Evidence map›Paper›PMID 18805920›Full record

ArticleBiophysical journal2008

Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics.

Chaoxing Yang, Seemanti Ramanath, William A Kronert, Sanford I Bernstein, David W Maughan, Douglas M Swank

Abstract read
In one paragraph

Article in Biophysical journal, 2008. 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
–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

22 citing papers in PubMed.

  1. Article
  2. Review
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  9. A new experimental model to study force depression: the Drosophila jump muscle.Journal of applied physiology (Bethesda, Md. : 1985) · 2014
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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

6 authors.

Chaoxing YangDepartment of Biology and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA.
Seemanti Ramanath
William A Kronert
Sanford I Bernstein
David W Maughan
Douglas M Swank

Funding

Genetics and Molecular Biology of Striated Muscle MyosinR01GM032443 · NIGMS · SAN DIEGO STATE UNIVERSITY · PI BERNSTEIN, SANFORD I · 1985 to 2016
$6.4M
Genetics and Molecular Biology of Striated Muscle MyosinR37GM032443 · NIGMS · SAN DIEGO STATE UNIVERSITY · PI Sanford I Bernstein · 2017 to 2026
$5.5M
Myosin structural and kinetic mechanisms that differentiate fast and slow muscle R01AR055611 · NIAMS · RENSSELAER POLYTECHNIC INSTITUTE · PI SWANK, DOUGLAS M · 2007 to 2012
$1.6M
Myosin-based kinetic differences between muscle typesR01AR049425 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MAUGHAN, DAVID WAYNE · 2003 to 2006
$1.1M
NIAMS NIH HHS AR049425NIAMS NIH HHS AR055611NIAMS NIH HHS R01 AR049425NIAMS NIH HHS R01 AR055611NIGMS NIH HHS GM32443NIGMS NIH HHS R01 GM032443NIGMS NIH HHS R37 GM032443
6 · The paper itself

Abstract

We measured the influence of alternative versions of the Drosophila melanogaster myosin heavy chain relay domain on muscle mechanical properties. We exchanged relay domain regions (encoded by alternative versions of exon 9) between an embryonic (EMB) isoform and the indirect flight muscle isoform (IFI) of myosin. Previously, we observed no effect of exchanging the EMB relay domain region into the flight muscle isoform (IFI-9b) on in vitro actin motility velocity or solution ATPase measurements compared to IFI. However, in indirect flight muscle fibers, IFI-9b exhibited decreased maximum power generation (P(max)) and optimal frequency of power generation (f(max)) to 70% and 83% of IFI fiber values. The decrease in muscle performance reduced the flight ability and wing-beat frequency of IFI-9b Drosophila compared to IFI Drosophila. Previously, we found that exchanging the flight muscle specific relay domain into the EMB isoform (EMB-9a) prevented actin movement in the in vitro motility assay compared to EMB, which does support actin movement. However, in indirect flight muscle fibers EMB-9a was a highly effective motor, increasing P(max) and f(max) 2.5-fold and 1.4-fold, respectively, compared to fibers expressing EMB. We propose that the oscillatory load EMB-9a experiences in the muscle fiber reduces a high activation energy barrier between two strongly bound states of the cross-bridge cycle, thereby promoting cross-bridge cycling. The IFI relay domain's enhanced sensitivity to load increases cross-bridge kinetics, whereas the EMB version is less load-sensitive.

Indexed as

ActomyosinAmino Acid SequenceAnimalsBiomechanical PhenomenaDrosophila melanogasterDrosophila ProteinsElastic ModulusFlight, AnimalKineticsMolecular Sequence DataMusclesMyofibrilsMyosin Heavy ChainsProtein IsoformsProtein Structure, TertiaryTransgenesActomyosinDrosophila ProteinsMyosin Heavy ChainsProtein Isoforms

Identifiers

PMID18805920
PMCPMC2586575

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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.