Evidence map›Paper›PMID 32341548›Full record

ArticleNature cell biology2020

Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity.

Matthew G Marzo, Jacqueline M Griswold, Steven M Markus

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
7.8field-weighted citation impact, top 1% 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

58 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  7. The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025
    Article
  8. Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025
    Article
  9. Article
  10. Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025
    Article
  11. Article
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  14. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
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  19. NUDC is critical for rod photoreceptor function, maintenance, and survival.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Matthew G MarzoDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.
Jacqueline M GriswoldDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.
Steven M MarkusDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA. steven.markus@colostate.edu.ORCID http://orcid.org/0000-0002-3098-0236
Colorado State University · US

Funding

Regulation of Spindle PositioningR01GM118492 · NIGMS · COLORADO STATE UNIVERSITY · PI MARKUS, STEVEN M · 2016 to 2020
$1.7M
NIGMS NIH HHS R01 GM118492
6 · The paper itself

Abstract

Dynein is a microtubule motor that transports many different cargos in various cell types and contexts. How dynein is regulated to perform these activities with spatial and temporal precision remains unclear. Human dynein is regulated by autoinhibition, whereby intermolecular contacts limit motor activity. Whether this mechanism is conserved throughout evolution, whether it can be affected by extrinsic factors, and its role in regulating dynein function remain unclear. Here, we use a combination of negative stain electron microscopy, single-molecule assays, genetic, and cell biological techniques to show that autoinhibition is conserved in budding yeast, and plays a key role in coordinating in vivo dynein function. Moreover, we find that the Lissencephaly-related protein, LIS1 (Pac1 in yeast), plays an important role in regulating dynein autoinhibition. Our studies demonstrate that, rather than inhibiting dynein motility, Pac1/LIS1 promotes dynein activity by stabilizing the uninhibited conformation, which ensures appropriate dynein localization and activity in cells.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseDyneinsEndoribonucleasesMicrotubule-Associated ProteinsMicrotubulesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins1-Alkyl-2-acetylglycerophosphocholine EsteraseDyneinsEndoribonucleasesMicrotubule-Associated ProteinsPAC1 protein, S cerevisiaePAFAH1B1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID32341548
PMCPMC7413593
OpenAlexW3020176739

What OpenQuestion holds

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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.