Evidence map›Paper›PMID 28886386›Full record

ArticleCell2017

Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein.

Morgan E DeSantis, Michael A Cianfrocco, Zaw Min Htet, Phuoc Tien Tran, Samara L Reck-Peterson, Andres E Leschziner

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.9field-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

57 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
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  7. Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025
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  8. Review
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  15. Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023
    Article
  16. New pieces for the Lis1-dynein puzzle.Nature structural & molecular biology · 2023
    Article
  17. Article
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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

6 authors at 2 institutions in 1 country.

Morgan E DeSantisDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Michael A CianfroccoDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Zaw Min HtetDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA; Biophysics Graduate Program, Harvard University, Boston, MA 92105, USA.
Phuoc Tien TranDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Samara L Reck-PetersonDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA; Section of Cellular and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093 USA. Electronic address: sreckpeterson@ucsd.edu.
Andres E LeschzinerDepartment of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093, USA; Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: aleschziner@ucsd.edu.
University of California, San Diego · USHarvard University · US

Funding

Regulation of Cytoplasmic DyneinR01GM107214 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LESCHZINER, ANDRES · 2014 to 2021
$3.1M
NIGMS NIH HHS R01 GM107214
6 · The paper itself

Abstract

Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, a conserved regulator of dynein, binds to its motor domain and induces a tight microtubule-binding state in dynein. The work we present here-a combination of biochemistry, single-molecule assays, and cryoelectron microscopy-led to the surprising discovery that Lis1 has two opposing modes of regulating dynein, being capable of inducing both low and high affinity for the microtubule. We show that these opposing modes depend on the stoichiometry of Lis1 binding to dynein and that this stoichiometry is regulated by the nucleotide state of dynein's AAA3 domain. The low-affinity state requires Lis1 to also bind to dynein at a novel conserved site, mutation of which disrupts Lis1's function in vivo. We propose a new model for the regulation of dynein by Lis1.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAdenosine TriphosphateAmino Acid SequenceCryoelectron MicroscopyDyneinsHumansMicrotubule-Associated ProteinsModels, MolecularMolecular Motor ProteinsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Alignment1-Alkyl-2-acetylglycerophosphocholine EsteraseAdenosine TriphosphateDyneinsKIP2 protein, S cerevisiaeMicrotubule-Associated ProteinsMolecular Motor ProteinsPAFAH1B1 protein, humanPAFAH1B1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsAAA+cryoelectron microscopycryo-EMdyneinLis1lissencephalymicrotubulemolecular motorsingle-moleculetransport

Identifiers

PMID28886386
PMCPMC5625841
OpenAlexW2721965856

What OpenQuestion holds

Textmetadata
LicenceTDM
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.