Evidence map›Paper›PMID 24916158›Full record

ArticleeLife2014

Reconstitution of dynein transport to the microtubule plus end by kinesin.

Anthony J Roberts, Brian S Goodman, Samara L Reck-Peterson

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

62 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
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  9. CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024
    Article
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  16. Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Article
  19. Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022
    Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Anthony J RobertsDepartment of Cell Biology, Harvard Medical School, Boston, United States Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom anthony_roberts@hms.harvard.edu.
Brian S GoodmanDepartment of Cell Biology, Harvard Medical School, Boston, United States.
Samara L Reck-PetersonDepartment of Cell Biology, Harvard Medical School, Boston, United States reck-peterson@hms.harvard.edu.
Harvard University · USUniversity of Leeds · GB

Funding

Regulation of Cytoplasmic DyneinR01GM107214 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LESCHZINER, ANDRES · 2014 to 2021
$3.1M
Dissecting dynein motor function using DNA nanotechnologyR01GM100947 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI RECK-PETERSON, SAMARA L · 2013 to 2016
$1.2M
NIGMS NIH HHS 01GM100947NIGMS NIH HHS R01 GM100947NIGMS NIH HHS R01 GM107214
6 · The paper itself

Abstract

Cytoplasmic dynein powers intracellular movement of cargo toward the microtubule minus end. The first step in a variety of dynein transport events is the targeting of dynein to the dynamic microtubule plus end, but the molecular mechanism underlying this spatial regulation is not understood. Here, we reconstitute dynein plus-end transport using purified proteins from S. cerevisiae and dissect the mechanism using single-molecule microscopy. We find that two proteins-homologs of Lis1 and Clip170-are sufficient to couple dynein to Kip2, a plus-end-directed kinesin. Dynein is transported to the plus end by Kip2, but is not a passive passenger, resisting its own plus-end-directed motion. Two microtubule-associated proteins, homologs of Clip170 and EB1, act as processivity factors for Kip2, helping it overcome dynein's intrinsic minus-end-directed motility. This reveals how a minimal system of proteins transports a molecular motor to the start of its track.DOI: http://dx.doi.org/10.7554/eLife.02641.001.

Indexed as

DyneinsKinesinsMicrotubule-Associated ProteinsMicrotubulesModels, BiologicalMolecular Motor ProteinsMultiprotein ComplexesProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDyneinsKinesinsKIP2 protein, S cerevisiaeMicrotubule-Associated ProteinsMolecular Motor ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinscytoskeletonDNA origamidyneinkinesinmicrotubule

Identifiers

PMID24916158
PMCPMC4046564
OpenAlexW1994619959

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.