Evidence map›Paper›PMID 29515126›Full record

ArticleNature communications2018

A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity.

In-Gyun Lee, Mara A Olenick, Malgorzata Boczkowska, Clara Franzini-Armstrong, Erika L F Holzbaur, Roberto Dominguez

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing 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

74 citing papers in PubMed.

  1. Article
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  6. AnbioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
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  10. Occludin acts as a dynein adaptor regulating permeability and collateral angiogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
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  20. Article

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

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.

In-Gyun LeeDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Mara A OlenickDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Malgorzata BoczkowskaDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Clara Franzini-ArmstrongDepartment of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Erika L F HolzbaurDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA. droberto@pennmedicine.upenn.edu.

Funding

Role of Myosin-l in Membrane Dynamics and TransportP01GM087253 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 2009 to 2018
$15.3M
Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
Molecular Mechanisms of Axonal Transport and Organelle DynamicsR35GM126950 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Erika L Holzbaur · 2018 to 2026
$5.6M
NIGMS NIH HHS P01 GM087253NIGMS NIH HHS R01 GM073791NIGMS NIH HHS R35 GM126950
6 · The paper itself

Abstract

Cytoplasmic dynein is the major minus-end-directed microtubule-based motor in cells. Dynein processivity and cargo selectivity depend on cargo-specific effectors that, while generally unrelated, share the ability to interact with dynein and dynactin to form processive dynein-dynactin-effector complexes. How this is achieved is poorly understood. Here, we identify a conserved region of the dynein Light Intermediate Chain 1 (LIC1) that mediates interactions with unrelated dynein-dynactin effectors. Quantitative binding studies map these interactions to a conserved helix within LIC1 and to N-terminal fragments of Hook1, Hook3, BICD2, and Spindly. A structure of the LIC1 helix bound to the N-terminal Hook domain reveals a conformational change that creates a hydrophobic cleft for binding of the LIC1 helix. The LIC1 helix competitively inhibits processive dynein-dynactin-effector motility in vitro, whereas structure-inspired mutations in this helix impair lysosomal positioning in cells. The results reveal a conserved mechanism of effector interaction with dynein-dynactin necessary for processive motility.

Indexed as

Amino Acid SequenceCytoplasmic DyneinsDynactin ComplexHeLa CellsHumansMovementProtein ConformationCytoplasmic DyneinsDynactin ComplexDYNC1LI1 protein, human

Identifiers

PMID29515126
PMCPMC5841405

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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.