Evidence map›Paper›PMID 19393244›Full record

ArticleJournal of molecular biology2009

Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head.

Marieke J Bloemink, Corey M Dambacher, Aileen F Knowles, Girish C Melkani, Michael A Geeves, Sanford I Bernstein

Abstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Alternative N-terminal regions ofThe Journal of biological chemistry · 2020
    Article
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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.

Marieke J BloeminkDepartment of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
Corey M Dambacher
Aileen F Knowles
Girish C Melkani
Michael A Geeves
Sanford I Bernstein

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
NMR STUDIES OF ACYL-CARRIER PROTEINR01GM032243 · NIGMS · YALE UNIVERSITY · PI PRESTEGARD, JAMES H · 1985 to 1994
–
NIGMS NIH HHS GM32243NIGMS NIH HHS R01 GM032443NIGMS NIH HHS R37 GM032443Wellcome Trust 070021Wellcome Trust 085309
6 · The paper itself

Abstract

We investigated the biochemical and biophysical properties of one of the four alternative regions within the Drosophila myosin catalytic domain: the relay domain encoded by exon 9. This domain of the myosin head transmits conformational changes in the nucleotide-binding pocket to the converter domain, which is crucial to coupling catalytic activity with mechanical movement of the lever arm. To study the function of this region, we used chimeric myosins (IFI-9b and EMB-9a), which were generated by exchange of the exon 9-encoded domains between the native embryonic body wall (EMB) and indirect flight muscle isoforms (IFI). Kinetic measurements show that exchange of the exon 9-encoded region alters the kinetic properties of the myosin S1 head. This is reflected in reduced values for ATP-induced actomyosin dissociation rate constant (K(1)k(+2)) and ADP affinity (K(AD)), measured for the chimeric constructs IFI-9b and EMB-9a, compared to wild-type IFI and EMB values. Homology models indicate that, in addition to affecting the communication pathway between the nucleotide-binding pocket and the converter domain, exchange of the relay domains between IFI and EMB affects the communication pathway between the nucleotide-binding pocket and the actin-binding site in the lower 50-kDa domain (loop 2). These results suggest an important role of the relay domain in the regulation of actomyosin cross-bridge kinetics.

Indexed as

Drosophila ProteinsExonsMyosinsProtein IsoformsActomyosinAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceAnimalsDrosophila melanogasterFlight, AnimalHumansModels, MolecularMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsActomyosinAdenosine DiphosphateAdenosine TriphosphateDrosophila ProteinsMyosinsProtein IsoformsRecombinant Fusion Proteins

Identifiers

PMID19393244
PMCPMC3119900

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Registered trials

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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.