Evidence map›Paper›PMID 33173051›Full record

ArticleNature communications2020

A tunable LIC1-adaptor interaction modulates dynein activity in a cargo-specific manner.

In-Gyun Lee, Sydney E Cason, Saif S Alqassim, Erika L F Holzbaur, Roberto Dominguez

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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  9. Dynein upsizes under load.Nature cell biology · 2026
    Article
  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
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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

5 authors at 3 institutions in 3 countries.

In-Gyun LeeDepartment of Physiology and Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Sydney E CasonDepartment of Physiology and Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Saif S AlqassimDepartment of Physiology and Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.ORCID 0000-0002-1726-1587
Erika L F HolzbaurDepartment of Physiology and Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.ORCID 0000-0001-5389-4114
Roberto DominguezDepartment of Physiology and Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA. droberto@pennmedicine.upenn.edu.ORCID 0000-0003-3186-5229
University of Pennsylvania · USKorea Institute of Science and Technology · KRMohammed Bin Rashid University of Medicine and Health Sciences · AE

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Integrative mechanisms of organelle dynamics from the atomic-to-cellular levelRM1GM136511 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO, HOLZBAUR, ERIKA L · 2020 to 2024
$7.4M
Molecular Mechanisms of Axonal Transport and Organelle DynamicsR35GM126950 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Erika L Holzbaur · 2018 to 2026
$5.6M
NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R35 GM126950NIGMS NIH HHS RM1 GM136511
6 · The paper itself

Abstract

Cytoplasmic dynein-1 (dynein) is the motor responsible for most retrograde transport of cargoes along microtubules in eukaryotic cells, including organelles, mRNA and viruses. Cargo selectivity and activation of processive motility depend on a group of so-called "activating adaptors" that link dynein to its general cofactor, dynactin, and cargoes. The mechanism by which these adaptors regulate dynein transport is poorly understood. Here, based on crystal structures, quantitative binding studies, and in vitro motility assays, we show that BICD2, CRACR2a, and HOOK3, representing three subfamilies of unrelated adaptors, interact with the same amphipathic helix of the dynein light intermediate chain-1 (LIC1). While the hydrophobic character of the interaction is conserved, the three adaptor subfamilies use different folds (coiled-coil, EF-hand, HOOK domain) and different surface contacts to bind the LIC1 helix with affinities ranging from 1.5 to 15.0 μM. We propose that a tunable LIC1-adaptor interaction modulates dynein's motility in a cargo-specific manner.

Indexed as

AnimalsBiological TransportCalcium-Binding ProteinsCarrier ProteinsCell MovementCrystallography, X-RayCytoplasmic DyneinsDynactin ComplexHumansMicrotubule-Associated ProteinsMolecular Motor ProteinsProtein BindingBICD2 protein, humanCalcium-Binding ProteinsCarrier ProteinsCRACR2A protein, humanCytoplasmic DyneinsDynactin Complexhook3 protein, humanMicrotubule-Associated ProteinsMolecular Motor Proteins

Identifiers

PMID33173051
PMCPMC7655957
OpenAlexW3105634631

What OpenQuestion holds

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LicenceCC BY
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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.