Evidence map›Paper›PMID 25185702›Full record

ArticleNature communications2014

Dynactin functions as both a dynamic tether and brake during dynein-driven motility.

Swathi Ayloo, Jacob E Lazarus, Aditya Dodda, Mariko Tokito, E Michael Ostap, Erika L F Holzbaur

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.5field-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

62 citing papers in PubMed, 98 citations in OpenAlex.

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2 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 at 2 institutions in 1 country.

Swathi Ayloo1] Department of Physiology and the Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA [2] Department of Biology Graduate Group, School of Arts and Sciences at the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA.
Jacob E LazarusDepartment of Physiology and the Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA.
Aditya DoddaDepartment of Chemical Engineering, University of Massachusetts, Amherst, Massachusetts 01008, USA.
Mariko TokitoDepartment of Physiology and the Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA.
E Michael OstapDepartment of Physiology and the Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA.
Erika L F HolzbaurDepartment of Physiology and the Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA.
University of Pennsylvania · USUniversity of Massachusetts Amherst · US

Funding

The Interaction of Cytoplasmic Dynein and DynactinR01GM048661 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOLZBAUR, ERIKA L · 1993 to 2017
$6.0M
Molecular function of myosin-IR01GM057247 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI OSTAP, E. MICHAEL · 1998 to 2014
$4.4M
NIGMS NIH HHS GM48661NIGMS NIH HHS R01 GM048661
6 · The paper itself

Abstract

Dynactin is an essential cofactor for most cellular functions of the microtubule motor cytoplasmic dynein, but the mechanism by which dynactin activates dynein remains unclear. Here we use single molecule approaches to investigate dynein regulation by the dynactin subunit p150(Glued). We investigate the formation and motility of a dynein-p150(Glued) co-complex using dual-colour total internal reflection fluorescence microscopy. p150(Glued) recruits and tethers dynein to the microtubule in a concentration-dependent manner. Single molecule imaging of motility in cell extracts demonstrates that the CAP-Gly domain of p150(Glued) decreases the detachment rate of the dynein-dynactin complex from the microtubule and also acts as a brake to slow the dynein motor. Consistent with this important role, two neurodegenerative disease-causing mutations in the CAP-Gly domain abrogate these functions in our assays. Together, these observations support a model in which dynactin enhances the initial recruitment of dynein onto microtubules and promotes the sustained engagement of dynein with its cytoskeletal track.

Indexed as

AnimalsBinding SitesCell MovementChlorocebus aethiopsCOS CellsDynactin ComplexDyneinsFemaleHumansMaleMiceMicrotubule-Associated ProteinsMicrotubulesProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsDCTN1 protein, humanDctn1 protein, mouseDynactin ComplexDyneinsMicrotubule-Associated ProteinsRecombinant Fusion ProteinsRNA, Small Interfering

Identifiers

PMID25185702
PMCPMC4470572
OpenAlexW2085969282

What OpenQuestion holds

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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.