Evidence map›Paper›PMID 34321209›Full record

ArticleScience advances2021

Molecular mechanism for kinesin-1 direct membrane recognition.

Zuriñe Antón, Johannes F Weijman, Christopher Williams, Edmund R R Moody, Judith Mantell, Yan Y Yip, Jessica A Cross, Tom A Williams, Roberto A Steiner, Matthew P Crump and 2 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

11 citing papers in PubMed, 17 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
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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

12 authors at 3 institutions in 2 countries.

Zuriñe AntónSchool of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK.ORCID 0000-0002-0175-8548
Johannes F WeijmanSchool of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK.ORCID 0000-0002-2082-5777
Christopher WilliamsSchool of Chemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TS, UK.ORCID 0000-0001-5806-9842
Edmund R R MoodySchool of Biological Sciences, Faculty of Life Sciences, University of Bristol, Life Sciences Building, Tyndall Avenue, Bristol BS8 1TQ, UK.ORCID 0000-0002-8785-5006
Judith MantellSchool of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK.ORCID 0000-0002-9061-8933
Yan Y YipRandall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King's College London, London, UK.
Jessica A CrossSchool of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK.ORCID 0000-0001-7725-3821
Tom A WilliamsSchool of Biological Sciences, Faculty of Life Sciences, University of Bristol, Life Sciences Building, Tyndall Avenue, Bristol BS8 1TQ, UK.ORCID 0000-0003-1072-0223
Roberto A SteinerRandall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King's College London, London, UK.ORCID 0000-0001-7084-9745
Matthew P CrumpSchool of Chemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TS, UK.ORCID 0000-0002-7868-5818
Derek N WoolfsonSchool of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK.ORCID 0000-0002-0394-3202
Mark P DoddingSchool of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK. mark.dodding@bristol.ac.uk.ORCID 0000-0001-8091-6534
University of Bristol · GBKing's College London · GBUniversity of Padua · IT

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

The cargo-binding capabilities of cytoskeletal motor proteins have expanded during evolution through both gene duplication and alternative splicing. For the light chains of the kinesin-1 family of microtubule motors, this has resulted in an array of carboxyl-terminal domain sequences of unknown molecular function. Here, combining phylogenetic analyses with biophysical, biochemical, and cell biology approaches, we identify a highly conserved membrane-induced curvature-sensitive amphipathic helix within this region of a subset of long kinesin light-chain paralogs and splice isoforms. This helix mediates the direct binding of kinesin-1 to lipid membranes. Membrane binding requires specific anionic phospholipids, and it contributes to kinesin-1-dependent lysosome positioning, a canonical activity that, until now, has been attributed exclusively the recognition of organelle-associated cargo adaptor proteins. This leads us to propose a protein-lipid coincidence detection framework for kinesin-1-mediated organelle transport.

Indexed as

KinesinsMicrotubulesAdaptor Proteins, Signal TransducingLipidsPhylogenyAdaptor Proteins, Signal TransducingKinesinsLipids

Identifiers

PMID34321209
PMCPMC8318374
OpenAlexW3175718360

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.