPMC4780624

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.