Evidence map›Paper›PMID 28302907›Full record

ArticleJournal of cell science2017

SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain.

Anneri Sanger, Yan Y Yip, Thomas S Randall, Stefano Pernigo, Roberto A Steiner, Mark P Dodding

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Selective targeting of kinesin on lipid droplets in the liver reduces plasma lipids.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Specific kinesin and dynein molecules participate in the unconventional protein secretion of transmembrane proteins.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024
    Article
  8. Involvement of kinesins in skeletal dysplasia: a review.American journal of physiology. Cell physiology · 2024
    Review
  9. Article
  10. Selective motor activation in organelle transport along axons.Nature reviews. Molecular cell biology · 2022
    Review
  11. Article
  12. Article
  13. Endomembrane remodeling and dynamics inMicrobial cell (Graz, Austria) · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

6 authors at 1 institution in 1 country.

Anneri SangerRandall Division of Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Yan Y YipRandall Division of Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Thomas S RandallRandall Division of Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Stefano PernigoRandall Division of Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Roberto A SteinerRandall Division of Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.
Mark P DoddingRandall Division of Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK mark.dodding@kcl.ac.uk.ORCID 0000-0001-8091-6534
King's College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L006774/1Wellcome TrustWellcome Trust 097316/Z/11/Z
6 · The paper itself

Abstract

The molecular interplay between cargo recognition and regulation of the activity of the kinesin-1 microtubule motor is not well understood. Using the lysosome adaptor SKIP (also known as PLEKHM2) as model cargo, we show that the kinesin heavy chains (KHCs), in addition to the kinesin light chains (KLCs), can recognize tryptophan-acidic-binding determinants on the cargo when presented in the context of an extended KHC-interacting domain. Mutational separation of KHC and KLC binding shows that both interactions are important for SKIP-kinesin-1 interaction

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCalcium-Binding ProteinsHeLa CellsHumansKinesinsLysosomesMutationProtein BindingProtein DomainsRatsAdaptor Proteins, Signal TransducingCalcium-Binding ProteinsKIF5B protein, humanKIF5C protein, ratKinesinsKinesin-1Lysosome positioningMicrotubule transportSKIP

Identifiers

PMID28302907
PMCPMC5450233
OpenAlexW2596517952

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.