Evidence map›Paper›PMID 38547289›Full record

ArticleScience (New York, N.Y.)2024

Molecular mechanism of dynein-dynactin complex assembly by LIS1.

Kashish Singh, Clinton K Lau, Giulia Manigrasso, José B Gama, Reto Gassmann, Andrew P Carter

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
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  11. Review
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  14. Dynein upsizes under load.Nature cell biology · 2026
    Article
  15. Article
  16. Review
  17. Article
  18. Review
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  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.

Kashish Singh *MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID 0000-0002-9891-8148
Clinton K Lau *MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID 0000-0003-1083-2989
Giulia ManigrassoMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
José B GamaInstituto de Investigação e Inovação em Saúde (i3S)/Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, 4200-135 Porto, Portugal.ORCID 0000-0002-7011-1502
Reto GassmannInstituto de Investigação e Inovação em Saúde (i3S)/Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, 4200-135 Porto, Portugal.ORCID 0000-0002-0360-2977
Andrew P CarterMRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.ORCID 0000-0001-7292-5430

Funding

Medical Research Council MC_UP_A025_1011Wellcome Trust 210711Wellcome Trust 210711/Z/18/Z
6 · The paper itself

Abstract

Cytoplasmic dynein is a microtubule motor vital for cellular organization and division. It functions as a ~4-megadalton complex containing its cofactor dynactin and a cargo-specific coiled-coil adaptor. However, how dynein and dynactin recognize diverse adaptors, how they interact with each other during complex formation, and the role of critical regulators such as lissencephaly-1 (LIS1) protein (LIS1) remain unclear. In this study, we determined the cryo-electron microscopy structure of dynein-dynactin on microtubules with LIS1 and the lysosomal adaptor JIP3. This structure reveals the molecular basis of interactions occurring during dynein activation. We show how JIP3 activates dynein despite its atypical architecture. Unexpectedly, LIS1 binds dynactin's p150 subunit, tethering it along the length of dynein. Our data suggest that LIS1 and p150 constrain dynein-dynactin to ensure efficient complex formation.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAdaptor Proteins, Signal TransducingDynactin ComplexDyneinsMicrotubule-Associated ProteinsNerve Tissue ProteinsCryoelectron MicroscopyHeLa CellsHumansMicrotubulesProtein BindingProtein Interaction MappingWD40 Repeats1-Alkyl-2-acetylglycerophosphocholine EsteraseAdaptor Proteins, Signal TransducingDynactin ComplexDyneinsMAPK8IP3 protein, humanMicrotubule-Associated ProteinsNerve Tissue ProteinsPAFAH1B1 protein, human

Identifiers

PMID38547289
PMCPMC7615804

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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.