Evidence map›Paper›PMID 19546158›Full record

ArticleMolecular biology and evolution2009

Protease gene duplication and proteolytic activity in Drosophila female reproductive tracts.

Erin S Kelleher, James E Pennington

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology and evolution, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

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  6. Proceedings. Biological sciences · 2022
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  15. Recurrent specialization on a toxic fruit in an island Drosophila population.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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

2 authors at 2 institutions in 1 country.

Erin S KelleherDepartment of Ecology and Evolutionary Biology, University of Arizona, USA. esk72@cornell.edu
James E Pennington
Cornell University · USUniversity of Arizona · US

Funding

REGULATION OF DIGESTION IN BLOOD-SUCKING INSECTSR01AI031951 · NIAID · UNIVERSITY OF ARIZONA · PI MIESFELD, ROGER L · 1992 to 2010
$3.0M
NIAID NIH HHS AI31951NIAID NIH HHS R01 AI031951
6 · The paper itself

Abstract

Secreted proteases play integral roles in sexual reproduction in a broad range of taxa. In the genetic model Drosophila melanogaster, these molecules are thought to process peptides and activate enzymes inside female reproductive tracts, mediating critical postmating responses. A recent study of female reproductive tract proteins in the cactophilic fruit fly Drosophila arizonae, identified pervasive, lineage-specific gene duplication amongst secreted proteases. Here, we compare the evolutionary dynamics, biochemical nature, and physiological significance of secreted female reproductive serine endoproteases between D. arizonae and its congener D. melanogaster. We show that D. arizonae lower female reproductive tract (LFRT) proteins are significantly enriched for recently duplicated secreted proteases, particularly serine endoproteases, relative to D. melanogaster. Isolated lumen from D. arizonae LFRTs, furthermore, exhibits significant trypsin-like and elastase-like serine endoprotease activity, whereas no such activity is seen in D. melanogaster. Finally, trypsin- and elastase-like activity in D. arizonae female reproductive tracts is negatively regulated by mating. We propose that the intense proteolytic environment of the D. arizonae female reproductive tract relates to the extraordinary reproductive physiology of this species and that ongoing gene duplication amongst these proteases is an evolutionary consequence of sexual conflict.

Indexed as

Gene DuplicationAnimalsDigestive SystemDrosophilaDrosophila melanogasterEvolution, MolecularFemaleGenitalia, FemalePancreatic ElastaseProtein Processing, Post-TranslationalReproductionSerine EndopeptidasesTrypsinPancreatic ElastaseSerine EndopeptidasesTrypsin

Identifiers

PMID19546158
PMCPMC2734159
OpenAlexW2110475110

What OpenQuestion holds

Textmetadata
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.