Evidence map›Paper›PMID 22939623›Full record

ArticleCell2012

Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor.

Julie Huang, Anthony J Roberts, Andres E Leschziner, Samara L Reck-Peterson

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 154 papers.

0numbers the graph read from it
0cells of the map it votes in
154citing papers in PubMed
12.7field-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

154 citing papers in PubMed, 246 citations in OpenAlex.

  1. Article
  2. Review
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  10. Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025
    Article
  15. Article
  16. Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Julie HuangDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Anthony J Roberts
Andres E Leschziner
Samara L Reck-Peterson
Harvard University · USUniversity of Leeds · GB

Funding

Cellular Control of Microtubule-Based Transport: Unraveling its Molecular MechanDP2OD004268 · OD · HARVARD MEDICAL SCHOOL · PI RECK-PETERSON, SAMARA L · 2008 to 2008
$2.5M
NIH HHS 1 DP2 OD004268-01NIH HHS DP2 OD004268
6 · The paper itself

Abstract

The lissencephaly protein Lis1 has been reported to regulate the mechanical behavior of cytoplasmic dynein, the primary minus-end-directed microtubule motor. However, the regulatory mechanism remains poorly understood. Here, we address this issue using purified proteins from Saccharomyces cerevisiae and a combination of techniques, including single-molecule imaging and single-particle electron microscopy. We show that rather than binding to the main ATPase site within dynein's AAA+ ring or its microtubule-binding stalk directly, Lis1 engages the interface between these elements. Lis1 causes individual dynein motors to remain attached to microtubules for extended periods, even during cycles of ATP hydrolysis that would canonically induce detachment. Thus, Lis1 operates like a "clutch" that prevents dynein's ATPase domain from transmitting a detachment signal to its track-binding domain. We discuss how these findings provide a conserved mechanism for dynein functions in living cells that require prolonged microtubule attachments.

Indexed as

1-Alkyl-2-acetylglycerophosphocholine EsteraseAmino Acid SequenceAnimalsDyneinsHumansMicrotubule-Associated ProteinsMicrotubulesModels, MolecularMolecular Sequence DataProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins1-Alkyl-2-acetylglycerophosphocholine EsteraseDyneinsMicrotubule-Associated ProteinsNdl1 protein, S cerevisiaePAFAH1B1 protein, humanSaccharomyces cerevisiae Proteins

Identifiers

PMID22939623
PMCPMC3438448
OpenAlexW1994529490

What OpenQuestion holds

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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.