Evidence map›Paper›PMID 26691840›Full record

ArticleJournal of proteomics2016

Intrinsic disorder and multiple phosphorylations constrain the evolution of the flightin N-terminal region.

Dominick Lemas, Panagiotis Lekkas, Bryan A Ballif, Jim O Vigoreaux

Abstract read
In one paragraph

Article in Journal of proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 25% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Molecular Characterization and Phylogenetic Analysis of Flightin Gene inAnimals : an open access journal from MDPI · 2024
    Article
  2. Structure of the Flight Muscle Thick Filament from the Bumble Bee,International journal of molecular sciences · 2022
    Article
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  8. Selection maintains signaling function of a highly diverged intrinsically disordered region.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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 1 institution in 1 country.

Dominick LemasDepartment of Biology, University of Vermont, Burlington, VT 05405, United States.
Panagiotis LekkasDepartment of Biology, University of Vermont, Burlington, VT 05405, United States.
Bryan A BallifDepartment of Biology, University of Vermont, Burlington, VT 05405, United States.
Jim O VigoreauxDepartment of Biology, University of Vermont, Burlington, VT 05405, United States. Electronic address: jvigorea@uvm.edu.
University of Vermont · US

Funding

Vermont INBRE Administrative Supplement 2024 AWD 118P20GM103449 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI CHRISTOPHER S FRANCKLYN · 2012 to 2026
$58.4M
NIGMS NIH HHS 20GM103449NIGMS NIH HHS P20 GM103449
6 · The paper itself

Abstract

Flightin is a myosin binding phosphoprotein that originated in the ancestor to Pancrustacea ~500 MYA. In Drosophila melanogaster, flightin is essential for length determination and flexural rigidity of thick filaments. Here, we show that among 12 Drosophila species, the N-terminal region is characterized by low sequence conservation, low pI, a cluster of phosphorylation sites, and a high propensity to intrinsic disorder (ID) that is augmented by phosphorylation. Using mass spectrometry, we identified eight phosphorylation sites within a 29 amino acid segment in the N-terminal region of D. melanogaster flightin. We show that phosphorylation of D. melanogaster flightin is modulated during flight and, through a comparative analysis to orthologs from other Drosophila species, we found phosphorylation sites that remain invariant, sites that retain the charge character, and sites that are clade-specific. While the number of predicted phosphorylation sites differs across species, we uncovered a conserved pattern that relates the number of phosphorylation sites to pI and ID. Extending the analysis to orthologs of other insects, we found additional conserved features in flightin despite the near absence of sequence identity. Collectively, our results demonstrate that structural constraints demarcate the evolution of the highly variable N-terminal region.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsFilaminsPhosphorylationProtein Structure, TertiaryDrosophila ProteinsFilaminsfln protein, Drosophila

Identifiers

PMID26691840
PMCPMC4762717
OpenAlexW2193919785

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.