Evidence map›Paper›PMID 23765379›Full record

ArticleMolecular biology and evolution2013

The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling.

Paula Ramos-Silva, Jaap Kaandorp, Lotte Huisman, Benjamin Marie, Isabelle Zanella-Cléon, Nathalie Guichard, David J Miller, Frédéric Marin

Open access · bronzeAbstract read
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Article in Molecular biology and evolution, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
15.4field-weighted citation impact, top 1% 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

86 citing papers in PubMed, 206 citations in OpenAlex.

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26 more citing papers are in PubMed but not listed here.

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

8 authors at 6 institutions in 3 countries.

Paula Ramos-SilvaUMR 6282 CNRS, Biogéosciences, Université de Bourgogne, Dijon, France.
Jaap Kaandorp
Lotte Huisman
Benjamin Marie
Isabelle Zanella-Cléon
Nathalie Guichard
David J Miller
Frédéric Marin
Biogéosciences · FRVrije Universiteit Amsterdam · NLARC Centre of Excellence for Coral Reef Studies · AUMuséum national d'Histoire naturelle · FRUniversité Claude Bernard Lyon 1 · FRUniversité de Bourgogne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In corals, biocalcification is a major function that may be drastically affected by ocean acidification (OA). Scleractinian corals grow by building up aragonitic exoskeletons that provide support and protection for soft tissues. Although this process has been extensively studied, the molecular basis of biocalcification is poorly understood. Notably lacking is a comprehensive catalog of the skeleton-occluded proteins-the skeletal organic matrix proteins (SOMPs) that are thought to regulate the mineral deposition. Using a combination of proteomics and transcriptomics, we report the first survey of such proteins in the staghorn coral Acropora millepora. The organic matrix (OM) extracted from the coral skeleton was analyzed by mass spectrometry and bioinformatics, enabling the identification of 36 SOMPs. These results provide novel insights into the molecular basis of coral calcification and the macroevolution of metazoan calcifying systems, whereas establishing a platform for studying the impact of OA at molecular level. Besides secreted proteins, extracellular regions of transmembrane proteins are also present, suggesting a close control of aragonite deposition by the calicoblastic epithelium. In addition to the expected SOMPs (Asp/Glu-rich, galaxins), the skeletal repertoire included several proteins containing known extracellular matrix domains. From an evolutionary perspective, the number of coral-specific proteins is low, many SOMPs having counterparts in the noncalcifying cnidarians. Extending the comparison with the skeletal OM proteomes of other metazoans allowed the identification of a pool of functional domains shared between phyla. These data suggest that co-option and domain shuffling may be general mechanisms by which the trait of calcification has evolved.

Indexed as

Evolution, MolecularPhylogenyAmino Acid SequenceAnimalsAnthozoaCalcification, PhysiologicCalcium CarbonateExtracellular MatrixMass SpectrometryMolecular Sequence AnnotationMolecular Sequence DataProtein Structure, TertiaryProteomeSequence AlignmentSequence Homology, Amino AcidCalcium CarbonateProteomebiomineralizationcalcium carbonate skeletonevolutionproteomicsscleractinian

Identifiers

PMID23765379
PMCPMC3748352
OpenAlexW2156326351

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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.