Evidence map›Paper›PMID 37919547›Full record

ArticleNature chemical biology2024

Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules.

Emre Kusakci, Zaw Min Htet, Yuanchang Zhao, John P Gillies, Samara L Reck-Peterson, Ahmet Yildiz

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025
    Article
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 3 institutions in 1 country.

Emre KusakciGraduate Group in Biophysics, University of California Berkeley, Berkeley, CA, USA.
Zaw Min HtetDepartment of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, USA.
Yuanchang ZhaoDepartment of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0003-1458-5321
John P GilliesDepartment of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA, USA.
Samara L Reck-PetersonDepartment of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA, USA.
Ahmet YildizGraduate Group in Biophysics, University of California Berkeley, Berkeley, CA, USA. yildiz@berkeley.edu.ORCID http://orcid.org/0000-0003-4792-174X
University of California, Berkeley · USHoward Hughes Medical Institute · USUniversity of California San Diego · US

Funding

The Mechanism and Regulation of the Dynein Transport MachineryR35GM136414 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Ahmet Yildiz · 2020 to 2026
$5.1M
Understanding the Mechanism and Regulation of the Human Cytoplasmic Dynein ComplexR01GM094522 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI YILDIZ, AHMET · 2011 to 2019
$2.8M
Mechanisms of microtubule-based transportR35GM141825 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI RECK-PETERSON, SAMARA L · 2021 to 2025
$1.9M
NIGMS NIH HHS R01 GM094522NIGMS NIH HHS R35 GM136414NIGMS NIH HHS R35 GM141825
6 · The paper itself

Abstract

Lis1 is a key cofactor for the assembly of active cytoplasmic dynein complexes that transport cargo along microtubules. Lis1 binds to the AAA+ ring and stalk of dynein and slows dynein motility, but the underlying mechanism has remained unclear. Using single-molecule imaging and optical trapping assays, we investigated how Lis1 binding affects the motility and force generation of yeast dynein in vitro. We showed that Lis1 slows motility by binding to the AAA+ ring of dynein, not by serving as a roadblock or tethering dynein to microtubules. Lis1 binding also does not affect force generation, but it induces prolonged stalls and reduces the asymmetry in the force-induced detachment of dynein from microtubules. The mutagenesis of the Lis1-binding sites on the dynein stalk partially recovers this asymmetry but does not restore dynein velocity. These results suggest that Lis1-stalk interaction slows the detachment of dynein from microtubules by interfering with the stalk sliding mechanism.

Indexed as

Cytoplasmic DyneinsMicrotubule-Associated ProteinsDyneinsMicrotubulesSaccharomyces cerevisiaeCytoplasmic DyneinsDyneinsMicrotubule-Associated Proteins

Identifiers

PMID37919547
PMCPMC11164236
OpenAlexW4388217294

What OpenQuestion holds

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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.