Evidence map›Paper›PMID 26149240›Full record

ArticleNature nanotechnology2015

Mechanical coordination in motor ensembles revealed using engineered artificial myosin filaments.

R F Hariadi, R F Sommese, A S Adhikari, R E Taylor, S Sutton, J A Spudich, S Sivaramakrishnan

Abstract read
In one paragraph

Article in Nature nanotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 72 citations in OpenAlex.

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  17. Patterning protein complexes on DNA nanostructures using a GFP nanobody.Protein science : a publication of the Protein Society · 2016
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

R F HariadiDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
R F SommeseDepartment of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
A S AdhikariDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA.
R E TaylorDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA.
S SuttonDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA.
J A SpudichDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA.
S Sivaramakrishnan1] Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA [2] Department of Biophysics, University of Michigan, Ann Arbor, Michigan 48109, USA [3] Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.
Stanford University · USUniversity of Michigan–Ann Arbor · US

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
Molecular Characterization of Cardiomyopathy Mutations in Human Cardiac MyosinR01HL117138 · NHLBI · UNIVERSITY OF COLORADO · PI LEINWAND, LESLIE ANNE, PERKINS, THOMAS TUPPER · 2013 to 2021
$4.2M
The kinase toolbox: Mapping the spatial and temporal regulation of cell signalingDP2CA186752 · NCI · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2013 to 2013
$2.3M
Probing molecular mechanisms of GPCR functional selectivity in live cellsR01GM105646 · NIGMS · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2014 to 2017
$1.1M
Biomechanical analysis of sarcomeric mutations that cause early-onset cardiomyopaF32HL123247 · NHLBI · STANFORD UNIVERSITY · PI TAYLOR, REBECCA E. · 2014 to 2016
$122k
NCI NIH HHS 1DP2 CA186752-01NCI NIH HHS DP2 CA186752NHLBI NIH HHS F32 HL123247NHLBI NIH HHS F32 HL123247-02NHLBI NIH HHS HL117138NHLBI NIH HHS R01 HL117138NIGMS NIH HHS 1-R01-GM-105646-01-A1NIGMS NIH HHS GM33289NIGMS NIH HHS R01 GM033289NIGMS NIH HHS R01 GM105646
6 · The paper itself

Abstract

The sarcomere of muscle is composed of tens of thousands of myosin motors that self-assemble into thick filaments and interact with surrounding actin-based thin filaments in a dense, near-crystalline hexagonal lattice. Together, these actin-myosin interactions enable large-scale movement and force generation, two primary attributes of muscle. Research on isolated fibres has provided considerable insight into the collective properties of muscle, but how actin-myosin interactions are coordinated in an ensemble remains poorly understood. Here, we show that artificial myosin filaments, engineered using a DNA nanotube scaffold, provide precise control over motor number, type and spacing. Using both dimeric myosin V- and myosin VI-labelled nanotubes, we find that neither myosin density nor spacing has a significant effect on the gliding speed of actin filaments. This observation supports a simple model of myosin ensembles as energy reservoirs that buffer individual stochastic events to bring about smooth, continuous motion. Furthermore, gliding speed increases with cross-bridge compliance, but is limited by Brownian effects. As a first step to reconstituting muscle motility, we demonstrate human β-cardiac myosin-driven gliding of actin filaments on DNA nanotubes.

Indexed as

Models, BiologicalActinsBioengineeringDNAHumansMovementMyosinsNanotechnologyNanotubesActinsDNAMyosins

Identifiers

PMID26149240
PMCPMC4799650
OpenAlexW2211695465

What OpenQuestion holds

Textmetadata
LicenceTDM
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.