Evidence map›Paper›PMID 25272277›Full record

ArticleeLife2014

A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region.

Courtney M Schroeder, Jonathan M L Ostrem, Nicholas T Hertz, Ronald D Vale

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

56 citing papers in PubMed, 93 citations in OpenAlex.

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  13. MAPping tubulin mutations.Frontiers in cell and developmental biology · 2023
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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

4 authors at 2 institutions in 1 country.

Courtney M SchroederDepartment of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.
Jonathan M L OstremDepartment of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.
Nicholas T HertzDepartment of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.
Ronald D ValeDepartment of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, United States.
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

Immune Responses to Vibrio cholerae infection and vaccination in HaitiR01AI099243 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI HARRIS, JASON B, IVERS, LOUISE C. · 2012 to 2022
$7.9M
RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
Microtubule Complexes Involved in Intracelluar TransportR37GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2006 to 2015
$3.2M
Structure and mechanism of the dynein motorR01GM097312 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VALE, RONALD D · 2011 to 2016
$1.5M
MICROTUBULE-BASED ORGANELLE TRANSPORTR01GM038499 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI VALE, RONALD D · 1988 to 2005
$1.2M
Howard Hughes Medical InstituteNIAID NIH HHS 5R01AI099243NIAID NIH HHS R01 AI099243NIGMS NIH HHS R01 GM038499NIGMS NIH HHS R01 GM097312NIGMS NIH HHS R01GM097312NIGMS NIH HHS R37 GM038499NIGMS NIH HHS R37GM038499NIGMS NIH HHS T32 GM064337
6 · The paper itself

Abstract

Cytoplasmic dynein, a microtubule-based motor protein, transports many intracellular cargos by means of its light intermediate chain (LIC). In this study, we have determined the crystal structure of the conserved LIC domain, which binds the motor heavy chain, from a thermophilic fungus. We show that the LIC has a Ras-like fold with insertions that distinguish it from Ras and other previously described G proteins. Despite having a G protein fold, the fungal LIC has lost its ability to bind nucleotide, while the human LIC1 binds GDP preferentially over GTP. We show that the LIC G domain binds the dynein heavy chain using a conserved patch of aromatic residues, whereas the less conserved C-terminal domain binds several Rab effectors involved in membrane transport. These studies provide the first structural information and insight into the evolutionary origin of the LIC as well as revealing how this critical subunit connects the dynein motor to cargo.

Indexed as

Amino Acid SequenceAnimalsBinding SitesConserved SequenceCrystallography, X-RayCytoplasmic DyneinsHEK293 CellsHumansModels, MolecularMolecular Sequence DataNucleotidesProtein BindingProtein Structure, SecondaryProtein Structure, Tertiaryrab GTP-Binding Proteinsras ProteinsCytoplasmic DyneinsDYNC1H1 protein, humanDYNC1LI1 protein, humanNucleotidesrab GTP-Binding Proteinsras Proteinsbiochemistrybiophysicsdynein subunitE. coliG proteinhumanintracellular motilitymolecular motorRab effectorsstructural biology

Identifiers

PMID25272277
PMCPMC4359372
OpenAlexW1973068928

What OpenQuestion holds

Textmetadata
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.